An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.

Common name: GDP-L-fucose synthase

Reaction: GDP-L-fucose + NAD⁺ = GDP-4-dehydro-6-deoxy-D-mannose + NADH + H⁺

For diagram click here.

Other name(s): GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase

Systematic name: GDP-L-fucose:NAD⁺ 4-oxidoreductase (3,5-epimerizing)

References:

1. Chang, S., Duerr, B. and Serif, G. An epimerase-reductase in L-fucose synthesis. J. Biol. Chem. 263 (1988) 1693-1697. [PMID: 3338988]

2. Mattila, P., Räbinä, J, Hortling, S., Jelin, J. and Renkonen, R. Functional expression of Escherichia coli enzymes synthesizing GDP-L-fucose from inherent GDP-D-mannose in Saccharomyces cerevisiae. Glycobiology 10 (2000) 1041-1047. [PMID: 11030750]

EC 1.1.1.272

Common name: (R)-2-hydroxyacid dehydrogenase

Reaction: (S)-3-sulfolactate + NAD(P)⁺ = 3-sulfopyruvate + NAD(P)H + H⁺

Other name(s): (R)-sulfolactate:NAD(P)⁺ oxidoreductase; L-sulfolactate dehydrogenase

Systematic name: (R)-2-hydroxyacid:NAD(P)⁺ oxidoreductase

Comments: This dehydrogenase acts on (R)-lactate and other 2-hydroxycarboxylic acids with this configuration.

References:

1. Graupner, M., Xu, H. and White, R.H. Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing reactions involved in coenzyme biosynthesis in methanoarchaea. J. Bacteriol. 182 (2000) 3688-3692. [PMID: 10850983]

2. Graupner, M. and White, R.H. The first examples of (S)-2-hydroxyacid dehydrogenases catalyzing the transfer of the pro-4S hydrogen of NADH are found in the archaea. Biochim. Biophys. Acta 1548 (2001) 169-173. [PMID: 11451450]

EC 1.4.99.5

Common name: glycine dehydrogenase (cyanide-forming)

Reaction: glycine + 2 A = HCN + CO₂ + 2 AH₂

For diagram click here.

Other name(s): hydrogen cyanide synthase; HCN synthase

Systematic name: glycine:acceptor oxidoreductase (hydrogen-cyanide-forming)

Comments: The enzyme from Pseudomonas sp. contains FAD. The enzyme is membrane-bound, and the 2-electron acceptor is a component of the respiratory chain. The enzyme can act with various artificial electron acceptors, including phenazine methosulfate.

References:

1. Wissing, F. Cyanide production from glycine by a homogenate from a Pseudomonas species. J. Bacteriol. 121 (1975) 695-699. [PMID: 234422]

2. Castric, P.A. Glycine metabolism by Pseudomonas aeruginosa: Hydrogen cyanide biosynthesis. J. Bacteriol. 130 (1977) 826-831. [PMID: 233722]

3. Laville, J., Blumer, C., Von Schroetter, C., Gaia, V., Defago, G., Keel, C. and Haas, D. Characterization of the hcnABC gene cluster encoding hydrogen cyanide synthase and anaerobic regulation by ANR in the strictly aerobic biocontrol agent Pseudomonas fluorescens CHA0. J. Bacteriol. 180 (1998) 3187-3196. [PMID: 9620970]

4. Blumer, C. and Haas, D. Mechanism, regulation, and ecological role of bacterial cyanide biosynthesis. Arch. Microbiol. 173 (2000) 170-177. [PMID: 10763748]

*EC 1.13.99.1

Common name: inositol oxygenase

Reaction: myo-inositol + O₂ = D-glucuronate + H₂O

For diagram click here.

Other name(s): meso-inositol oxygenase; myo-inositol oxygenase; MOO

Systematic name: myo-inositol:oxygen oxidoreductase

Comments: An iron protein. Formerly EC 1.13.1.11 and 1.99.2.6.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9029-59-8

References:

1. Charalampous, F.C. Biochemical studies on inositol. V. Purification and properties of the enzyme that cleaves inositol to D-glucuronic acid. J. Biol. Chem. 234 (1959) 220-227.

2. Reddy, C.C., Swan, J.S. and Hamilton, G.A. myo-Inositol oxygenase from hog kidney. I. Purification and characterization of the oxygenase and of an enzyme complex containing the oxygenase and D-glucuronate reductase. J. Biol. Chem. 256 (1981) 8510-8518. [PMID: 7263666]

3. Arner, R.J., Prabhu, K.S., Thompson, J.T., Hildenbrandt, G.R., Liken, A.D. and Reddy, C.C. myo-Inositol oxygenase: molecular cloning and expression of a unique enzyme that oxidizes myo-inositol and D-chiro-inositol. Biochem. J. 360 (2001) 313-320. [PMID: 11716759]

*EC 2.1.1.39

Common name: inositol 3-methyltransferase

Reaction: S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-3-O-methyl-myo-inositol

For diagram click here.

Other name(s): inositol L-1-methyltransferase; myo-inositol 1-methyltransferase; S-adenosylmethionine:myo-inositol 1-methyltransferase; myo-inositol 1-O-methyltransferase (name based on 1L-numbering system and not 1D-numbering); S-adenosyl-L-methionine:myo-inositol 1-O-methyltransferase

Systematic name: S-adenosyl-L-methionine:1D-myo-inositol 3-O-methyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37257-05-9

References:

1. Hofmann, H., Wagner, I. and Hoffmann-Ostenhof, O. Untersuchungen über die Biosynthese der Cyclite. XXIV. Über ein lösliches Enzym aus Vinca rosea, das myo-Inosit zu L-Bornesit methyliert. Hoppe-Seyler's Z. Physiol. Chem. 350 (1969) 1465-1468. [PMID: 5362621]

*EC 2.1.1.40

Common name: inositol 1-methyltransferase

Reaction: S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-1-O-methyl-myo-inositol

For diagram click here.

Other name(s): inositol D-1-methyltransferase; S-adenosylmethionine:myo-inositol 3-methyltransferase; myo-inositol 3-O-methyltransferase; inositol 3-O-methyltransferase (name based on 1L-numbering system and not 1D-numbering); S-adenosyl-L-methionine:myo-inositol 3-O-methyltransferase

Systematic name: S-adenosyl-L-methionine:1D-myo-inositol 1-O-methyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37257-06-0

References:

1 .Wagner, I., Hofmann, H. and Hoffmann-Ostenhof, O. Untersuchungen über die Biosynthese der Cyclite. XXIII. Über ein lösliches Enzym aus Erbsenkeimlingen, das myo-Inosit zu D-Bornesit methyliert. Hoppe-Seyler's Z. Physiol. Chem. 350 (1969) 1460-1464. [PMID: 5362620]

*EC 2.1.1.129

Common name: inositol 4-methyltransferase

Reaction: S-adenosyl-L-methionine + myo-inositol = S-adenosyl-L-homocysteine + 1D-4-O-methyl-myo-inositol

For diagram click here.

Other name(s): myo-inositol 4-O-methyltransferase; S-adenosyl-L-methionine:myo-inositol 4-O-methyltransferase; myo-inositol 6-O-methyltransferase

Systematic name: S-adenosyl-L-methionine:1D-myo-inositol 4-methyltransferase

Comments: The enzyme from the rice bean Vigna umbellata (Fabaceae) is highly specific for S-adenosyl-L-methionine. The enzyme also methylates 1L-1,2,4/3,5-cyclohexanepentol, 2,4,6/3,5-pentahydroxycyclohexanone, D,L-2,3,4,6/5-pentacyclohexanone and 2,2'-anhydro-2-C-hydroxymethyl-myo-inositol, but at lower rates than that of myo-inositol.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 146048-86-4; 169277-48-9 (from EC 2.1.1.134)

References:

1. Vernon, D.M., Bohnert, H.J. A novel methyl transferase induced by osmotic stress in the facultative halophyte Mesembryanthemum crystallinum. EMBO J. 11 (1992) 2077-2085. [PMID: 1600940]

2. Wanek, W. and Richter, A. Purification and characterization of myo-inositol 6-O-methyltransferase from Vigna umbellata Ohwi et Ohashi. Planta 197 (1995) 427-434.

[EC 2.1.1.134 Deleted entry: myo-inositol 6-O-methyltransferase. Now included with EC 2.1.1.129, inositol 4-methyltransferase (EC 2.1.1.134 created 1999, deleted 2002)]

*EC 2.3.1.4

Common name: glucosamine 6-phosphate N-acetyltransferase

Reaction: acetyl-CoA + D-glucosamine 6-phosphate = CoA + N-acetyl-D-glucosamine 6-phosphate

For diagram click here.

Other name(s): phosphoglucosamine transacetylase; phosphoglucosamine acetylase; glucosamine-6-phosphate acetylase; D-glucosamine-6-P N-acetyltransferase; aminodeoxyglucosephosphate acetyltransferase; glucosamine 6-phosphate acetylase; glucosamine 6-phosphate N-acetyltransferase; N-acetylglucosamine-6-phosphate synthase; phosphoglucosamine N-acetylase; glucosamine-phosphate N-acetyltransferase

Systematic name: acetyl-CoA:D-glucosamine-6-phosphate N-acetyltransferase

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9031-91-8

References:

1. Davidson, E.A. Glucosamine 6-phosphate N-acetylase. Methods Enzymol. 9 (1966) 704-707.

2. Davidson, E.A., Blumenthal, H.J. and Roseman, F. Glucosamine metabolism. II. Studies of glucosamine 6-phosphate N-acetylase. J. Biol. Chem. 226 (1957) 125-133.

3. Pattabiraman, T.N. and Bachhawat, B.K. Purification of glucosamine-6-phosphate N-acetylase from sheep brain. Biochim. Biophys. Acta 59 (1962) 681-689.

4. Boehmelt, G., Fialka, I., Brothers, G., McGinley, M.D., Patterson, S.D., Mo, R., Hui, C.C., Chung, S., Huber, L.A., Mak, T.W. and Iscove, N.N. Cloning and characterization of the murine glucosamine-6-phosphate acetyltransferase EMeg32. Differential expression and intracellular membrane association. J. Biol. Chem. 275 (2000) 12821-12832. [PMID: 10777580]

*EC 2.3.1.106

Common name: tartronate O-hydroxycinnamoyltransferase

Reaction: sinapoyl-CoA + 2-hydroxymalonate = CoA + sinapoyltartronate

For diagram click here.

Glossary:
sinapic acid = 4-hydroxy-3,5-dimethoxycinnamic acid
tartonic acid = 2-hydroxymalonic acid

Other name(s): tartronate sinapoyltransferase; hydroxycinnamoyl-coenzyme-A:tartronate hydroxycinnamoyltransferase

Systematic name: sinapoyl-CoA:2-hydroxymalonate O-(hydroxycinnamoyl)transferase

Comments: 4-Coumaroyl-CoA (4-hydroxycinnamoyl-CoA), caffeoyl-CoA (3,4-dihydroxycinnamoyl-CoA) and feruloyl-CoA (4-hydroxy-3-methoxycinnamoyl-CoA) can also act as donors for the enzyme from the mung bean (Vigna radiata).

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 102484-57-1

References:

1. Strack, D., Ruhoff, R. and Gräwe, W. Hydroxycinnamoyl-Coenzyme-A-tartronate hydroxycinnamoyltransferase in protein preparations from mung bean. Phytochemistry 25 (1986) 833-837.

*EC 2.4.1.65

Common name: 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase

Reaction: GDP-β-L-fucose + β-D-galactosyl-(13)-N-acetyl-D-glucosaminyl-R = GDP + β-D-galactosyl-(13)-[α-L-fucosyl-(14)]-N-acetyl-D-glucosaminyl-R

For diagram click here.

Other name(s): blood group Lewis α-4-fucosyltransferase; guanosine diphosphofucose-β-acetylglucosaminylsaccharide 4-α-L-fucosyltransferase; α(1,3/1,4) fucosyltransferase III; α-(14)-L-fucosyltransferase; α-4-L-fucosyltransferase; β-acetylglucosaminylsaccharide fucosyltransferase; blood-group substance Le^a-dependent fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-fucosyltransferase; guanosine diphosphofucose-glycoprotein 4-α-L-fucosyltransferase; Lewis blood group α-(13/4)-fucosyltransferase; Lewis α-(13/4)-fucosyltransferase; FucT-II; (Le^a)-dependent (α-3/4)-fucosyltransferase; Lewis α-(13/4)-fucosyltransferase; Lewis(Le) blood group gene-dependent α-(13/4)-L-fucosyltransferase; 3-α-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase; GDP-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4^I-α-L-fucosyltransferase

Systematic name: GDP-β-L-fucose:3-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 4^I-α-L-fucosyltransferase

Comments: This enzyme is the product of the Lewis blood group gene. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. Although it is a 4-fucosyltransferase, it has a persistent 3-fucosyltransferase activity towards the glucose residue in free lactose. This enzyme fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3, unlike EC 2.4.1.154, 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase, which fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37277-69-3

References:

1. Prieels, J.-P., Monnom, D., Dolmans, M., Beyer, T.A. and Hill, R.L. Co-purification of the Lewis blood group N-acetylglucosaminide α14 fucosyltransferase and an N-acetylglucosaminide α13 fucosyltransferase from human milk. J. Biol. Chem. 256 (1981) 10456-10463. [PMID: 7287719]

*EC 2.4.1.69

Common name: galactoside 2-α-L-fucosyltransferase

Reaction: GDP-β-L-fucose + β-D-galactosyl-R = GDP + α-L-fucosyl-1,2-β-D-galactosyl-R

Other name(s): blood group H α-2-fucosyltransferase; guanosine diphosphofucose-galactoside 2-L-fucosyltransferase; α-(12)-L-fucosyltransferase; α-2-fucosyltransferase; α-2-L-fucosyltransferase; blood-group substance H-dependent fucosyltransferase; guanosine diphosphofucose-glycoprotein 2-α-fucosyltransferase; guanosine diphosphofucose-lactose fucosyltransferase; GDP fucose-lactose fucosyltransferase; guanosine diphospho-L-fucose-lactose fucosyltransferase; guanosine diphosphofucose-β-D-galactosyl-α-2-L-fucosyltransferase; guanosine diphosphofucose-galactosylacetylglucosaminylgalactosylglucosylceramide α-L-fucosyltransferase; guanosine diphosphofucose-glycoprotein 2-α-L-fucosyltransferase; H-gene-encoded β-galactoside α12fucosyltransferase; secretor-type β-galactoside α12fucosyltransferase; β-galactoside α12fucosyltransferase; GDP-L-fucose:lactose fucosyltransferase

Systematic name: GDP-β-L-fucose:β-D-galactosyl-R 2-α-L-fucosyltransferase

Comments: Free lactose can act as acceptor. Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. The action on glycolipid was previously listed as EC 2.4.1.89.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 56093-23-3

References:

1. Basu, S., Basu, M. and Chien, J.L. Enzymatic synthesis of a blood group H-related glycosphingolipid by an α-fucosyltransferase from bovine spleen. J. Biol. Chem. 250 (1975) 2956-2962. [PMID: 804484]

2. Beyer, T.A. and Hill, R.L. Enzymatic properties of the β-galactoside α 1 leads to 2 fucosyltransferase from porcine submaxillary gland. J. Biol. Chem. 255 (1980) 5373-5379. [PMID: 7372640]

3. Beyer, T.A., Sadler, J.E. and Hill, R.L. Purification to homogeneity of H blood group β-galactoside α 1 leads to 2 fucosyltransferase from porcine submaxillary gland. J. Biol. Chem. 255 (1980) 5364-5372. [PMID: 6246105]

4. Grollman, A.P. GDP-L-fucose:lactose fucosyltransferase from mammary gland. Methods Enzymol. 8 (1966) 351-353.

*EC 2.4.1.152

Common name: 4-galactosyl-N-acetylglucosaminide 3-α-L-fucosyltransferase

Reaction: GDP-β-L-fucose + 1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R = GDP + 1,4-β-D-galactosyl-(α-1,3-L-fucosyl)-N-acetyl-D-glucosaminyl-R

For diagram click here.

Other name(s): Lewis-negative α-3-fucosyltransferase; plasma α-3-fucosyltransferase; guanosine diphosphofucose-glucoside α13-fucosyltransferase; galactoside 3-fucosyltransferase; GDP-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase

Systematic name: GDP-β-L-fucose:1,4-β-D-galactosyl-N-acetyl-D-glucosaminyl-R 3-L-fucosyltransferase

Comments: Normally acts on a glycoconjugate where R (see reaction) is a glycoprotein or glycolipid. This enzyme fucosylates on O-3 of an N-acetylglucosamine that carries a galactosyl group on O-4, unlike EC 2.4.1.65, 3-galactosyl-N-acetylglucosaminide 4-α-L-fucosyltransferase, which fucosylates on O-4 of an N-acetylglucosamine that carries a galactosyl group on O-3.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 111310-38-4

References:

1. Johnson, P.H., Yates, A.D. and Watkins, W.M. Human salivary fucosyltransferase: evidence for two distinct α-3-L-fucosyltransferase activities one of which is associated with the Lewis blood Le gene. Biochem. Biophys. Res. Commun. 100 (1981) 1611-1618.

2. Schachter, H., Narasimhan, S., Gleeson, P. and Vella, G. Glycosyltransferases involved in elongation of N-glycosidically linked oligosaccharides of the complex or N-acetyllactosamine type. Methods Enzymol. 98 (1983) 98-134. [Medline UI: 6366476]

EC 2.4.1.217

Common name: mannosyl-3-phosphoglycerate synthase

Reaction: GDPmannose + 3-phospho-D-glycerate = GDP + 2-(α-D-mannosyl)-3-phosphoglycerate

Other name(s): MPG synthase

Systematic name: GDPmannose:3-phosphoglycerate 3-α-D-mannosyltransferase

Comments: Requires Mg²⁺. The enzyme is absolutely specific for GDPmannose and 3-phosphoglycerate, and transfers the mannosyl group with retention of configuration. In the hyperthermophilic archaeon Pyrococcus horikoshii, the mannosyl-3-phosphoglycerate formed is subsequently dephosphorylated by a specific phosphatase, EC 3.1.3.70 (mannosyl-3-phosphoglycerate phosphatase), producing mannosylglycerate.

References:

1. Empadinhas, N., Marugg, J.D., Borges, N., Santos, H. and da Costa, M.S. Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key-enzymes. J. Biol. Chem. 276 (2001) 43580-43588. [PMID: 11562374]

EC 2.4.1.218

Common name: hydroquinone glucosyltransferase

Reaction: UDPglucose + hydroquinone = UDP + hydroquinone-O-β-D-glucopyranoside

Other name(s): arbutin synthase; hydroquinone:O-glucosyltransferase

Systematic name: UDPglucose:hydroquinone-O-β-D-glucosyltransferase

Comments: Hydroquinone is the most effective acceptor, but over 40 phenolic compounds are also glucosylated, but at lower rates.

References:

1. Arend, J., Warzecha, H. and Stöckigt, J. Hydroquinone:O-glucosyltransferase from cultivated Rauvolfia cells: enrichment and partial amino acid sequences. Phytochemistry 53 (2000) 187-193. [PMID: 10680170]

2. Arend, J., Warzecha, H., Hefner, T. and Stöckigt, J. Utilizing genetically engineered bacteria to produce plant specific glucosides. Biotechnol. Bioeng. 76 (2001) 126-131. [PMID: 11505382]

*EC 2.7.1.67

Common name: 1-phosphatidylinositol 4-kinase

Reaction: ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 4-phosphate

For diagram click here.

Other name(s): phosphatidylinositol kinase (phosphorylating); phosphatidylinositol 4-kinase; phosphatidylinositol kinase; type II phosphatidylinositol kinase; PI kinase; PI 4-kinase

Systematic name: ATP:1-phosphatidyl-1D-myo-inositol 4-phosphotransferase

Comments: This reaction is catalysed by at least two different isoforms.

Links to other databases: BRENDA, EXPASY, GTD, KEGG, WIT, CAS registry number: 37205-54-2

References:

1. Colodzin, M. and Kennedy, E.P. Biosynthesis of diphosphoinositide in brain. J. Biol. Chem. 240 (1965) 3771-3780. [PMID: 4284712]

2. Kai, M., White, G.L. and Hawthorne, J.N. The phosphatidylinositol kinase of rat brain. Biochem. J. 101 (1966) 328-337. [PMID: 4290722]

3. Walker, D.H., Dougherty, N. and Pike, L.J. Purification and characterization of a phosphatidylinositol kinase from A431 cells. Biochemistry 27 (1988) 6504-6511. [PMID: 2851325]

4. Whitman, M., Downes, C.P., Keeler, M., Keller, T. and Cantley, L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332 (1988) 644-646. [PMID: 2833705]

5. Barylko, B., Gerber, S.H., Binns, D.D., Grichine, N., Khvotchev, M., Sudhof, T.C. and Albanesi, J.P. A novel family of phosphatidylinositol 4-kinases conserved from yeast to humans. J. Biol. Chem. 276 (2001) 7705-7708. [PMID: 11244087]

*EC 2.7.1.68

Common name: 1-phosphatidylinositol-4-phosphate 5-kinase

Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate

For diagram click here.

Other name(s): diphosphoinositide kinase; PIP kinase; phosphatidylinositol 4-phosphate kinase; phosphatidylinositol-4-phosphate 5-kinase; type I PIP kinase

Systematic name: ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 5-phosphotransferase

Comments: This enzyme can also phosphorylate PtdIns3P in the 4-position, and PtdIns, PtdIns3P and PtdIns(3,4)P₂ in the 5-position in vitro, but to a lesser extent. The last of these reactions occurs in vivo and is physiologically relevant. Three different isoforms are known.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9032-61-5

References:

1. Kai, M., Salway, J.G. and Hawthorne, J.N. The diphosphoinositide kinase of rat brain. Biochem. J. 106 (1968) 791-801. [PMID: 4295336]

2. Kai, M., Salway, J.G., Michell, R.H. and Hawthorne, J.N. The biosynthesis of triphosphoinositide by rat brain in vitro. Biochem. Biophys. Res. Commun. 22 (1966) 370-375.

3. Rameh, L.E., Tolias, K.F., Duckworth, B.C. and Cantley, L.C. A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature 390 (1997) 192-196. [PMID: 9367159]

*EC 2.7.1.127

Common name: inositol-trisphosphate 3-kinase

Reaction: ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate

For diagram click here.

Other name(s): 1D-myo-inositol-trisphosphate 3-kinase

Systematic name: ATP:1D-myo-inositol-1,4,5-trisphosphate 3-phosphotransferase

Comments: Activated by Ca²⁺. Three isoforms have been shown to exist [3].

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 106283-10-7

References:

1. Hansen, C.A., Mah, S. and Williamson, J.R. Formation and metabolism of inositol 1,3,4,5-tetrakisphosphate in liver. J. Biol. Chem. 261 (1986) 8100-8103. [PMID: 3487541]

2. Irvine, R.F., Letcher, A.J., Heslop, J.P. and Berridge, M.J. The inositol tris/tetrakisphosphate pathway - demonstration of Ins(1,4,5)P₃ 3-kinase activity in animal tissues. Nature 320 (1986) 631-634. [PMID: 3010126]

3. Irvine, R.F. and Schell, M.J. Back in the water - the return of the inositol phosphates. Nat. Rev. Mol. Cell. Biol. 2 (2001) 327-338. [PMID: 11331907]

[EC 2.7.1.133 Deleted entry: inositol-trisphosphate 6-kinase. Now included with EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase (EC 2.7.1.133 created 1990, deleted 2002)]

*EC 2.7.1.134

Common name: inositol-tetrakisphosphate 1-kinase

Reaction: ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

For diagram click here.

Other name(s): 1D-myo-inositol-tetrakisphosphate 1-kinase; inositol-trisphosphate 6-kinase; 1D-myo-inositol-trisphosphate 6-kinase; ATP:1D-myo-inositol-1,3,4-trisphosphate 6-phosphotransferase; inositol-trisphosphate 5-kinase; 1D-myo-inositol-trisphosphate 5-kinase; ATP:1D-myo-inositol-1,3,4-trisphosphate 5-phosphotransferase

Systematic name: ATP:1D-myo-inositol-3,4,5,6-tetrakisphosphate 1-phosphotransferase

Comments: This enzyme also phosphorylates Ins(1,3,4)P₃ on O-5 and O-6. The phosphotransfer from ATP to either inositol 1,3,4-trisphosphate or inositol 3,4,5,6-tetrakisphosphate appears to be freely reversible to the extent that the enzyme can act like an inositol polyphosphate phosphatase in the presence of ADP. It can also catalyse an isomerization between Ins(1,3,4,5)P₄ and Ins(1,3,4,6)P₄ in the presence of ADP.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 113356-25-5; 111694-07-6 (from EC 2.7.1.139); 116677-02-2 (from EC 2.7.1.133)

References:

1. Stephens, L.R., Hawkins, P.T., Morris, A.J. and Downes, P.C. L-myo-Inositol 1,4,5,6-tetrakisphosphate (3-hydroxy)kinase. Biochem. J. 249 (1988) 283-292. [PMID: 2829850]

2. Balla, T., Guillemette, G., Baukal, A.J. and Catt, K. Metabolism of inositol 1,3,4-trisphosphate to a new tetrakisphosphate isomer in angiotensin-stimulated adrenal glomerulosa cells. J. Biol. Chem. 262 (1987) 9952-9955. [PMID: 3497156]

3. Shears, S.B., Parry, J.B., Tang, E.K.Y., Irvine, R.F., Michell, R.H. and Kirk, C.J. Metabolism of D-myo-inositol 1,3,4,5-tetrakisphosphate by rat liver, including the synthesis of a novel isomer of myo-inositol tetrakisphosphate. Biochem. J. 246 (1987) 139-147. [PMID: 2823793]

4. Shears, S.B. The pathway of myo-inositol 1,3,4-trisphosphate phosphorylation in liver. Identification of myo-inositol 1,3,4-trisphosphate 6-kinase, myo-inositol 1,3,4-trisphosphate 5-kinase, and myo-inositol 1,3,4,6-tetrakisphosphate 5-kinase. J. Biol. Chem. 264 (1989) 19879-19886. [PMID: 2584198]

5. Yang, X. and Shears, S.B. Multitasking in signal transduction by a promiscuous human Ins(3,4,5,6)P₄ 1-kinase/Ins(1,3,4)P₃ 5/6-kinase. Biochem. J. 351 (2000) 551-555. [PMID: 11042108]

6. Ho, M.W.Y., Yang, X., Carew, M.A., Zhan, T., Hua, L., Kwon, Y.-U., Chung, S.-K., Adelt, S., Vogel, G, Riley, A.M., Potter, B.V.L. and Shears, S.B. Regulation of Ins(3,4,5,6)P₄ signalling by a reversible kinase/phosphatase. Curr. Biol. 2002, in press.

*EC 2.7.1.137

Common name: phosphatidylinositol 3-kinase

Reaction: ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate

For diagram click here.

Other name(s): 1-phosphatidylinositol 3-kinase; type III phosphoinositide 3-kinase; Vps34p; type I phosphatidylinositol kinase

Systematic name: ATP:1-phosphatidyl-1D-myo-inositol 3-phosphotransferase

Comments: One mammalian isoform is known.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 115926-52-8

References:

1. Whitman, M., Downes, C.P., Keeler, M., Keller, T. and Cantley, L. Type I phosphatidylinositol kinase makes a novel inositol phospholipid, phosphatidylinositol-3-phosphate. Nature 332 (1988) 644-646. [PMID: 2833705]

2. Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535-602. [PMID: 11395417]

[EC 2.7.1.139 Deleted entry: inositol-trisphosphate 5-kinase. Now included with EC 2.7.1.134, inositol-tetrakisphosphate 1-kinase (EC 2.7.1.139 created 1992, deleted 2002)]

EC 2.7.1.149

Common name: 1-phosphatidylinositol-5-phosphate 4-kinase

Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate

For diagram click here.

Other name(s): type II PIP kinase

Systematic name: ATP:1-phosphatidyl-1D-myo-inositol-5-phosphate 4-phosphotransferase

References:

1. Rameh, L.E., Tolias, K.F., Duckworth, B.C. and Cantley, L.C. A new pathway for synthesis of phosphatidylinositol-4,5-bisphosphate. Nature 390 (1997) 192-196. [PMID: 9367159]

EC 2.7.1.150

Common name: 1-phosphatidylinositol-3-phosphate 5-kinase

Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 3-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate

For diagram click here.

Other name(s): type III PIP kinase; phosphatidylinositol 3-phosphate 5-kinase

Systematic name: ATP:1-phosphatidyl-1D-myo-inositol-3-phosphate 5-phosphotransferase

References:

1. Cooke, F.T., Dove, S.K., McEwen, R.K., Painter, G., Holmes, A.B., Hall, M.N., Michell, R.H. and Parker, P.J. The stress-activated phosphatidylinositol 3-phosphate 5-kinase Fab1p is essential for vacuole function in S. cerevisiae. Curr. Biol. 9 (1998) 1219-1222. [PMID: 9811604]

EC 2.7.1.151

Common name: inositol-polyphosphate multikinase

Reaction: ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate

ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate

For diagram click here.

Systematic name: ATP:1D-myo-inositol-1,4,5-trisphosphate 6-phosphotransferase

Comments: This enzyme also phosphorylates Ins(1,4,5)P₃ to Ins(1,3,4,5)P₄, Ins(1,3,4,5)P₄ to Ins(1,3,4,5,6)P₅, and Ins(1,3,4,5,6)P₄ to Ins(PP)P₄, isomer unknown.

References:

1. Saiardi, A., Erdjument-Bromage, H., Snowman, A.M., Tempst, P. and Snyder, S.H. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9 (1999) 1323-1326. [PMID: 10574768]

EC 2.7.1.152

Common name: inositol-hexakisphosphate kinase

Reaction: ATP + myo-inositol hexakisphosphate = ADP + diphospho-myo-inositol pentakisphosphate (isomeric configuration unknown)

Systematic name: ATP:1D-myo-inositol-hexakisphosphate phosphotransferase

Comments: This enzyme also phosphorylates Ins(1,3,4,5,6)P₅ to Ins(PP)P₄, isomer unknown. Two mammalian isoforms are known to exist.

References:

1. Saiardi, A., Erdjument-Bromage, H., Snowman, A.M., Tempst, P. and Snyder, S.H. Synthesis of diphosphoinositol pentakisphosphate by a newly identified family of higher inositol polyphosphate kinases. Curr. Biol. 9 (1999) 1323-1326. [PMID: 10574768]

2. Schell, M.J., Letcher, A.J., Brearley, C.A., Biber, J., Murer, H. and Irvine, R.F. PiUS (Pi uptake stimulator) is an inositol hexakisphosphate kinase. FEBS Lett. 461 (1999) 169-172. [PMID: 10567691]

EC 2.7.1.153

Common name: phosphatidylinositol-4,5-bisphosphate 3-kinase

Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate

For diagram click here.

Other name(s): type I phosphoinositide 3-kinase

Systematic name: ATP:1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate 3-phosphotransferase

Comments: This enzyme also catalyses the phosphorylation of PtdIns4P to PtdIns(3,4)P₂, and of PtdIns to PtdIns3P. Four mammalian isoforms are known to exist.

References:

1. Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535-602. [PMID: 11395417]

EC 2.7.1.154

Common name: phosphatidylinositol-4-phosphate 3-kinase

Reaction: ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate

For diagram click here.

Other name(s): type II phosphoinositide 3-kinase, C2-domain-containing phosphoinositide 3-kinase; phosphoinositide 3-kinase

Systematic name: ATP:1-phosphatidyl-1D-myo-inositol-4-phosphate 3-phosphotransferase

Comments: This enzyme also phosphorylates PtdIns to PtdIns3P. Three mammalian isoforms have been found to date.

References:

1. Vanhaesebroeck, B., Leevers, S.J., Ahmadi, K., Timms, J., Katso, R., Driscoll, P.C., Woscholski, R., Parker, P.J. and Waterfield, M.D. Synthesis and function of 3-phosphorylated inositol lipids. Annu. Rev. Biochem. 70 (2001) 535-602. [PMID: 11395417]

*EC 2.7.7.3

Common name: pantetheine-phosphate adenylyltransferase

Reaction: ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA

Other name(s): dephospho-CoA pyrophosphorylase; pantetheine phosphate adenylyltransferase; dephospho-CoA pyrophosphorylase; dephospho-coenzyme A pyrophosphorylase; 3'-dephospho-CoA pyrophosphorylase

Systematic name: ATP:pantetheine-4'-phosphate adenylyltransferase

Comments: The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9026-99-7

References:

1. Hoagland, M.B. and Novelli, G.D. Biosynthesis of coenzyme A from phosphopantetheine and of pantetheine from pantothenate. J. Biol. Chem. 207 (1954) 767-773.

2. Novelli, G.D. Enzymatic synthesis and structure of CoA. Fed. Proc. 12 (1953) 675-682.

3. Martin, D.P. and Drueckhammer, D.G. Separate enzymes catalyze the final two steps of coenzyme A biosynthesis in Brevibacterium ammoniagenes: purification of pantetheine phosphate adenylyltransferase. Biochem. Biophys. Res. Commun. 192 (1993) 1155-1161. [PMID: 8389542]

4. Geerlof, A., Lewendon, A. and Shaw, W.V. Purification and characterization of phosphopantetheine adenylyltransferase from Escherichia coli. J. Biol. Chem. 274 (1999) 27105-27111. [PMID: 10480925]

5. Izard, T., Geerlof, A., Lewendon, A. and Barker, J.J. Cubic crystals of phosphopantetheine adenylyltransferase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 55 1999) 1226-1228. [PMID: 10329792]

[EC 3.1.1.69 Transferred entry: now EC 3.5.1.89, N-acetylglucosaminylphosphatidylinositol deacetylase. Previously classified erroneously as an enzyme that hydrolysed an ester and not an amide (EC 3.1.1.69 created 1992, deleted 2002)]

*EC 3.1.3.25

Common name: inositol-1(or 4)-monophosphatase

Reaction: myo-inositol 1-phosphate + H₂O = myo-inositol + phosphate

For diagram click here.

Other name(s): myo-inositol-1(or 4)-monophosphatase; inositol 1-phosphatase; L-myo-inositol-1-phosphate phosphatase; myo-inositol 1-phosphatase; inositol phosphatase; inositol monophosphate phosphatase

Systematic name: myo-inositol-1(or 4)-phosphate phosphohydrolase

Comments: Acts on both enantiomers of myo-inositol 1-phosphate and myo-inositol 4-phosphate. Does not act on inositol bisphosphates, trisphosphates or tetrakisphosphates. Two isoforms are known [4].

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37184-63-7

References:

1. Eisenberg, P., Jr. D-Myoinositol 1-phosphate as product of cyclization of glucose 6-phosphate and substrate for a specific phosphatase in rat testis. J. Biol. Chem. 242 (1967) 1375-1382. [PMID: 4290245]

2. Gee, N.S., Ragan, C.I., Watling, K.J., Aspley, S., Jackson, R.G., Reid, G.G., Gani, D. and Shute, J.K. The purification and properties of myo-inositol monophosphatase from bovine brain. Biochem. J. 249 (1988) 883-889. [PMID: 2833231]

3. Hallcher, L.M. and Sherman, W.R. The effects of lithium ion and other agents on the activity of myo-inositol-1-phosphatase from bovine brain. J. Biol. Chem. 255 (1980) 10896-10901. [PMID: 6253491]

4. Yoshikawa, T., Turner, G., Esterling, L.E., Sanders, A.R. and Detera-Wadleigh, S.D. A novel human myo-inositol monophosphatase gene, IMP.18p, maps to a susceptibility region for bipolar disorder. Mol. Psychiatry 2 (1997) 393-397. [PMID: 9322233]

5. Woscholski, R. and Parker, P.J. Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates. In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Oxford University Press, Oxford, 2000, pp. 320-338.

*EC 3.1.3.36

Common name: phosphoinositide 5-phosphatase

Reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 4-phosphate + phosphate

For diagram click here.

Other name(s): type II inositol polyphosphate 5-phosphatase; triphosphoinositide phosphatase; IP₃ phosphatase; PtdIns(4,5)P₂ phosphatase; triphosphoinositide phosphomonoesterase; diphosphoinositide phosphatase; inositol 1,4,5-triphosphate 5-phosphomonoesterase; inositol triphosphate 5-phosphomonoesterase; phosphatidylinositol-bisphosphatase; phosphatidyl-myo-inositol-4,5-bisphosphate phosphatase; phosphatidylinositol 4,5-bisphosphate phosphatase; polyphosphoinositol lipid 5-phosphatase; phosphatidyl-inositol-bisphosphate phosphatase

Systematic name: phosphatidyl-myo-inositol-4,5-bisphosphate 4-phosphohydrolase

Comments: These enzymes can also remove the 5-phosphate from Ins(1,4,5)P₃ and/or Ins(1,3,4,5)P₄. They are a diverse family of enzymes, with differing abilities to catalyse two or more of the four reactions listed. They are thought to use inositol lipids rather than inositol phosphates as substrates in vivo. All of them can use either or both of PtdIns(4,5)P₂ and PtdIns(3,4,5)P₃ as substrates; this is the main property that distinguishes them from EC 3.1.3.56, inositol-polyphosphate 5-phosphatase.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9036-01-5

References:

1. Dawson, R.M.C. and Thompson, W. The triphosphoinositide phosphomonoesterase of brain tissue. Biochem. J. 91 (1964) 244-250. [PMID: 4284485]

2. Roach, P.D. and Palmer, F.B.S. Human erythrocyte cytosol phosphatidyl-inositol-bisphosphate phosphatase. Biochim. Biophys. Acta 661 (1981) 323-333. [PMID: 6271223]

3. Woscholski, R. and Parker, P.J. Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates. In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Oxford University Press, Oxford, 2000, pp. 320-338.

*EC 3.1.3.56

Common name: inositol-polyphosphate 5-phosphatase

Reaction: D-myo-inositol 1,4,5-trisphosphate + H₂O = myo-inositol 1,4-bisphosphate + phosphate

For diagram click here.

1D-myo-inositol 1,3,4,5-tetrakisphosphate + H₂O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate

Other name(s): type I inositol-polyphosphate phosphatase; inositol trisphosphate phosphomonoesterase; InsP₃/Ins(1,3,4,5)P₄ 5-phosphatase; inosine triphosphatase; D-myo-inositol 1,4,5-triphosphate 5-phosphatase; D-myo-inositol 1,4,5-trisphosphate 5-phosphatase; L-myo-inositol 1,4,5-trisphosphate-monoesterase; inositol phosphate 5-phosphomonoesterase; inositol-1,4,5-trisphosphate/1,3,4,5-tetrakisphosphate 5-phosphatase; Ins(1,4,5)P₃ 5-phosphatase; D-myo-inositol(1,4,5)/(1,3,4,5)-polyphosphate 5-phosphatase; inositol 1,4,5-trisphosphate phosphatase; inositol polyphosphate-5-phosphatase; inositol 1,4,5-trisphosphate phosphatase; myo-inositol-1,4,5-trisphosphate 5-phosphatase; inositol-1,4,5-trisphosphate 5-phosphatase

Systematic name: 1D-myo-inositol-1,4,5-trisphosphate 5-phosphohydrolase

Comments: One mammalian isoform is known. This enzyme is distinguished from the family of enzymes classified under EC 3.1.3.36, phosphoinositide 5-phosphatase, by its inability to dephosphorylate inositol lipids.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9082-57-9 and 106283-14-1

References:

1. Downes, C.P., Mussat, M.C. and Michell, R.H. The inositol trisphosphate phosphomonoesterase of the human erythrocyte membrane. Biochem. J. 203 (1982) 169-177. [PMID: 6285891]

2. Erneux, C., Lemos, M., Verjans, B., Vanderhaeghen, P., Delvaux, A. and Dumont, J.E. Soluble and particulate Ins(1,4,5)P₃/Ins(1,3,4,5)P₄ 5-phosphatase in bovine brain. Eur. J. Biochem. 181 (1989) 317-322. [PMID: 2540972]

3. Woscholski, R. and Parker, P.J. Inositol phosphatases: constructive destruction of phosphoinositides and inositol phosphates. In: Cockcroft, S. (Ed.), Biology of Phosphoinositides, Oxford University Press, Oxford, 2000, pp. 320-338.

4. Verjans, B., De Smedt, F., Lecocq, R., Vanweyenberg, V., Moreau, C. and Erneux, C. Cloning and expression in Escherichia coli of a dog thyroid cDNA encoding a novel inositol 1,4,5-trisphosphate 5-phosphatase. Biochem. J. 300 (1994) 85-90. [PMID: 8198557]

*EC 3.1.3.57

Common name: inositol-1,4-bisphosphate 1-phosphatase

Reaction: 1D-myo-inositol 1,4-bisphosphate + H₂O = 1D-myo-inositol 4-phosphate + phosphate

For diagram click here.

Other name(s): inositol-polyphosphate 1-phosphatase

Systematic name: 1D-myo-inositol-1,4-bisphosphate 1-phosphohydrolase

Comments: The enzyme acts on inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (forming inositol 3,4-bisphosphate) with similar V_max values for both substrates, but with a five-times higher affinity for the bisphosphate. Does not act on inositol 1-phosphate, inositol 1,4,5-trisphosphate or inositol 1,3,4,5-tetrakisphosphate.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 111070-17-8

References:

1. Berridge, M.J., Dawson, R.M.C., Downes, C.P., Heslop, J.P. and Irvine, R.F. Changes in the levels of inositol phosphates after agonist-dependent hydrolysis of membrane phosphoinositides. Biochem. J. 212 (1983) 473-482. [PMID: 6309146]

2. Connolly, T.M., Bansal, V.S., Bross, T.E., Irvine, R.F. and Majerus, P.W. The metabolism of tris- and tetraphosphates of inositol by 5-phosphomonoesterase and 3-kinase enzymes. J. Biol. Chem. 262 (1987) 2146-2149. [PMID: 3029066]

3. Inhorn, R.C. and Majerus, P.W. Inositol polyphosphate 1-phosphatase from calf brain. Purification and inhibition by Li⁺, Ca²⁺, and Mn²⁺. J. Biol. Chem. 262 (1987) 15946-15952. [PMID: 2824473]

[EC 3.1.3.61 Deleted entry: inositol-1,4,5-trisphosphate 1-phosphatase, as its existence has not been established (EC 3.1.3.61 created 1992, deleted 2002)]

*EC 3.1.3.62

Common name: multiple inositol-polyphosphate phosphatase

Reaction: myo-inositol hexakisphosphate + H₂O = myo-inositol pentakisphosphate (mixed isomers) + phosphate

Other name(s): inositol (1,3,4,5)-tetrakisphosphate 3-phosphatase; inositol 1,3,4,5-tetrakisphosphate 3-phosphomonoesterase; inositol 1,3,4,5-tetrakisphosphate-5-phosphomonoesterase; inositol tetrakisphosphate phosphomonoesterase; inositol-1,3,4,5-tetrakisphosphate 3-phosphatase; MIPP

Systematic name: 1D-myo-inositol-hexakisphosphate 5-phosphohydrolase

Comments: This enzyme exists in two isoforms. It also acts on Ins(1,3,4,5)P₄ to yield Ins(1,4,5)P₃.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 116958-30-6

References:

1. Cullen, P.J., Irvine, R.F., Drøbak, B.J. and Dawson, A.P. Inositol 1,3,4,5-tetrakisphosphate causes release of Ca²⁺ from permeabilized mouse lymphoma L1210 cells by its conversion into inositol 1,4,5-trisphosphate. Biochem. J. 259 (1989) 931-933. [PMID: 2786415]

2. Craxton, A., Caffrey, J.J., Burkhart, W., Safrany, S.T. and Shears, S.B. Molecular cloning and expression of a rat hepatic multiple inositol polyphosphate phosphatase. Biochem. J. 328 (1997) 75-81. [PMID: 9359836]

*EC 3.1.3.64

Common name: phosphatidylinositol-3-phosphatase

Reaction: 1-phosphatidyl-1D-myo-inositol 3-phosphate + H₂O = 1-phosphatidyl-1D-myo-inositol + phosphate

For diagram click here.

Other name(s): inositol-1,3-bisphosphate 3-phosphatase; inositol 1,3-bisphosphate phosphatase; inositol-polyphosphate 3-phosphatase; D-myo-inositol-1,3-bisphosphate 3-phosphohydrolase; phosphatidyl-3-phosphate 3-phosphohydrolase

Systematic name: 1-phosphatidyl-1D-myo-inositol-3-phosphate 3-phosphohydrolase

Comments: This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3)P₂ to Ins-1-P.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 124248-47-1

References:

1. Lips, D.L. and Majerus, P.W. The discovery of a 3-phosphomonoesterase that hydrolyzes phosphatidylinositol 3-phosphate in NIH 3T3 cells. J. Biol. Chem. 264 (1989) 19911-19915. [PMID: 2555336]

2. Caldwell, K.K., Lips, D.L., Bansal, V.S. and Majerus, P.W. Isolation and characterization of two 3-phosphatases that hydrolyze both phosphatidylinositol 3-phosphate and inositol 1,3-bisphosphate. J. Biol. Chem. 266 (1991) 18378-18386. [PMID: 1655747]

[EC 3.1.3.65 Deleted entry: inositol-1,3-bisphosphate 3-phosphatase. Now included with EC 3.1.3.64, phosphatidylinositol-3-phosphatase(EC 3.1.3.65 created 1992, deleted 2002)]

*EC 3.1.3.66

Common name: phosphatidylinositol-3,4-bisphosphate 4-phosphatase

Reaction: 1-phosphatidyl-myo-inositol 3,4-bisphosphate + H₂O = 1-phosphatidyl-1D-myo-inositol 3-phosphate + phosphate

For diagram click here.

Other name(s): inositol-3,4-bisphosphate 4-phosphatase; D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase; phosphoinositide 4-phosphatase; inositol polyphosphate 4-phosphatase; D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase; inositol polyphosphate 4-phosphatase type II

Systematic name: 1-phosphatidyl-1D-myo-inositol-3,4-bisphosphate 4-phosphohydrolase

Comments: Mg²⁺-independent. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4)P₃ to Ins(1,3)P₂. It also converts Ins(3,4)P₂ into Ins-3-P.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 122653-78-5

References:

1. Howell, S., Barnaby, R.J., Rowe, T., Ragan, C.I. and Gee, N.S. Evidence for at least four different inositol bisphosphatases in bovine brain. Eur. J. Biochem. 183 (1989) 169-172. [PMID: 2546770]

2. Norris, F.A., Auethavekiat, V. and Majerus, P.W. The isolation and characterization of cDNA encoding human and rat brain inositol polyphosphate 4-phosphatase. J. Biol. Chem. 270 (1995) 16128-16133. [PMID: 7608176]

3. Norris, F.A., Atkins, R.C. and Majerus, P.W. The cDNA cloning and characterization of inositol polyphosphate 4-phosphatase type II. Evidence for conserved alternative splicing in the 4-phosphatase family. J. Biol. Chem. 272 (1997) 23859-23864. [PMID: 9295334]

*EC 3.1.3.67

Common name: phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase

Reaction: phosphatidylinositol-3,4,5-trisphosphate + H₂O = phosphatidyl inositol-4,5-bisphosphate + phosphate

For diagram click here.

Other name(s): PTEN, MMAC1; phosphatidylinositol-3,4,5-trisphosphate 3-phosphohydrolase

Systematic name: 1-phosphatidyl-1D-myo-inositol-3,4,5-trisphosphate 3-phosphohydrolase

Comments: Requires Mg²⁺. Does not dephosphorylate inositol 4,5-bisphosphate. This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyses Ins(1,3,4,5)P₄ to Ins(1,4,5)P₃

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 171715-24-5

References:

1. Kabuyama, Y., Nakatsu, N., Homma, Y., Fukui, Y. Purification and characterization of phosphatidyl inositol-3,4,5-trisphosphate phosphatase in bovine thymus. Eur. J. Biochem. 238 (1996) 350-356. [PMID: 8681945]

2. Maehama, T. and Dixon, J.E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273 (1998) 13375-13378. [PMID: 9593664]

EC 3.1.3.70

Common name: mannosyl-3-phosphoglycerate phosphatase

Reaction: 2(α-D-mannosyl)-3-phosphoglycerate + H₂O = 2(α-D-mannosyl)-D-glycerate + phosphate

Systematic name: α-D-mannosyl-3-phosphoglycerate phosphohydrolase

Comments: Requires Mg²⁺. The enzyme from Pyrococcus horikoshii is specific for α-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate.

References:

1. Empadinhas, N., Marugg, J.D., Borges, N., Santos, H. and da Costa, M.S. Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key-enzymes. J. Biol. Chem. 276 (2001) 43580-43588. [PMID: 11562374]

EC 3.1.3.71

Common name: 2-phosphosulfolactate phosphatase

Reaction: 2-phospho-3-sulfolactate + H₂O = 3-sulfolactate + phosphate

Other name(s): (2R)-phosphosulfolactate phosphohydrolase; ComB phosphatase

Systematic name: (R)-2-phospho-3-sulfolactate phosphohydrolase

Comments: Requires Mg²⁺. The enzyme from Methanococcus jannaschii acts on both stereoisoimers of the substrate and also hydrolyses a number of phosphate monoesters of (S)-2-hydroxycarboxylic acids, including 2-phosphomalate, 2-phospholactate and 2-phosphoglycolate. This enzyme can also hydrolyze phosphate monoesters of (R)-2-hydroxycarboxylic acids such as (S)-2-phospho-3-sulfolactate and (R)-2-phosphomalate, which, presumably, bind to the enzyme in opposite orientations.

References:

1. Graham, D.E., Graupner, M., Xu, H. and White, R.H. Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. Eur. J. Biochem. 268 (2001) 5176-5188. [PMID: 11589710]

[EC 3.1.4.10 Transferred entry: now EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase. As there is no hydrolysis of the inositol 1,2-cyclic phosphate formed, previous classification of the enzyme as a hydrolase was incorrect. (EC 3.1.4.10 created 1972, modified 1976, deleted 2002)]

*EC 3.1.4.11

Common name: phosphoinositide phospholipase C

Reaction: 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H₂O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol

For diagram click here.

Other name(s): triphosphoinositide phosphodiesterase; phosphoinositidase C; 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase; monophosphatidylinositol phosphodiesterase; phosphatidylinositol phospholipase C, PI-PLC; 1-phosphatidyl-D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase

Systematic name: 1-phosphatidyl-1D-myo-inositol-4,5-bisphosphate inositoltrisphosphohydrolase

Comments: These enzymes form some of the cyclic phosphate Ins(cyclic1,2)P(4,5)P₂ as well as Ins(1,4,5)P₃. They show activity towards phosphatidylinositol, i.e., the activity of EC 4.6.1.13, phosphatidylinositol diacylglycerol-lyase, in vitro at high [Ca²⁺]. Four β-isoforms regulated by G-proteins, two γ-forms regulated by tyrosine kinases, four δ-forms regulated at least in part by calcium and an ε-form, probably regulated by the oncogene ras, have been found.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37213-51-7

References:

1. Downes, C.P. and Michell, R.H. The polyphosphoinositide phosphodiesterase of erythrocyte membranes. Biochem. J. 198 (1981) 133-140. [PMID: 6275838]

2. Thompson, W. and Dawson, R.M.C. The triphosphoinositide phosphodiesterase of brain tissue. Biochem. J. 91 (1964) 237-243.

3. Rhee, S.G. and Bae, Y.S. Regulation of phosphoinositide-specific phospholipase C isozymes. J. Biol. Chem. 272 (1997) 15045-15048. [PMID: 9182519]

[EC 3.1.4.36 Deleted entry: 1,2-cyclic-inositol-phosphate phosphodiesterase. Now included with EC 3.1.4.43, glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.36 created 1976, deleted 2002)]

*EC 3.1.4.43

Common name: glycerophosphoinositol inositolphosphodiesterase

Reaction: 1-(sn-glycero-3-phospho)-1D-myo-inositol + H₂O = glycerol + 1D-myo-inositol 1-phosphate

For diagram click here.

Other name(s): 1,2-cyclic-inositol-phosphate phosphodiesterase; D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase; D-inositol 1,2-cyclic phosphate 2-phosphohydrolase; D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase; 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase; inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase

Systematic name: 1-(sn-glycero-3-phospho)-1D-myo-inositol inositolphosphohydrolase

Comments: This enzyme also hydrolyses Ins(cyclic 1,2)P to Ins-1-P

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9076-91-9 (from EC 3.1.4.36)

References:

1. Dawson, R.M.C. and Hemington, N. A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol. Biochem. J. 162 (1977) 241-245. [PMID: 192216]

2. Dawson, R.M.C. and Clarke, N.G. D-myoInositol 1:2-cyclic phosphate 2-phosphohydrolase. Biochem. J. 127 (1972) 113-118. [PMID: 4342209]

3. Dawson, R.M.C. and Clarke, N.G. A comparison of D-inositol 1:2-cyclic phosphate 2-phosphohydrolase with other phosphodiesterases of kidney. Biochem. J. 134 (1973) 59-67. [PMID: 4353088]

4. Ross, T.S. and Majerus, P.W. Inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase. Substrate specificity and regulation of activity by phospholipids, metal ion chelators, and inositol 2-phosphate. J. Biol. Chem. 266 (1991) 851-856. [PMID: 1845995]

*EC 3.1.4.44

Common name: glycerophosphoinositol glycerophosphodiesterase

Reaction: 1-(sn-glycero-3-phospho)-1D-myo-inositol + H₂O = myo-inositol + sn-glycerol 3-phosphate

For diagram click here.

Other name(s): sn-glycero(3)phosphoinositol glycerophosphohydrolase; sn-glycero-3-phospho-1-inositol glycerophosphohydrolase

Systematic name: 1-(sn-glycero-3-phospho)-1D-myo-inositol glycerophosphohydrolase

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:

References:

1. Dawson, R.M.C., Hemington, N., Richards, D.E. and Irvine, R.F. sn-Glycero(3)phosphoinositol glycerophosphohydrolase. A new phosphodiesterase in rat tissues. Biochem. J. 182 (1979) 39-49. [PMID: 40550]

*EC 3.5.1.85

Common name: (S)-N-acetyl-1-phenylethylamine hydrolase

Reaction: N-acetylphenylethylamine + H₂O = phenylethylamine + acetate

Other name: (S)-N-acetyl-1-phenylethylamine amidohydrolase

Systematic name: (S)-N-acetylphenylethylamine:H₂O hydrolase

Comments: Inhibited by phenylmethanesulfonyl fluoride. Some related acetylated compounds are hydrolysed with variable enantiomeric selectivities.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 192230-94-7

References:

1. Brunella, A., Graf, M., Kittelmann, M., Lauma, K. and Ghisalba, O. Production, purification, and characterization of a highly enantioselective (S)-N-acetyl-1-phenylethyl amidohydrolase from Rhodococcus. Appl. Microbiol. Biotechnol. 47 (1997) 515-520.

EC 3.5.1.89

Common name: N-acetylglucosaminylphosphatidylinositol deacetylase

Reaction: N-acetyl-D-glucosaminylphosphatidylinositol + H₂O = D-glucosaminylphosphatidylinositol + acetate

Other name(s): acetylglucosaminylphosphatidylinositol deacetylase; N-acetylglucosaminylphosphatidylinositol de-N-acetylase; GlcNAc-PI deacetylase

Systematic name: N-acetyl-D-glucosaminylphosphatidylinositol acetylhydrolase

Comments: Involved in the formation of the glycosylphosphatidylinositol membrane anchor of the trypanosome variant-surface glycoprotein.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number:

References:

1. Doering, T.L., Masteron, W.J., Englund, P.T. and Hart, G.W. Biosynthesis of the glycosyl phosphatidylinositol membrane anchor of the trypanosome variant surface glycoprotein. Origin of the non-acetylated glucosamine. J. Biol. Chem. 264 (1989) 11168-11173. [PMID: 2525555]

2. Ferguson, M.A. The structure, biosynthesis and functions of glycosylphosphatidylinositol anchors, and the contributions of trypanosome research. J. Cell Sci. 112 (1999) 2799-2809. [PMID: 10444375]

EC 3.5.99.7

Common name: 1-aminocyclopropane-1-carboxylate deaminase

Reaction: 1-aminocyclopropane-1-carboxylate + H₂O = 2-oxobutanoate + NH₃

Other name(s): 1-aminocyclopropane-1-carboxylate endolyase (deaminating)

Systematic name: 1-aminocyclopropane-1-carboxylate aminohydrolase (isomerizing)

Comments: A pyridoxal 5'-phosphate enzyme. Its introduction has been used to make fruit ripening dependent on externally added ethylene, as it removes the substrate for endogenous ethylene formation.

Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, WIT, CAS registry number: 69553-48-6

References:

1. Honma, M. and Shimomura T. Metabolism of 1-aminocyclopropane-1-carboxylic acid. Agric. Biol. Chem. 42 (1978) 1825-1831.

2. Yao, M., Ose, T., Sugimoto, H., Horiuchi, A., Nakagawa, A., Wakatsuki, S., Yokoi, D., Murakami, T., Honma, M. and Tanaka, I. Crystal structure of 1-aminocyclopropane-1-carboxylate deaminase from Hansenula saturnus. J. Biol. Chem. 275 (2000) 34557-34565. [PMID: 10938279]

EC 3.6.1.52

Common name: diphosphoinositol-polyphosphate diphosphatase

Reaction: diphospho-myo-inositol polyphosphate + H₂O = myo-inositol polyphosphate + phosphate

Other name(s): diphosphoinositol-polyphosphate phosphohydrolase; DIPP

Systematic name: diphospho-myo-inositol-polyphosphate diphosphohydrolase

Comments: This enzyme hydrolyses the diphosphate bond, leaving a phospho group where a diphospho group had been. It can also act on bis(adenosine) diphosphate.

References:

1. Safrany, S.T., Caffrey, J.J., Yang, X., Bembenek, M.E., Moyer, M.B., Burkhart, W.A. and Shears, S.B. A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolase. EMBO J. 17 (1998) 6599-6607. [PMID: 9822604]

2. Caffrey, J.J., Safrany, S.T., Yang, X. and Shears, S.B. Discovery of molecular and catalytic diversity among human diphosphoinositol-polyphosphate phosphohydrolases. An expanding Nudt family. J. Biol. Chem. 275 (2000) 12730-12736. [PMID: 10777568]

EC 4.1.1.79

Common name: sulfopyruvate decarboxylase

Reaction: 3-sulfopyruvate = 2-sulfoacetaldehyde + CO₂

Systematic name: sulfopyruvate carboxy-lyase

Comments: Requires thiamine diphosphate. Does not decarboxylate pyruvate or phosphonopyruvate. The enzyme appears to be oxygen-sensitive.

References:

1. Graupner, M., Xu, H. and White, R.H. Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M. J. Bacteriol. 182 (2000) 4862-4867. [PMID: 10940029]

*EC 4.1.2.12

Common name: 2-dehydropantoate aldolase

Reaction: 2-dehydropantoate = 3-methyl-2-oxobutanoate + formaldehyde

Glossary:
pantoate = 2,4-dihydroxy-3,3-dimethylbutanoate

Other name(s): ketopantoaldolase

Systematic name: 2-dehydropantoate formaldehyde-lyase

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9024-51-5

References:

1. McIntosh, E.N., Purko, M. and Wood, W.A. Ketopantoate formation by a hydroxymethylation enzyme from Escherichia coli. J. Biol. Chem. 228 (1957) 499-510.

[EC 4.1.99.4 Transferred entry: now EC 3.5.99.7, 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4 created 1981, deleted 2002)]

[EC 4.2.1.26 Transferred entry: now EC 4.3.1.21, aminodeoxygluconate ammonia-lyase (EC 4.2.1.26 created 1965, deleted 2002)]

*EC 4.2.3.4

Common name: 3-dehydroquinate synthase

Reaction: 3-deoxy-arabino-heptulonate 7-phosphate = 3-dehydroquinate + phosphate

For diagram click here and mechanism here.

Other name(s): 5-dehydroquinate synthase; 5-dehydroquinic acid synthetase; dehydroquinate synthase; 3-dehydroquinate synthetase; 3-deoxy-arabino-heptulosonate-7-phosphate phosphate-lyase (cyclizing)

Systematic name: 3-deoxy-arabino-heptulonate-7-phosphate phosphate-lyase (cyclizing)

Comments: Requires Co²⁺ and bound NAD⁺. The hydrogen atoms on C-7 of the substrate are retained on C-2 of the product.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37211-77-1

References:

1. Rotenberg, S.L. and Sprinson, D.B. Mechanism and stereochemistry of 5-dehydroquinate synthetase. Proc. Natl. Acad. Sci. USA 67 (1970) 1669-1672. [PMID: 5275368]

2. Srinivasan, P.R., Rothschild, J. and Sprinson, D.B. The enzymic conversion of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate to 5-dehydroquinate. J. Biol. Chem. 238 (1963) 3176-3182.

3. Bender, S.L., Mehdi, S. and Knowles, J.R. Dehydroquinate synthase: the role of divalent metal cations and of nicotinamide adenine dinucleotide in catalysis. Biochemistry 28 (1989) 7555-7560. [PMID: 2514789]

4. Carpenter, E.P., Hawkins, A.R., Frost, J.W. and Brown, K.A. Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis. Nature 394 (1998) 299-302. [PMID: 9685163]

EC 4.3.1.21

Common name: aminodeoxygluconate ammonia-lyase

Reaction: 2-amino-2-deoxy-D-gluconate = 2-dehydro-3-deoxy-D-gluconate + NH₃

Other name(s): glucosaminic dehydrase; D-glucosaminate dehydratase; D-glucosaminic acid dehydrase; acetylenemonocarboxylic acid hydrase; aminodeoxygluconate dehydratase; 2-amino-2-deoxy-D-gluconate hydro-lyase (deaminating)

Systematic name: 2-amino-2-deoxy-D-gluconate ammonia-lyase

Comments: A pyridoxal-phosphate protein.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9032-93-3

References:

1. Merrick, J.M. and Roseman, S. D-Glucosaminic acid dehydrase. Methods Enzymol. 9 (1966) 657-660.

2. Yamada, E.W. and Jakoby, W.B. Enzymatic utilization of acetylenic compounds. II. Acetylenemonocarboxylic acid hydrase. J. Biol. Chem. 234 (1959) 941-945.

3. Iwamoto, R., Imanaga, Y. and Soda, K. D-Glucosaminate dehydratase from Agrobacterium radiobacter. Physicochemical and enzymological properties. J. Biochem. (Tokyo) 91 (1982) 283-289. [PMID: 7068563]

4. Iwamoto, R., Taniki, H., Koishi, J. and Nakura, S. D-Glucosaminate aldolase activity of D-glucosaminate dehydratase from Pseudomonas fluorescens and its requirement for Mn²⁺ ion. Biosci. Biotechnol. Biochem. 59 (1995) 408-411. [PMID: 7766176]

EC 4.6.1.13

Common name: phosphatidylinositol diacylglycerol-lyase

Reaction: 1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol

For diagram click here.

Other name(s): monophosphatidylinositol phosphodiesterase; phosphatidylinositol phospholipase C; 1-phosphatidylinositol phosphodiesterase; 1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming)

Systematic name: 1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming)

Comments: This enzyme is bacterial. Activity is also found in animals, but this activity is due to the presence of EC 3.1.4.11, phosphoinositide phospholipase C.

Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37288-19-0

References:

1. Allan, D. and Michell, R.H. Phosphatidylinositol cleavage catalysed by the soluble fraction from lymphocytes. Activity at pH5.5 and pH7.0. Biochem. J. 142 (1974) 591-597. [PMID: 4377210]

2. Friedel, R.O., Brown, J.D. and Durell, J. Monophosphatidyl inositol inositolphosphohydrolase in guinea-pig brain. Biochim. Biophys. Acta 144 (1967) 684-686. [PMID: 4294905]

3. Irvine, R.F. The enzymology of stimulated inositol lipid turnover. Cell Calcium 3 (1982) 295-309. [PMID: 6297738]

4. Michell, R.H. and Allan, D. Inositol cyclic phosphate as a product of phosphatidylinositol breakdown by phospholipase C (Bacillus cereus). FEBS Lett. 53 (1975) 302-304. [PMID: 236918]

5. Low, M.G. and Finean, J.B. Release of alkaline phosphatase fom membranes by a bacterial phosphatidylinositol phospholipase C. Biochem J. 167 (1977) 281-284. [PMID: 588258]

6. Henner, D.J., Yang, M., Chen, E., Helmikss, R. and Low, M.G. Sequence of the Bacillus thuringiensis phosphatidylinositol-specific phospholipase C. Nucleic Acids Res. 16 (1988) 10383 only. [PMID: 3194218]