6)-β-D-galactosyl]-1,2-diacyl-sn-glycerol + 1,2-diacyl-sn-glycerol
An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Common name: glycerol-3-phosphate dehydrogenase (NAD+)
Reaction: sn-glycerol 3-phosphate + NAD+ = glycerone phosphate + NADH + H+
Other name(s): α-glycerol phosphate dehydrogenase (NAD); α-glycerophosphate dehydrogenase (NAD); glycerol 1-phosphate dehydrogenase; glycerol phosphate dehydrogenase (NAD); glycerophosphate dehydrogenase (NAD); hydroglycerophosphate dehydrogenase; L-α-glycerol phosphate dehydrogenase; L-α-glycerophosphate dehydrogenase; L-glycerol phosphate dehydrogenase; L-glycerophosphate dehydrogenase; NAD-α-glycerophosphate dehydrogenase; NAD-dependent glycerol phosphate dehydrogenase; NAD-dependent glycerol-3-phosphate dehydrogenase; NAD-L-glycerol-3-phosphate dehydrogenase; NAD-linked glycerol 3-phosphate dehydrogenase; NADH-dihydroxyacetone phosphate reductase; glycerol-3-phosphate dehydrogenase (NAD)
Systematic name: sn-glycerol-3-phosphate:NAD+ 2-oxidoreductase
Comments: Also acts on propane-1,2-diol phosphate and glycerone sulfate (but with a much lower affinity).
Links to other databases: BRENDA, EXPASY, GTD, KEGG, ERGO, PDB, CAS registry number: 9075-65-4
References:
1. Baranowski, T. α-Glycerophosphate dehydrogenase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, pp. 85-96.
2. Brosemer, R.W. and Kuhn, R.W. Comparative structural properties of honeybee and rabbit α-glycerophosphate dehydrogenases. Biochemistry 8 (1969) 2095-2105. [PMID: 4307630]
3. O'Brien, S.J. and MacIntyre, R.J. The α-glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Biochem. Genet. 7 (1972) 141-161. [PMID: 4340553]
4. Warkentin, K.L. and Fondy, T.P. Isolation and characterization of cytoplasmic L-glycerol-3-phosphate dehydrogenase from rabbit-renal-adipose tissue and its comparison with the skeletal-muscle enzyme. Eur. J. Biochem. 36 (1973) 97-109. [PMID: 4200180]
5. Albertyn, J., van Tonder, A. and Prior, B.A. Purification and characterization of glycerol-3-phosphate dehydrogenase of Saccharomyces cerevisiae. FEBS Lett. 308 (1992) 130-132. [PMID: 1499720]
6. Koekemoer, T.C., Litthauer, D. and Oelofsen, W. Isolation and characterization of adipose tissue glycerol-3-phosphate dehydrogenase. Int. J. Biochem. Cell. Biol. 27 (1995) 625-632. [PMID: 7671141]
Common name: methylglyoxal reductase (NADH-dependent)
Reaction: (R)-lactaldehyde + NAD+ = methylglyoxal + NADH + H+
Other name(s): methylglyoxal reductase; D-lactaldehyde dehydrogenase
Systematic name: (R)-lactaldehyde:NAD+ oxidoreductase
Comments: This mammalian enzyme differs from the yeast enzyme, EC 1.1.1.283, methylglyoxal reductase (NADPH-dependent), in using NADH rather than NADPH as reductant. It oxidizes HO-CH2-CHOH-CHO (glyceraldehyde) as well as CH3-CHOH-CHO (lactaldehyde).
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 37250-16-1
References:
1. Ting, S.-M., Miller, O.N. and Sellinger, O.Z. The metabolism of lactaldehyde. VII. The oxidation of D-lactaldehyde in rat liver. Biochim. Biophys. Acta 97 (1965) 407-415. [PMID: 14323585]
Common name: glycerol-3-phosphate dehydrogenase [NAD(P)+]
Reaction: sn-glycerol 3-phosphate + NAD(P)+ = glycerone phosphate + NAD(P)H + H+
Other name(s): L-glycerol-3-phosphate:NAD(P) oxidoreductase; glycerol phosphate dehydrogenase (nicotinamide adenine dinucleotide (phosphate)); glycerol 3-phosphate dehydrogenase (NADP); glycerol-3-phosphate dehydrogenase [NAD(P)]
Systematic name: sn-glycerol-3-phosphate:NAD(P)+ 2-oxidoreductase
Comments: The enzyme from Escherichia coli shows specificity for the B side of NADPH.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 37250-30-9
References:
1. Kito, M. and Pizer, L.I. Purification and regulatory properties of the biosynthetic L-glycerol 3-phosphate dehydrogenase from Escherichia coli. J. Biol. Chem. 244 (1969) 3316-3323. [PMID: 4389388]
2. Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. J. Biol. Chem. 253 (1978) 6348-6353. [PMID: 355254]
3. Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol 3-phosphate, a precursor of phospholipid. Kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. J. Biol. Chem. 253 (1978) 6354-6363. [PMID: 28326]
4. Edgar, J.R. and Bell, R.M. Biosynthesis in Escherichia coli of sn-glycerol-3-phosphate, a precursor of phospholipid. Further kinetic characterization of wild type and feedback-resistant forms of the biosynthetic sn-glycerol-3-phosphate dehydrogenase. J. Biol. Chem. 255 (1980) 3492-3497. [PMID: 6767719]
Common name: methylglyoxal reductase (NADPH-dependent)
Reaction: lactaldehyde + NADP+ = methylglyoxal + NADPH + H+
Other name(s): lactaldehyde dehydrogenase (NADP+); Gre2
Systematic name: lactaldehyde:NADP+ oxidoreductase
Comments: The enzyme from the yeast Saccharomyces cerevisiae catalyses the conversion of methylglyoxal into lactaldehyde; the reverse reaction has not been demonstrated. It differs in coenzyme requirement from EC 1.1.1.78, methylglyoxal reductase (NADH-dependent), which is found in mammals. It also acts on phenylglyoxal and glyoxal.
References:
1. Murata, K., Fukuda, Y., Simosaka, M., Watanabe, K., Saikusa, T. and Kimura, A. Metabolism of 2-oxoaldehyde in yeasts. Purification and characterization of NADPH-dependent methylglyoxal-reducing enzyme from Saccharomyces cerevisiae. Eur. J. Biochem. 151 (1985) 631-636. [PMID: 3896793]
2. Chen, C.N., Porubleva, L., Shearer, G., Svrakic, M., Holden, L.G., Dover, J.L., Johnston, M., Chitnis, P.R. and Kohl, D.H. Associating protein activities with their genes: rapid identification of a gene encoding a methylglyoxal reductase in the yeast Saccharomyces cerevisiae. Yeast 20 (2003) 545-554. [PMID: 12722185]
Common name: S-(hydroxymethyl)glutathione dehydrogenase
Reaction: S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+
Other name(s): NAD-linked formaldehyde dehydrogenase (incorrect); formaldehyde dehydrogenase (incorrect); formic dehydrogenase (incorrect); class III alcohol dehydrogenase; ADH3; χ-ADH; FDH (incorrect); formaldehyde dehydrogenase (glutathione) (incorrect); GS-FDH (incorrect); glutathione-dependent formaldehyde dehydrogenase (incorrect); NAD-dependent formaldehyde dehydrogenase; GD-FALDH; NAD- and glutathione-dependent formaldehyde dehydrogenase
Systematic name: S-(hydroxymethyl)glutathione:NAD+ oxidoreductase
Comments: The substrate, S-(hydroxymethyl)glutathione, forms spontaneously from glutathione and formaldehyde; its rate of formation is increased in some bacteria by the presence of EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase. This enzyme forms part of the pathway that detoxifies formaldehyde, since the product is hydrolysed by EC 3.1.2.12, S-formylglutathione hydrolase. The human enzyme belongs to the family of zinc-dependent alcohol dehydrogenases. Also specifically reduces S-nitrosylglutathione.
References:
1. Jakoby, W.B. Aldehyde dehydrogenases. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd ed, vol. 7, Academic Press, New York, pp. 203-221.
2. Rose, Z.B. and Racker, E. Formaldehyde dehydrogenase. Methods Enzymol. 9 (1966) 357-360.
3. Liu, L., Hausladen, A., Zeng, M., Que, L., Heitman, J. and Stamler, J.S. A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410 (2001) 490-494. [PMID: 11260719]
4. Sanghani, P.C., Stone, C.L., Ray, B.D., Pindel, E.V., Hurley, T.D. and Bosron, W.F. Kinetic mechanism of human glutathione-dependent formaldehyde dehydrogenase. Biochemistry 39 (2000) 10720-10729. [PMID: 10978156]
5. van Ophem, P.W. and Duine, J.A. NAD- and co-substrate (GSH or factor)-dependent formaldehyde dehydrogenases from methylotrophic microorganisms act as a class III alcohol dehydrogenase. FEMS Microbiol. Lett. 116 (1994) 87-94.
6. Ras, J., van Ophem, P.W., Reijnders, W.N., Van Spanning, R.J., Duine, J.A., Stouthamer, A.H. and Harms, N. Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth. J. Bacteriol. 177 (1995) 247-251. [PMID: 7798140]
7. Barber, R.D., Rott, M.A. and Donohue, T.J. Characterization of a glutathione-dependent formaldehyde dehydrogenase from Rhodobacter sphaeroides. J. Bacteriol. 178 (1996) 1386-1393. [PMID: 8631716]
[EC 1.2.1.1 Deleted entry: glutathione-dependent formaldehyde dehydrogenase. This enzyme was classified on the basis of an incorrect reaction. It has been replaced by two enzymes, EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase and EC 4.4.1.22, S-(hydroxymethyl)glutathione synthase (EC 1.2.1.1 created 1961, modified 1982, modified 2002, deleted 2005)]
Common name: 1,2-dihydroxy-3-methyl-1,2-dihydrobenzoate dehydrogenase
Reaction: 1,6-dihydroxy-5-methylcyclohexa-2,4-diene-1-carboxylate + NAD+ = 3-methylcatechol + CO2 + NADH
Other name(s): 1,6-dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate dehydrogenase; 1,6-dihydroxy-5-methylcyclohexa-2,4-dienecarboxylate:NAD+ oxidoreductase (decarboxylating)
Systematic name: 1,6-dihydroxy-5-methylcyclohexa-2,4-diene-1-carboxylate:NAD+ oxidoreductase (decarboxylating)
Comments: Involved in the m-xylene degradation pathway in bacteria.
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, ERGO, CAS registry number:
References:
1. Neidle, E., Hartnett, C., Ornston, L.N., Bairoch, A., Rekik, M. and Harayama, S. cis-Diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily. Eur. J. Biochem. 204 (1992) 113-120. [PMID: 1740120]
Common name: methylenetetrahydrofolate reductase [NAD(P)H]
Reaction: 5-methyltetrahydrofolate + NAD(P)+ = 5,10-methylenetetrahydrofolate + NAD(P)H + H+
For diagram of reaction click here and for its place in C1 metabolism, click here
Other name(s): methylenetetrahydrofolate (reduced nicotinamide adenine dinucleotide phosphate) reductase; 5,10-methylenetetrahydrofolate reductase (NADPH); 5,10-methylenetetrahydrofolic acid reductase; 5,10-CH2-H4folate reductase; methylenetetrahydrofolate reductase (NADPH2); 5-methyltetrahydrofolate:NAD oxidoreductase; 5-methyltetrahydrofolate:NAD+ oxidoreductase; methylenetetrahydrofolate (reduced riboflavin adenine dinucleotide) reductase; 5,10-methylenetetrahydrofolate reductase; methylenetetrahydrofolate reductase; N5,10-methylenetetrahydrofolate reductase; 5,10-methylenetetrahydropteroylglutamate reductase; N5,N10-methylenetetrahydrofolate reductase; methylenetetrahydrofolic acid reductase; 5-methyltetrahydrofolate:(acceptor) oxidoreductase (incorrect); 5,10-methylenetetrahydrofolate reductase (FADH2); MetF; methylenetetrahydrofolate reductase (NADPH); 5-methyltetrahydrofolate:NADP+ oxidoreductase
Systematic name: 5-methyltetrahydrofolate:NAD(P)+ oxidoreductase
Comments: A flavoprotein (FAD). Menadione can also serve as an electron acceptor.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 71822-25-8
References:
1. Daubner, S.C. and Matthews, R.T. Purification and properties of methylenetetrahydrofolate reductase from pig liver. J. Biol. Chem. 257 (1982) 140-145. [PMID: 6975779]
2. Kutzbach, C. and Stokstad, E.L.R. Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine. Biochim. Biophys. Acta 250 (1971) 459-477. [PMID: 4399897]
3. Sheppard, C.A., Trimmer, E.E. and Matthews, R.G. Purification and properties of NADH-dependent 5,10-methylenetetrahydrofolate reductase (MetF) from Escherichia coli. J. Bacteriol. 181 (1999) 718-725. [PMID: 9922232]
4. Guenther, B.D., Sheppard, C.A., Tran, P., Rozen, R., Matthews, R.G. and Ludwig, M.L. The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia. Nat. Struct. Biol. 6 (1999) 359-365. [PMID: 10201405]
EC 1.5.7 With an iron-sulfur protein as acceptor
Common name: methylenetetrahydrofolate reductase (ferredoxin)
Reaction: 5-methyltetrahydrofolate + oxidized ferredoxin = 5,10-methylenetetrahydrofolate + reduced ferredoxin
Other name(s): 5,10-methylenetetrahydrofolate reductase
Systematic name: 5-methyltetrahydrofolate:ferredoxin oxidoreductase
Comments: An iron-sulfur flavoprotein that also contains zinc. The enzyme from Clostridium formicoaceticum catalyses the reduction of methylene blue, menadione, benzyl viologen, rubredoxin or FAD with 5-methyltetrahydrofolate and the oxidation of reduced ferredoxin or FADH2 with 5,10-methylenetetrahydrofolate. However, unlike EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H], there is no activity with NAD(P)H.
References:
1. Clark, J.E. and Ljungdahl, L.G. Purification and properties of 5,10-methylenetetrahydrofolate reductase, an iron-sulfur flavoprotein from Clostridium formicoaceticum. J. Biol. Chem. 259 (1984) 10845-10849. [PMID: 6381490]
Common name: urate oxidase
Reaction: urate + O2 + H2O = 5-hydroxyisourate + H2O2
For diagram click here.
Other name(s): uric acid oxidase; uricase; uricase II
Systematic name: urate:oxygen oxidoreductase
Comments: This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine mas), the mould Aspergillus flavus and Bacillus subtilus contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, CAS registry number: 9002-12-4
References:
1. London, M. and Hudson, P.B. Purification and properties of solubilized uricase. Biochim. Biophys. Acta 21 (1956) 290-298.
2. Mahler, H.R., Hübscher, G. and Baum, H. Studies on uricase. I. Preparation, purification, and properties of a cuproprotein. J. Biol. Chem. 216 (1955) 625-641.
3. Robbins, K.C., Barnett, E.L. and Grant, N.H. Partial purification of porcine liver uricase. J. Biol. Chem. 216 (1955) 27-35. [PMID: 13252004]
4. Kahn, K. and Tipton, P.A. Spectroscopic characterization of intermediates in the urate oxidase reaction. Biochemistry 37 (1998) 11651-11659. [PMID: 9709003]
5. Colloc'h, N., el Hajji, M., Bachet, B., L'Hermite, G., Schiltz, M., Prange, T., Castro, B. and Mornon, J.-P. Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution. Nat. Struct. Biol. 4 (1997) 947-952. [PMID: 9360612]
6. Imhoff, R.D., Power, N.P., Borrok, M.J. and Tipton, P.A. General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad. Biochemistry 42 (2003) 4094-4100. [PMID: 12680763]
[EC 1.7.99.5 Deleted entry: 5,10-methylenetetrahydrofolate reductase (FADH2). Now included with EC 1.5.1.20, methylenetetrahydrofolate reductase [NAD(P)H]. Based on the reference, it had been thought that this was a separate enzyme from EC 1.5.1.20 but the reference upon which the entry was based has since been disproved. (EC 1.7.99.5 created 1965 as EC 1.1.1.68, transferred 1978 to EC 1.1.99.15, transferred 1980 to EC 1.7.99.5, deleted 2005)]
Common name: deacetoxyvindoline 4-hydroxylase
Reaction: deacetoxyvindoline + 2-oxoglutarate + O2 = deacetylvindoline + succinate + CO2
For reaction pathway click here.
Other name(s): desacetoxyvindoline 4-hydroxylase; desacetyoxyvindoline-17-hydroxylase; D17H; desacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4β-hydroxylating)
Systematic name: deacetoxyvindoline,2-oxoglutarate:oxygen oxidoreductase (4β-hydroxylating)
Comments: Requires Fe2+ and ascorbate. Also acts on 3-hydroxy-16-methoxy-2,3-dihydrotabersonine and to a lesser extent on 16-methoxy-2,3-dihydrotabersonine.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 132084-83-4
References:
1. De Carolis, E., Chan, F., Balsevich, J. and De Luca, V. Isolation and characterization of a 2-oxoglutarate dependent dioxygenase involved in the 2nd-to-last step in vindoline biosynthesis Plant Physiol. 94 (1990) 1323-1329.
2. De Carolis, E. and De Luca, V. Purification, characterization, and kinetic analysis of a 2-oxoglutarate-dependent dioxygenase involved in vindoline biosynthesis from Catharanthus roseus. J. Biol. Chem. 268 (1993) 5504-5511. [PMID: 8449913]
3. Vazquez-Flota, F.A. and De Luca, V. Developmental and light regulation of desacetoxyvindoline 4-hydroxylase in Catharanthus roseus (L.) G. Don. Evidence of a multilevel regulatory mechanism. Plant Physiol. 117 (1998) 1351-1361. [PMID: 9701591]
Common name: 3-phenylpropanoate dioxygenase
Reaction: 3-phenylpropanoate + NADH + H+ + O2 = 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate + NAD+
For diagram click here.
Other name(s): HcaA1A2CD; Hca dioxygenase; 3-phenylpropionate dioxygenase
Systematic name: 3-phenylpropanoate,NADH:oxygen oxidoreductase (2,3-hydroxylating)
Comments: This enzyme catalyses the insertion of both atoms of molecular oxygen into positions 2 and 3 of the phenyl ring of 3-phenylpropanoate. The product, 3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate, is then converted into 3-(2,3-dihydroxyphenyl)propanoate, by a dehydrogenase, with the concomitant regeneration of NADH. The enzyme also acts on (2E)-3-phenylprop-2-enoate (cinnamate).
References:
1. Díaz, E., Ferrández, A. and García, J.L. Characterization of the hca cluster encoding the dioxygenolytic pathway for initial catabolism of 3-phenylpropionic acid in Escherichia coli K-12. J. Bacteriol. 180 (1998) 2915-2923. [PMID: 9603882]
2. Burlingame, R. and Chapman, P.J. Catabolism of phenylpropionic acid and its 3-hydroxy derivative by Escherichia coli. J. Bacteriol. 155 (1983) 113-121. [PMID: 6345502]
Common name: CDP-4-dehydro-6-deoxyglucose reductase
Reaction: CDP-4-dehydro-3,6-dideoxy-D-glucose + NAD(P)+ + H2O = CDP-4-dehydro-6-deoxy-D-glucose + NAD(P)H + H+
For diagram click here.
Other name(s): CDP-4-keto-6-deoxyglucose reductase; cytidine diphospho-4-keto-6-deoxy-D-glucose reductase; cytidine diphosphate 4-keto-6-deoxy-D-glucose-3-dehydrogenase; CDP-4-keto-deoxy-glucose reductase; CDP-4-keto-6-deoxy-D-glucose-3-dehydrogenase system; NAD(P)H:CDP-4-keto-6-deoxy-D-glucose oxidoreductase
Systematic name: CDP-4-dehydro-3,6-dideoxy-D-glucose:NAD(P)+ 3-oxidoreductase
Comments: The enzyme consists of two proteins. One forms an enzyme-bound adduct of the CDP-4-dehydro-6-deoxyglucose with pyridoxamine phosphate, in which the 3-hydroxy group has been removed. The second catalyses the reduction of this adduct by NAD(P)H and release of the CDP-4-dehydro-3,6-dideoxy-D-glucose and pyridoxamine phosphate.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 37256-87-4
References:
1. Pape, H. and Strominger, J.L. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. V. Partial purification of the two protein components required for introduction of the 3-deoxy group. J. Biol. Chem. 244 (1969) 3598-3604. [PMID: 4389672]
2. Rubenstein, P.A. and Strominger, J.L. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. VII. Mechanistic roles of enzyme E1 and pyridoxamine 5'-phosphate in the formation of cytidine diphosphate-4-keto-3,6-dideoxy-D-glucose from cytidine diphosphate-4-keto-6-deoxy-D-glucose. J. Biol. Chem. 249 (1974) 3776-3781. [PMID: 4152100]
3. Liu, H.-W. and Thorson, J.S. Pathways and mechanisms in the biogenesis of novel deoxysugars by bacteria. Annu. Rev. Microbiol. 48 (1994) 223-256. [PMID: 7826006]
Common name: tRNA guanosine-2'-O-methyltransferase
Reaction: S-adenosyl-L-methionine + tRNA = S-adenosyl-L-homocysteine + tRNA containing 2'-O-methylguanosine
Other name(s): transfer ribonucleate guanosine 2'-methyltransferase; tRNA guanosine 2'-methyltransferase; tRNA (guanosine 2')-methyltransferase; tRNA (Gm18) 2'-O-methyltransferase; tRNA (Gm18) methyltransferase; tRNA (guanosine-2'-O-)-methyltransferase; S-adenosyl-L-methionine:tRNA (guanosine-2'-O-)-methyltransferase
Systematic name: S-adenosyl-L-methionine:tRNA guanosine-2'-O-methyltransferase
Comments: Methylates the 2'-hydroxy group of a guanosine present in a GG sequence at position 18. Yeast tRNAPhe is one of the best substrate tRNAs.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, CAS registry number: 37257-01-5
References:
1. Gefter, M.L. The in vitro synthesis of 2'-O-methylguanosine and 2-methylthio 6N (γ,γ-dimethylallyl) adenosine in transfer RNA of Escherichia coli. Biochem. Biophys. Res. Commun. 36 (1969) 435-441. [PMID: 4898378]
2. Kumagai, I., Watanabe, K. and Oshima, T. Thermally induced biosynthesis of 2'-O-methylguanosine in tRNA from an extreme thermophile, Thermus thermophilus HB27. Proc. Natl. Acad. Sci. USA 77 (1980) 1922-1926. [PMID: 6990416]
3. Hori, H., Yamazaki, N., Matsumoto, T., Watanabe, Y., Ueda, T., Nishikawa, K., Kumagai, I. and Watanabe, K. Substrate recognition of tRNA (guanosine-2'-)-methyltransferase from Thermus thermophilus HB27. J. Biol. Chem. 273 (1998) 25721-25727. [PMID: 9748240]
Common name: tabersonine 16-O-methyltransferase
Reaction: S-adenosyl-L-methionine + 16-hydroxytabersonine = S-adenosyl-L-homocysteine + 16-methoxytabersonine
For diagram click here.
Other name(s): 11-demethyl-17-deacetylvindoline 11-methyltransferase; 11-O-demethyl-17-O-deacetylvindoline O-methyltransferase; S-adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline 11-O-methyltransferase
Systematic name: S-adenosyl-L-methionine:16-hydroxytabersonine 16-O-methyltransferase
Comments: Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 100984-95-0
References:
1. De Luca, V., Balsevich, J., Tyler, R.T., Eilert, U., Panchuk, B.D. and Kurz, W.G.W. Biosynthesis of indole alkaloids - developmental regulation of the biosynthetic-pathway from tabersonine to vindoline in Catharanthus roseus. J. Plant Physiol. 125 (1986) 147-156.
2. Fahn, W., Laussermair, E., Deus-Neumann, B. and Stöckigt, J. Late enzymes of vindoline biosynthesis. S-Adenosyl-L-methionine:11-O-demethyl-17-O-deacetylvindoline 11-O-methylase and unspecific acetylesterase. Plant Cell Rep. 4 (1985) 337-340.
Common name: 3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase
Reaction: S-adenosyl-L-methionine + 3-hydroxy-16-methoxy-2,3-dihydrotabersonine = S-adenosyl-L-homocysteine + deacetoxyvindoline
For diagram click here.
Other name(s): 16-methoxy-2,3-dihydro-3-hydroxytabersonine methyltransferase; NMT; 16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase; S-adenosyl-L-methionine:16-methoxy-2,3-dihydro-3-hydroxytabersonine N-methyltransferase
Systematic name: S-adenosyl-L-methionine:3-hydroxy-16-methoxy-2,3-dihydrotabersonine N-methyltransferase
Comments: Involved in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle Catharanthus roseus.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 113478-40-3
References:
1. De Luca, V., Balsevich, J., Tyler, R.T., Eilert, U., Panchuk, B.D. and Kurz, W.G.W. Biosynthesis of indole alkaloids - developmental regulation of the biosynthetic-pathway from tabersonine to vindoline in Catharanthus roseus. J. Plant Physiol. 125 (1986) 147-156.
2. De Luca, V. and Cutler, A.J. Subcellular localization of enzymes involved in indole alkaloid biosynthesis in Catharanthus roseus. Plant Physiol. 85 (1987) 1099-1102.
Common name: sterigmatocystin 8-O-methyltransferase
Reaction: S-adenosyl-L-methionine + sterigmatocystin = S-adenosyl-L-homocysteine + 8-O-methylsterigmatocystin
For diagram click here.
Glossary: sterigmatocystin = 3a,12c-dihydro-8-hydroxy-6-methoxyfuro[3',2':4,5]furo[2,3-c]xanthen-7-one
Other name(s): sterigmatocystin methyltransferase; O-methyltransferase II; sterigmatocystin 7-O-methyltransferase (incorrect); S-adenosyl-L-methionine:sterigmatocystin 7-O-methyltransferase (incorrect)
Systematic name: S-adenosyl-L-methionine:sterigmatocystin 8-O-methyltransferase
Comments: Dihydrosterigmatocystin can also act as acceptor. Involved in the biosynthesis of aflatoxins in fungi.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 116958-29-3
References:
1. Bhatnagar, D., McCormick, S.P., Lee, L.S. and Hill, R.A. Identification of O-methylsterigmatocystin as an aflatoxin B1 and G1 precursor in Aspergillus parasiticus. Appl. Environ. Microbiol. 53 (1987) 1028-1033. [PMID: 3111363]
2. Yabe, K., Ando, Y., Hashimoto, J. and Hamasaki, T. Two distinct O-methyltransferases in aflatoxin biosynthesis. Appl. Environ. Microbiol. 55 (1989) 2172-2177. [PMID: 2802602]
Common name: deacetylvindoline O-acetyltransferase
Reaction: acetyl-CoA + deacetylvindoline = CoA + vindoline
For diagram click here.
Other name(s): deacetylvindoline acetyltransferase; DAT; 17-O-deacetylvindoline-17-O-acetyltransferase; acetylcoenzyme A-deacetylvindoline 4-O-acetyltransferase; acetyl-CoA-17-O-deacetylvindoline 17-O-acetyltransferase; acetylcoenzyme A:deacetylvindoline 4-O-acetyltransferase; acetylcoenzyme A:deacetylvindoline O-acetyltransferase; 17-O-deacetylvindoline O-acetyltransferase; acetyl-CoA:17-O-deacetylvindoline 17-O-acetyltransferase
Systematic name: acetyl-CoA:deacetylvindoline 4-O-acetyltransferase
Comments: Catalyses the final step in the biosynthesis of vindoline from tabersonine in the Madagascar periwinkle, Catharanthus roseus.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 100630-41-9
References:
1. Fahn, W., Gundlach, H., Deus-Neumann, B. and Stöckigt, J. Late enzymes of vindoline biosynthesis. Acetyl-CoA:17-O-deactylvindoline 17-O-acetyl-transferase. Plant Cell Rep. 4 (1985) 333-336.
Common name: monogalactosyldiacylglycerol synthase
Reaction: UDP-galactose + 1,2-diacyl-sn-glycerol = UDP + 3-β-D-galactosyl-1,2-diacyl-sn-glycerol
For diagram click here.
Other name(s): uridine diphosphogalactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose:diacylglycerol galactosyltransferase; MGDG synthase; UDP galactose-1,2-diacylglycerol galactosyltransferase; UDP-galactose-diacylglyceride galactosyltransferase; UDP-galactose:1,2-diacylglycerol 3-β-D-galactosyltransferase; 1β-MGDG; 1,2-diacylglycerol 3-β-galactosyltransferase
Systematic name: UDP-galactose:1,2-diacyl-sn-glycerol 3-β-D-galactosyltransferase
Comments: This enzyme adds only one galactosyl group to the diacylglycerol; EC 2.4.1.241, digalactosyldiacylglycerol synthase, adds a galactosyl group to the product of the above reaction. There are three isoforms in Arabidopsis that can be divided into two types, A-type (MGD1) and B-type (MGD2 and MGD3). MGD1 is the isoform responsible for the bulk of monogalactosyldiacylglycerol (MGDG) synthesis in Arabidopsis [4].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 37277-55-7
References:
1. Veerkamp, J.H. Biochemical changes in Bifidobacterium bifidum var. pennsylvanicus after cell-wall inhibition. VI. Biosynthesis of the galactosyldiglycerides. Biochim. Biophys. Acta 348 (1974) 23-34. [PMID: 4838219]
2. Wenger, D.A., Petipas, J.W. and Pieringer, R.A. The metabolism of glyceride glycolipids. II. Biosynthesis of monogalactosyl diglyceride from uridine diphosphate galactose and diglyceride in brain. Biochemistry 7 (1968) 3700-3707. [PMID: 5681471]
3. Miège, C., Maréchal, E., Shimojima, M., Awai, K., Block, M.A., Ohta, H., Takamiya, K., Douce, R. and Joyard, J. Biochemical and topological properties of type A MGDG synthase, a spinach chloroplast envelope enzyme catalyzing the synthesis of both prokaryotic and eukaryotic MGDG. Eur. J. Biochem. 265 (1999) 990-1001. [PMID: 10518794]
4. Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397-2400. [PMID: 15590685]
Common name: galactolipid galactosyltransferase
Reaction: 2 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol = 3-[α-D-galactosyl-(16)-β-D-galactosyl]-1,2-diacyl-sn-glycerol + 1,2-diacyl-sn-glycerol
For diagram click here.
Other name(s): galactolipid-galactolipid galactosyltransferase; galactolipid:galactolipid galactosyltransferase; interlipid galactosyltransferase; GGGT; DGDG synthase (ambiguous); digalactosyldiacylglycerol synthase (ambiguous)
Systematic name: 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol:mono-3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol β-D-galactosyltransferase
Comments: By further transfers of galactosyl residues to the digalactosyldiacylglycerol, trigalactosyldiacylglycerol and tetragalactosyldiacylglycerol are also formed. This enzyme was originally thought to be the major enzyme involved in the production of digalactosyldiacylglycerol in plants as it masked the effect of the true enzyme (EC 2.4.1.241, digalactosyldiacylglycerol synthase) [4,5]. Its activity is localized to chloroplast envelope membranes, but it does not contribute to net galactolipid synthesis in plants [4].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 66676-74-2
References:
1. Dorne, A.-J., Block, M.A., Joyard, J. and Douce, R. The galactolipid-galactolipid galactosyltransferase is located on the outer surface of the outer-membrane of the chloroplast envelope. FEBS Lett. 145 (1982) 30-34.
2. Heemskerk, J.W.M., Wintermans, J.F.G.M., Joyard, J., Block, M.A., Dorne, A.-J. and Douce, R. Localization of galactolipid:galactolipid galactosyltransferase and acyltransferase in outer envolope membranes of spinach chloroplasts. Biochim. Biophys. Acta 877 (1986) 281-289.
3. Heemskerk, J.W.M., Jacobs, F.H.H. and Wintermans, J.F.G.M. UDPgalactose-independent synthesis of monogalactosyldiacylglycerol. An enzymatic activity of the spinach chloroplast envelope. Biochim. Biophys. Acta 961 (1988) 38-47.
4. Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694-2706. [PMID: 14600212]
5. Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397-2400. [PMID: 15590685]
Common name: digalactosyldiacylglycerol synthase
Reaction: UDP-galactose + 3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol = UDP + 3-[α-D-galactosyl-(16)-β-D-galactosyl]-1,2-diacyl-sn-glycerol
For diagram click here.
Other name(s): DGD1; DGD2; DGDG synthase (ambiguous); UDP-galactose-dependent DGDG synthase; UDP-galactose-dependent digalactosyldiacylglycerol synthase; UDP-galactose:MGDG galactosyltransferase
Systematic name: UDP-galactose:3-(β-D-galactosyl)-1,2-diacyl-sn-glycerol 6-α-galactosyltransferase
Comments: Requires Mg2+. Diacylglycerol cannot serve as an acceptor molecule for galactosylation as in the reaction catalysed by EC 2.4.1.46, monogalactosyldiacylglyerol synthase. When phosphate is limiting, phospholipids in plant membranes are reduced but these are replaced, at least in part, by the glycolipids digalactosyldiacylglycerol (DGDG) and sulfoquinovosyldiacylglycerol [3]. While both DGD1 and DGD2 are increased under phosphate-limiting conditions, DGD2 does not contribute significantly under optimal growth conditions. DGD2 is responsible for the synthesis of DGDG molecular species that are rich in C16 fatty acids at sn-1 of diacylglycerol whereas DGD1 leads to molecular species rich in C18 fatty acids [3]. The enzyme has been localized to the outer side of chloroplast envelope membranes.
References:
1. Kelly, A.A. and Dörmann, P. DGD2, an Arabidopsis gene encoding a UDP-galactose-dependent digalactosyldiacylglycerol synthase is expressed during growth under phosphate-limiting conditions. J. Biol. Chem. 277 (2002) 1166-1173. [PMID: 11696551]
2. Härtel, H., Dörmann, P. and Benning, C. DGD1-independent biosynthesis of extraplastidic galactolipids after phosphate deprivation in Arabidopsis. Proc. Natl. Acad. Sci. USA 97 (2000) 10649-10654. [PMID: 10973486]
3. Kelly, A.A., Froehlich, J.E. and Dörmann, P. Disruption of the two digalactosyldiacylglycerol synthase genes DGD1 and DGD2 in Arabidopsis reveals the existence of an additional enzyme of galactolipid synthesis. Plant Cell 15 (2003) 2694-2706. [PMID: 14600212]
4. Benning, C. and Ohta, H. Three enzyme systems for galactoglycerolipid biosynthesis are coordinately regulated in plants. J. Biol. Chem. 280 (2005) 2397-2400. [PMID: 15590685]
Common name: squalene synthase
Reaction: (1) 2 farnesyl diphosphate = diphosphate + presqualene diphosphate
(2) presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate + NAD(P)+
For diagram click here.
Other name(s): farnesyltransferase; presqualene-diphosphate synthase; presqualene synthase; squalene synthetase; farnesyl-diphosphate farnesyltransferase
Systematic name: farnesyl-diphosphate:farnesyl-diphosphate farnesyltransferase
Comments: The enzyme from yeast requires either Mg2+ or Mn2+ for activity. In the absence of NAD(P)H, presqualene diphosphate is accumulated.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, CAS registry number: 9077-14-9
References:
1. Kuswick-Rabiega, G. and Rilling, H.C. Squalene synthetase. Solubilization and partial purification of squalene synthetase, copurification of presqualene pyrophosphate and squalene synthetase activities. J. Biol. Chem. 262 (1987) 1505-1509. [PMID: 3805037]
2. Ericsson, J., Appelkvist, E.L., Thelin, A., Chojnacki, T. and Dallner, G. Isoprenoid biosynthesis in rat liver peroxisomes. Characterization of cis-prenyltransferase and squalene synthetase. J. Biol. Chem. 267 (1992) 18708-18714. [PMID: 1527001]
3. Tansey, T.R. and Shechter, I. Structure and regulation of mammalian squalene synthase. Biochim. Biophys. Acta 1529 (2000) 49-62. [PMID: 11111077]
4. LoGrasso, P.V., Soltis, D.A. and Boettcher, B.R. Overexpression, purification, and kinetic characterization of a carboxyl-terminal-truncated yeast squalene synthetase. Arch. Biochem. Biophys. 307 (1993) 193-199. [PMID: 8239656]
5. Shechter, I., Klinger, E., Rucker, M.L., Engstrom, R.G., Spirito, J.A., Islam, M.A., Boettcher, B.R. and Weinstein, D.B. Solubilization, purification, and characterization of a truncated form of rat hepatic squalene synthetase. J. Biol. Chem. 267 (1992) 8628-8635. [PMID: 1569107]
Common name: poly(3-hydroxyoctanoate) depolymerase
Reaction: Hydrolyses the polyester poly{oxycarbonyl[(R)-2-pentylethylene]} to oligomers
Other name(s): PHO depolymerase, poly(3HO) depolymerase; poly[(R)-hydroxyalkanoic acid] depolymerase; poly(HA) depolymerase; poly(HAMCL) depolymerase; poly[(R)-3-hydroxyoctanoate] hydrolase
Systematic name: poly{oxycarbonyl[(R)-2-pentylethylene]} hydrolase
Comments: The main product after prolonged incubation is the dimer [3]. Besides hydrolysing polymers of 3-hydroxyoctanoic acid, the enzyme also hydrolyses other polymers derived from medium-chain-length (C6-C12) hydroxyalkanoic acids and copolymers of mixtures of these. It also hydrolyses p-nitrophenyl esters of fatty acids. Polymers of short-chain-length hydroxyalkanoic acids such as poly[(R)-3-hydroxybutanoic acid] and poly[(R)-3-hydroxypentanoic acid] are not hydrolysed.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number:
References:
1. Jendrossek, D. Microbial degradation of polyesters. Adv. Biochem. Eng. Biotechnol. 71 (2001) 293-325. [PMID: 11217416]
2. García, B., Olivera, E.R., Miñambres, B., Fernández-Valverde, M., Cañedo, L.M., Prieto, M.A., García, J.L., Martínez, M. and Luengo, J.M. Novel biodegradable aromatic plastics from a bacterial source. Genetic and biochemical studies on a route of the phenylacetyl-CoA catabolon. J. Biol. Chem. 274 (1999) 29228-29241. [PMID: 10506180]
3. Schirmer, A., Jendrossek, D. and Schlegel, H.G. Degradation of poly(3-hydroxyoctanoic acid) [P(3HO)] by bacteria: purification and properties of a P(3HO) depolymerase from Pseudomonas fluorescens GK13. Appl. Environ. Microbiol. 59 (1993) 1220-1227. [PMID: 8476295]
[EC 3.1.2.24 Transferred entry: 2-(2-hydroxyphenyl)benzenesulfinate hydrolase, the enzyme was incorrectly classified as a thiolester hydrolase when the bond broken is a C-S bond, which is not an ester. Now EC 3.13.1.3, 2'-hydroxybiphenyl-2-sulfinate desulfinase (EC 3.1.2.24 created 2000, deleted 2005)]
Common name: bile-acid-CoA hydrolase
Reaction: deoxycholoyl-CoA + H2O = CoA + deoxycholate
Systematic name: deoxycholoyl-CoA hydrolase
Comments: Choloyl-CoA, 3-dehydrocholoyl-CoA and chenodeoxycholoyl-CoA can also act as substrates, but acetyl-CoA, isovaleryl-CoA, palmitoyl-CoA and phenylacetyl-CoA cannot.
References:
1. Ye, H.Q., Mallonee, D.H., Wells, J.E., Bjorkhem, I. and Hylemon, P.B. The bile acid-inducible baiF gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A hydrolase. J. Lipid Res. 40 (1999) 17-23. [PMID: 9869646]
Common name: mannosylglycoprotein endo-β-mannosidase
Reaction: Hydrolysis of the α-D-mannosyl-(16)-β-D-mannosyl-(14)-β-D-N-acetylglucosaminyl-(14)-β-D-N-acetylglucosaminyl sequence of glycoprotein to α-D-mannosyl-(16)-D-mannose and β-D-N-acetylglucosaminyl-(14)-β-D-N-acetylglucosaminyl sequences
Other name(s): endo-β-mannosidase
Comments: The substrate group is a substituent on N-4 of an asparagine residue in the glycoprotein. The mannose residue at the non-reducing end of the sequence may carry further α-D-mannosyl groups on O-3 or O-6, but such a substituent on O-3 of the β-D-mannosyl group prevents the action of the enzyme. The enzyme was obtained from the lily, Lilium longiflorum.
References:
1. Ishimizu, T., Sasaki, A., Okutani, S., Maeda, M., Yamagishi, M. and Hase, S. Endo-β-mannosidase, a plant enzyme acting on N-glycan. Purification, molecular cloning, and characterization. J. Biol. Chem. 279 (2004) 38555-38562. [PMID: 15247239]
2. Sasaki, A., Yamagishi, M., Mega, T., Norioka, S., Natsuka, S. and Hase, S. Partial purification and characterization of a novel endo-β-mannosidase acting on N-linked sugar chains from Lilium longiflorum thumb. J. Biochem. (Tokyo) 125 (1999) 363-367. [PMID: 9990135]
Common name: fructan β-(2,1)-fructosidase
Reaction: Hydrolysis of terminal, non-reducing 2,1-linked β-D-fructofuranose residues in fructans
For diagram click here.
Other name(s): β-(2-1)-D-fructan fructohydrolase; β-(2-1)fructan exohydrolase; inulinase; 1-FEH II; 1-fructan exohydrolase; 1-FEH w1; 1-FEH w2; β-(2-1)-linkage-specific fructan-β-fructosidase
Systematic name: β-(2,1)-D-fructan fructohydrolase
Comments: Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the inulin-type fructans, such as 1-kestose (β-D-fructofuranosyl-(21)-β-D-fructofuranosyl α-D-glucopyranoside) and 1,1-nystose (β-D-fructofuranosyl-(21)-β-D-fructofuranosyl-(21)-β-D-fructofuranosyl α-D-glucopyranoside), some (but not all) levan-type fructans can also be hydrolysed, but more slowly [see EC 3.2.1.154, fructan β-(2,6)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases.
References:
1. De Roover, J., Van Laere, A., De Winter, M., Timmermans, J.W. and Van den Ende, W. Purification and properties of a second fructan exohydrolase from the roots of Cichorium intybus. Physiol. Plant. 106 (1999) 28-34.
2. Van den Ende, W., Clerens, S., Vergauwen, R., Van Riet, L., Van Laere, A., Yoshida, M. and Kawakami, A. Fructan 1-exohydrolases. β-(2,1)-Trimmers during graminan biosynthesis in stems of wheat? Purification, characterization, mass mapping, and cloning of two fructan 1-exohydrolase isoforms. Plant Physiol. 131 (2003) 621-631. [PMID: 12586886]
Common name: fructan β-(2,6)-fructosidase
Reaction: Hydrolysis of terminal, non-reducing 2,6-linked β-D-fructofuranose residues in fructans
For diagram click here.
Other name(s): β-(2-6)-fructan exohydrolase; levanase; 6-FEH
Systematic name: β-(2,6)-D-fructan fructohydrolase
Comments: Possesses one of the activities of EC 3.2.1.80, fructan β-fructosidase. While the best substrates are the levan-type fructans such as 6-kestotriose (β-D-fructofuranosyl-(26)-β-D-fructofuranosyl α-D-glucopyranoside) and 6,6-kestotetraose (β-D-fructofuranosyl-(26)-β-D-fructofuranosyl-(26)-β-D-fructofuranosyl α-D-glucopyranoside), some (but not all) inulin-type fructans can also be hydrolysed, but more slowly (cf. EC 3.2.1.153, fructan β-(2,1)-fructosidase). Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases.
References:
1. Marx, S.P., Nösberger, J. and Frehner, M. Hydrolysis of fructan in grasses: A β-(2-6)-linkage specific fructan-β-fructosidase from stubble of Lolium perenne. New Phytol. 135 (1997) 279-290.
2. Van den Ende, W., De Coninck, B., Clerens, S., Vergauwen, R. and Van Laere, A. Unexpected presence of fructan 6-exohydrolases (6-FEHs) in non-fructan plants: characterization, cloning, mass mapping and functional analysis of a novel 'cell-wall invertase-like' specific 6-FEH from sugar beet (Beta vulgaris L.). Plant J. 36 (2003) 697-710. [PMID: 14617070]
3. Henson, C.A. and Livingston, D.P., III. Purification and characterization of an oat fructan exohydrolase that preferentially hydrolyzes β-2,6-fructans. Plant Physiol. 110 (1996) 639-644.
Common name: acetylspermidine deacetylase
Reaction: N8-acetylspermidine + H2O = acetate + spermidine
Glossary: spermidine
spermine
Other name(s): N8-monoacetylspermidine deacetylase; N8-acetylspermidine deacetylase; N-acetylspermidine deacetylase; N1-acetylspermidine amidohydrolase (incorrect)
Systematic name: N8-acetylspermidine amidohydrolase
Comments: It was initially thought that N1-acetylspermidine was the substrate for this deacetylase reaction [1] but this has since been disproved by Marchant et al. [3].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 67339-07-5
References:
1. Libby, P.R. Properties of an acetylspermidine deacetylase from rat liver. Arch. Biochem. Biophys. 188 (1978) 360-363. [PMID: 28089]
2. Blankenship, J. Deacetylation of N8-acetylspermidine by subcellular fractions of rat tissue. Arch. Biochem. Biophys. 189 (1978) 20-27. [PMID: 708044]
3. Marchant, P., Manneh, V.A. and Blankenship, J. N1-Acetylspermidine is not a substrate for N-acetylspermidine deacetylase. Biochim. Biophys. Acta 881 (1986) 297-299. [PMID: 3955076]
Common name: 2'-hydroxybiphenyl-2-sulfinate desulfinase
Reaction: 2'-hydroxybiphenyl-2-sulfinate + H2O = 2-hydroxybiphenyl + sulfite
For diagram click here.
Other name(s): gene dszB-encoded hydrolase; 2-(2-hydroxyphenyl) benzenesulfinate:H2O hydrolase; DszB; HBPSi desulfinase; 2-(2-hydroxyphenyl) benzenesulfinate sulfohydrolase; HPBS desulfinase; 2-(2-hydroxyphenyl)benzenesulfinate hydrolase; 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase; 2-(2-hydroxyphenyl)benzenesulfinate desulfinase
Systematic name: 2'-hydroxybiphenyl-2-sulfinate sulfohydrolase
Comments: The enzyme from Rhodococcus sp. strain IGTS8 is encoded by the plasmid-encoded dibenzothiophene-desulfurization (dsz) operon. The enzyme has a narrow substrate specificity with biphenyl-2-sulfinate being the only other substrate known to date [2].
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, ERGO, CAS registry number:
References:
1. Oldfield, C., Pogrebinsky, O., Simmonds, J., Ölson, E.S. and Kulpa, C.F. Elucidation of the metabolic pathway for dibenzothiophene desulfurization by Rhodococcus sp. strain IGTS8 (ATCC 53968). Microbiology 143 (1997) 2961-2973. [PMID: 9308179]
2. Nakayama, N., Matsubara, T., Ohshiro, T., Moroto, Y., Kawata, Y., Koizumi, K., Hirakawa, Y., Suzuki, M., Maruhashi, K., Izumi, Y. and Kurane, R. A novel enzyme, 2'-hydroxybiphenyl-2-sulfinate desulfinase (DszB), from a dibenzothiophene-desulfurizing bacterium Rhodococcus erythropolis KA2-5-1: gene overexpression and enzyme characterization. Biochim. Biophys. Acta 1598 (2002) 122-130. [PMID: 12147352]
3. Watkins, L.M., Rodriguez, R., Schneider, D., Broderick, R., Cruz, M., Chambers, R., Ruckman, E., Cody, M. and Mrachko, G.T. Purification and characterization of the aromatic desulfinase, 2-(2'-hydroxyphenyl)benzenesulfinate desulfinase. Arch. Biochem. Biophys. 415 (2003) 14-23. [PMID: 12801508]
Common name: phosphonopyruvate decarboxylase
Reaction: 3-phosphonopyruvate = 2-phosphonoacetaldehyde + CO2
Systematic name: 3-phosphonopyruvate carboxy-lyase
Comments: The enzyme catalyses a step in the biosynthetic pathway of 2-aminoethylphosphonate, a component of the capsular polysaccharide complex of Bacteroides fragilis. Requires thiamine diphosphate and Mg2+ as cofactors. The enzyme is activated by the divalent cations Mg2+, Ca2+ and Mn2+. Pyruvate and sulfopyruvate can also act as substrates, but more slowly.
References:
1. Zhang, G., Dai, J., Lu, Z. and Dunaway-Mariano, D. The phosphonopyruvate decarboxylase from Bacteroides fragilis. J. Biol. Chem. 278 (2003) 41302-41308. [PMID: 12904299]
Common name: bile-acid 7α-dehydratase
Reaction: 7α,12α-dihydroxy-3-oxochol-4-enoate = 12α-hydroxy-3-oxochola-4,6-dienoate + H2O
For diagram click here.
Systematic name: 7α,12α-dihydroxy-3-oxochol-4-enoate hydro-lyase
Comments: The enzyme from Eubacterium sp. strain VPI 12708 can also use 7α-hydroxy-3-oxochol-4-enoate as a substrate but not 7α,12α-dihydroxy-3-oxochol-5β-anoate, 3α,7α,12α-trihydroxychol-5β-anoate or 7β-hydroxy-3-oxochol-4-enoate.
References:
1. Dawson, J.A., Mallonee, D.H., Björkhem, I. and Hylemon, P.B. Expression and characterization of a C24 bile acid 7α-dehydratase from Eubacterium sp. strain VPI 12708 in Escherichia coli. J. Lipid Res. 37 (1996) 1258-1267. [PMID: 8808760]
[EC 4.2.99.19 Transferred entry: Now EC 4.4.1.23, 2-hydroxypropyl-CoM lyase. The enzyme was incorrectly classified as acting on a C-O bond rather than a C-S bond (EC 4.2.99.19 created 2001, deleted 2005)]
Common name: S-(hydroxymethyl)glutathione synthase
Reaction: S-(hydroxymethyl)glutathione = glutathione + formaldehyde
Other name(s): glutathione-dependent formaldehyde-activating enzyme; Gfa
Systematic name: S-(hydroxymethyl)glutathione formaldehyde-lyase
Comments: The enzyme from Paracoccus denitrificans accelerates the spontaneous reaction in which the adduct of formaldehyde and glutathione is formed, i.e. the substrate for EC 1.1.1.284, S-(hydroxymethyl)glutathione dehydrogenase, in the formaldehyde-detoxification pathway.
References:
1. Goenrich, M., Bartoschek, S., Hagemeier, C.H., Griesinger, C. and Vorholt, J.A. A glutathione-dependent formaldehyde-activating enzyme (Gfa) from Paracoccus denitrificans detected and purified via two-dimensional proton exchange NMR spectroscopy. J. Biol. Chem. 277 (2002) 3069-3072. [PMID: 11741920]
Common name: 2-hydroxypropyl-CoM lyase
Reaction: (R)-[or (S)-]2-hydroxypropyl-CoM = (R)-[or (S)-]1,2-epoxypropane + HS-CoM
For diagram click here.
Glossary:
coenzyme M (CoM) = 2-mercaptoethanesulfonate
Other name(s): epoxyalkane:coenzyme M transferase; epoxyalkane:CoM transferase; epoxyalkane:2-mercaptoethanesulfonate transferase; coenzyme M-epoxyalkane ligase; epoxyalkyl:CoM transferase; epoxypropane:coenzyme M transferase; epoxypropyl:CoM transferase; EaCoMT; 2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming)
Systematic name: (R)-[or (S)-]2-hydroxypropyl-CoM:2-mercaptoethanesulfonate lyase (epoxyalkane-ring-forming)
Comments: Requires zinc. Acts on both enantiomers of chiral epoxyalkanes to form the corresponding (R)- and (S)-2-hydroxyalkyl-CoM adducts. The enzyme will function with some other thiols (e.g., 2-sulfanylethanol) as the nucleophile. Uses short-chain epoxyalkanes from C2 (epoxyethane) to C6 (1,2-epoxyhexane). This enzyme forms component I of a four-component enzyme system {comprising EC 4.4.1.23 (2-hydroxypropyl-CoM lyase; component I), EC 1.8.1.5 [2-oxopropyl-CoM reductase (carboxylating); component II], EC 1.1.1.268 [2-(R)-hydroxypropyl-CoM dehydrogenase; component III] and EC 1.1.1.269 [2-(S)-hydroxypropyl-CoM dehydrogenase; component IV]} that is involved in epoxyalkane carboxylation in Xanthobacter sp. strain Py2.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, UM-BBD, CAS registry number: 244301-07-3
References:
1. Allen, J.R., Clark, D.D., Krum, J.G. and Ensign, S.A. A role for coenzyme M (2-mercaptoethanesulfonic acid) in a bacterial pathway of aliphatic epoxide carboxylation. Proc. Natl. Acad. Sci. USA 96 (1999) 8432-8437. [PMID: 10411892]
2. Krum, J.G., Ellsworth, H., Sargeant, R.R., Rich, G. and Ensign, S.A. Kinetic and microcalorimetric analysis of substrate and cofactor interactions in epoxyalkane:CoM transferase, a zinc-dependent epoxidase. Biochemistry 41 (2002) 5005-5014. [PMID: 11939797]
3. Coleman, N.V. and Spain, J.C. Epoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of Mycobacterium strain JS60. J. Bacteriol. 185 (2003) 5536-5545. [PMID: 12949106]
Common name: phenylacetaldoxime dehydratase
Reaction: (Z)-phenylacetaldehyde oxime = phenylacetonitrile + H2O
For diagram click here.
Other name(s): PAOx dehydratase; arylacetaldoxime dehydratase; OxdB
Systematic name: (Z)-phenylacetaldehyde-oxime hydro-lyase
Comments: The enzyme from Bacillus sp. OxB-1 contains protoheme IX, the iron of which must be in the form iron(II) for activity. (Z)-Phenylacetaldoxime binds to ferric heme (the iron(III) form) via the oxygen atom whereas it binds to the active ferrous form via the nitrogen atom. In this way, the oxidation state of the heme controls the coordination stucture of the substrate—heme complex, which regulates enzyme activity [2]. The enzyme is active towards several (Z)-arylacetaldoximes and (E/Z)-alkylaldoximes as well as towards arylalkylaldoximes such as 3-phenylpropionaldoxime and 4-phenylbutyraldoxime. However, it is inactive with phenylacetaldoximes that have a substituent group at an α-site of an oxime group, for example, with (E/Z)-2-phenylpropionaldoxime and (E/Z)-mandelaldoxime. The activity of the enzyme is inhibited completely by the heavy-metal cations Cu+, Cu2+, Ag+ and Hg+ whereas Fe2+ and Sn2+ have an activatory effect.
References:
1. Kato, Y., Nakamura, K., Sakiyama, H., Mayhew, S.G. and Asano, Y. Novel heme-containing lyase, phenylacetaldoxime dehydratase from Bacillus sp. strain OxB-1: purification, characterization, and molecular cloning of the gene. Biochemistry 39 (2000) 800-809. [PMID: 10651646]
2. Kobayashi, K., Yoshioka, S., Kato, Y., Asano, Y. and Aono, S. Regulation of aldoxime dehydratase activity by redox-dependent change in the coordination structure of the aldoxime-heme complex. J. Biol. Chem. 280 (2005) 5486-5490. [PMID: 15596434]
Common name: CDP-paratose 2-epimerase
Reaction: CDP-3,6-dideoxy-D-glucose = CDP-3,6-dideoxy-D-mannose
For diagram click here.
Other name(s): CDP-paratose epimerase; cytidine diphosphoabequose epimerase; cytidine diphosphodideoxyglucose epimerase; cytidine diphosphoparatose epimerase; cytidine diphosphate paratose-2-epimerase; CDP-abequose epimerase (incorrect); CDP-D-abequose 2-epimerase (incorrect)
Systematic name: CDP-3,6-dideoxy-D-glucose 2-epimerase
Comments: Requires NAD+. CDP-paratose (CDP-3,6-dideoxy-D-glucose), is more systematically called CDP-α-3,6-dideoxy-D-ribo-hexose. CDP-tyvelose (CDP-3,6-dideoxy-D-mannose) is systematically called CDP-3,6-dideoxy-D-arabino-hexose.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, ERGO, CAS registry number: 37318-36-8
References:
1. Matsuhashi, S. Enzymatic synthesis of cytidine diphosphate 3,6-dideoxyhexoses. II. Reversible 2-epimerization of cytidine diphosphate paratose. J. Biol. Chem. 241 (1966) 4275-4282. [PMID: 5924649]
2. Liu, H.-W. and Thorson, J.S. Pathways and mechanisms in the biogenesis of novel deoxysugars by bacteria. Annu. Rev. Microbiol. 48 (1994) 223-256. [PMID: 7826006]
Common name: dihydrofolate synthase
Reaction: ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8-dihydropteroylglutamate
For diagram click here.
Other name(s): dihydrofolate synthetase; 7,8-dihydrofolate synthetase; H2-folate synthetase; 7,8-dihydropteroate:L-glutamate ligase (ADP); dihydrofolate synthetase-folylpolyglutamate synthetase; folylpoly-(γ-glutamate) synthetase-dihydrofolate synthase; FHFS; FHFS/FPGS; dihydropteroate:L-glutamate ligase (ADP-forming); DHFS
Systematic name: 7,8-dihydropteroate:L-glutamate ligase (ADP-forming)
Comments: In bacteria, a single protein catalyses both this activity and that of EC 6.3.2.17, tetrahydrofolate synthase [2], the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates. In contrast, the activities are located on separate proteins in most eukaryotes studied to date [3]. This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa [3].
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, CAS registry number: 37318-62-0
References:
1. Griffin, M.J. and Brown, G.M. The biosynthesis of folic acid. III. Enzymatic formation of dihydrofolic acid from dihydropteroic acid and of tetrahydropteroylpolyglutamic acid compounds from tetrahydrofolic acid. J. Biol. Chem. 239 (1964) 310-316. [PMID: 14114858]
2. Bognar, A.L., Osborne, C., Shane, B., Singer, S.C. and Ferone, R. Folylpoly-γ-glutamate synthetase-dihydrofolate synthetase. Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product. J. Biol. Chem. 260 (1985) 5625-5630. [PMID: 2985605]
3. Ravanel, S., Cherest, H., Jabrin, S., Grunwald, D., Surdin-Kerjan, Y., Douce, R. and Rébeillé, F. Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 98 (2001) 15360-15365. [PMID: 11752472]
4. Cherest, H., Thomas, D. and Surdin-Kerjan, Y. Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae. J. Biol. Chem. 275 (2000) 14056-14063. [PMID: 10799479]
5. Cossins, E.A. and Chen, L. Folates and one-carbon metabolism in plants and fungi. Phytochemistry 45 (1997) 437-452. [PMID: 9190084]
Common name: tetrahydrofolate synthase
Reaction: ATP + tetrahydropteroyl-[γ-Glu]n + L-glutamate = ADP + phosphate + tetrahydropteroyl-[γ-Glu]n+1
For diagram click here.
Other name(s): folylpolyglutamate synthase; folate polyglutamate synthetase; formyltetrahydropteroyldiglutamate synthetase; N10-formyltetrahydropteroyldiglutamate synthetase; folylpoly-γ-glutamate synthase; folylpolyglutamyl synthetase; folylpoly(γ-glutamate) synthase; folylpolyglutamate synthetase; folylpoly-γ-glutamate synthetase-dihydrofolate synthetase; FPGS; tetrahydrofolylpolyglutamate synthase; tetrahydrofolate:L-glutamate γ-ligase (ADP-forming)
Systematic name: tetrahydropteroyl-[γ-Glu]n:L-glutamate γ-ligase (ADP-forming)
Comments: In bacteria, a single protein catalyses both this activity and that of EC 6.3.2.12, dihydrofolate synthase [3], the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H4PteGlun), i.e. various tetrahydrofolates (H4folate). In contrast, the activities are located on separate proteins in most eukaryotes studied to date [4]. In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast. Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes [4]. As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C1 metabolism. (reviewed in [5]). The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates.
Links to other databases: BRENDA, EXPASY, KEGG, ERGO, PDB, CAS registry number: 63363-84-8
References:
1. Cichowicz, D., Foo, S.K. and Shane, B. Folylpoly-γ-glutamate synthesis by bacteria and mammalian cells. Mol. Cell. Biochem. 39 (1981) 209-228. [PMID: 6458762]
2. McGuire, J.J. and Bertino, J.R. Enzymatic synthesis and function of folylpolyglutamates. Mol. Cell. Biochem. 38 (1981) 19-48. [PMID: 7027025]
3. Bognar, A.L., Osborne, C., Shane, B., Singer, S.C. and Ferone, R. Folylpoly-γ-glutamate synthetase-dihydrofolate synthetase. Cloning and high expression of the Escherichia coli folC gene and purification and properties of the gene product. J. Biol. Chem. 260 (1985) 5625-5630. [PMID: 2985605]
4. Ravanel, S., Cherest, H., Jabrin, S., Grunwald, D., Surdin-Kerjan, Y., Douce, R. and Rébeillé, F. Tetrahydrofolate biosynthesis in plants: molecular and functional characterization of dihydrofolate synthetase and three isoforms of folylpolyglutamate synthetase in Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 98 (2001) 15360-15365. [PMID: 11752472]
5. Cossins, E.A. and Chen, L. Folates and one-carbon metabolism in plants and fungi. Phytochemistry 45 (1997) 437-452. [PMID: 9190084]
6. Cherest, H., Thomas, D. and Surdin-Kerjan, Y. Polyglutamylation of folate coenzymes is necessary for methionine biosynthesis and maintenance of intact mitochondrial genome in Saccharomyces cerevisiae. J. Biol. Chem. 275 (2000) 14056-14063. [PMID: 10799479 ]