3)-N-acetyl-D-glucosamine + phosphate = α-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
An asterisk before 'EC' indicates that this is an amendment to an existing enzyme rather than a new enzyme entry.
Recommended name: dTDP-4-dehydro-6-deoxyglucose reductase
Reaction: dTDP-D-fucose + NADP = dTDP-4-dehydro-6-deoxy-D-glucose + NADPH2
For reaction pathway click here.
Other name(s): dTDP-4-keto-6-deoxyglucose reductase
Systematic name: dTDP-D-fucose:NADP oxidoreductase
Comments: The enzyme from the gram-negative bacterium Actinobacillus actinomycetemcomitans forms activated fucose for incorporation into capsular polysaccharide.
Reference:
1. Yoshida, Y., Nakano, Y., Nezu, T., Yamashita, Y. and Koga, T. A novel NDP-6-deoxyhexosyl-4-ulose reductase in the pathway for the synthesis of thymidine diphosphate-D-fucose. J. Biol. Chem. 274 (1999) 16933-16939. [Medline UI: 99287888]
Recommended name: nucleoside oxidase
Reaction: inosine + O2 = 9-riburonosylhypoxanthine + H2O
Systematic name: nucleoside:oxygen 5'-oxidoreductase
Comments: Other purine and pyrimidine nucleosides (as well as 2'-deoxynucleosides) are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps:
(1) 2 inosine + O2 = 2 5'-dehydroinosine + 2 H2O;
(2) 2 5'-dehydroinosine + O2 = 2 9-riburonosylhypoxanthine + 2 H2O
with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.39, nucleoside oxidase (H2O2-forming), as it produces water rather than hydrogen peroxide.
References:
1. Isono, Y., Sudo, T. and Hoshino, M. Purification and reaction of a new enzyme, nucleoside oxidase. Agric. Biol. Chem. 53 (1989) 1663-1669.
2. Isono, Y., Sudo, T. and Hoshino, M. Properties of a new enzyme, nucleoside oxidase, from Pseudomonas maltophilia LB-86. Agric. Biol. Chem. 53 (1989) 1671-1677.
Recommended name: nucleoside oxidase (H2O2-forming)
Reaction: adenosine + 2 O2 = 9-riburonosyladenine + 2 H2O2
Systematic name: nucleoside:oxygen 5'-oxidoreductase (H2O2-forming)
Comments: A heme-containing flavoprotein (FAD). Other purine and pyrimidine nucleosides (as well as 2'-deoxynucleosides and arabinosides) are substrates, but ribose and nucleotides are not substrates. The overall reaction takes place in two separate steps:
(1) adenosine + O2 = 5'-dehydroadenosine + H2O2
(2) 5'-dehydroadenosine + O2 = 9-riburonosyladenine + H2O2
with the 5'-dehydro nucleoside being released from the enzyme to serve as substrate for the second reaction. This enzyme differs from EC 1.1.3.28, nucleoside oxidase, as it produces hydrogen peroxide rather than water.
References:
1. Koga, S., Ogawa, J., Cheng, L.Y., Choi, Y.M., Yamada, H. and Shimizu, S. Nucleoside oxidase, a hydrogen peroxide-forming oxidase, from Flavobacterium meningosepticum. Appl. Environ. Microbiol. 63 (1997) 4282-4286.
Recommended name: zeatin reductase
Reaction: dihydrozeatin + NADP = zeatin + NADPH2
Glossary:
zeatin
Systematic name: dihydrozeatin:NADP oxidoreductase
Comments: Previously classified erroneously as EC 1.1.1.242.
References:
1. Martin, R.C., Mok, M.C., Shaw, G. and Mok, D.W.S. An enzyme mediating the conversion of zeatin to dihydrozeatin in Phaseolus embryos. Plant Physiol. 90 (1989) 1630-1635.
Recommended name: biphenyl 2,3-dioxygenase
Reaction: biphenyl + NADH2 + O2 = (2R,3S)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD
For reaction pathway click here.
Other name(s): biphenyl dioxygenase
Systematic name: biphenyl,NADH2:oxygen oxidoreductase (2,3-hydroxylating)
Comments: Requires Fe2+. The enzyme from Pseudomonas sp. strain LB400 is part of a multicomponent system composed of an NADH:ferredoxin oxidoreductase (FAD cofactor), a [2Fe-2S] Rieske-type ferredoxin, and a terminal oxygenase that contains a [2Fe-2S] Rieske-type iron-sulfur cluster and a catalytic mononuclear nonheme iron centre. Chlorine-substituted biphenyls can also act as substrates. Similar to the three-component enzyme systems EC 1.14.12.3 (benzene 1,2-dioxygenase) and EC 1.14.12.11 (toluene dioxygenase).
References:
1. Haddock, J.D. and Gibson, D.T. Purification and characterization of the oxygenase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400. J. Bacteriol. 177 (1995) 5834-5839. [Medline UI: 96011369]
2. Haddock, J.D., Pelletier, D.A. and Gibson, D.T. Purification and properties of ferredoxinBPH, a component of biphenyl 2,3-dioxygenase of Pseudomonas sp. strain LB400. J. Indust. Microbiol. Biotechnol. 19 (1997) 355-359. [Medline UI: 98113813]
3. Broadus, R.M. and Haddock, J.D. Purification and characterization of the NADH:ferredoxinBPH oxidoreductase component of biphenyl 2,3-dioxygenase from Pseudomonas sp. strain LB400. Arch. Microbiol. 170 (1998) 106-112. [Medline UI: 98350019]
Recommended name: choline monooxygenase
Reaction: choline + 2 reduced ferredoxin + O2 = betaine aldehyde + 2 oxidized ferredoxin + H2O
Glossary
betaine: N,N,N-trimethylammonioacetate
betaine aldehyde: N,N,N-trimethyl-2-oxoethylammonium
choline: (2-hydroxyethyl)trimethylammonium
Systematic name: choline,reduced-ferredoxin:oxygen oxidoreductase
Comments: Requires Mg2+ and contains a Rieske-type [2Fe-2S] cluster. Catalyses the first step of glycine betaine synthesis in plants, where it is found in the chloroplast.
References:
1. Brouquisse, R., Weigel, P., Rhodes, D., Yocum, C.F. and Hanson, A.D. Evidence for a ferredoxin-dependent choline monooxygenase from spinach chloroplast stroma. Plant Physiol. 90 (1989) 322-329.
2. Burnet, M., Lafontaine, P.J. and Hanson, A.D. Assay, purification, and partial characterization of choline monooxygenase from spinach. Plant Physiol. 108 (1995) 581-588.
3. Rathinasabapathi, B., Burnet, M., Russell, B.L., Gage, D.A., Liao, P., Nye, G.J., Scott, P., Golbeck, J.H. and Hanson, A.D. Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: Prosthetic group characterization and cDNA cloning. Proc. Natl. Acad. Sci. USA 94 (1997) 3454-3458. [Medline UI: 97250559]
4. Russell, B.L., Rathinasabapathi, B. and Hanson, A.D. Osmotic stress induces expression of choline monooxygenase in sugar beet and amaranth. Plant Physiol. 116 (1998) 859-865. [Medline UI: 98150283]
5. Nuccio, M.L., Russell, B.L., Nolte, K.D., Rathinasabapathi, B., Gage, D.A. and Hanson, A.D. The endogenous choline supply limits glycine betaine synthesis in transgenic tobacco expressing choline. Plant J. 16 (1998) 487-496. [Medline UI: 99097843]
Recommended name: glucosamine-1-phosphate N-acetyltransferase
Reaction: acetyl-CoA + D-glucosamine 1-phosphate = CoA + N-acetyl-D-glucosamine 1-phosphate
Systematic name: acetyl-CoA:D-glucosamine-1-phosphate N-acetyltransferase
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 2.7.7.23, UDP-N-acetylglucosamine diphosphorylase.
References:
1. Mengin-Lecreulx, D. and van Heijenoort, J. Copurification of glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyltransferase activities of Escherichia coli: characterization of the glmU gene product as a bifunctional enzyme catalyzing two subsequent steps in the pathway for UDP-N-acetylglucosamine synthesis. J. Bacteriol. 176: (1994) 5788-5795. [Medline UI: 94364959]
Recommended name: 1,3-β-galactosyl-N-acetylhexosamine phosphorylase
Reaction: β-D-galactopyranosyl-(13)-N-acetyl-D-glucosamine + phosphate = α-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
Systematic name: β-D-galactopyranosyl-(13)-N-acetyl-D-hexosamine:phosphate galactosyltransferase
Comments: Reaction also occurs with β-D-galactopyranosyl-(13)-N-acetyl-D-galactosamine as the substrate, giving N-acetyl-D-galactosamine as the product.
References:
1. Derensy-Dron, D., Krzewinski, F., Brassart, C. and Bouquelet S. β-1,3-Galactosyl-N-acetylhexosamine phosphorylase from Bifidobacterium bifidum DSM 20082: characterization, partial purification and relation to mucin degradation. Biotechnol. Appl. Biochem. 29 (1999) 3-10. [Medline UI: 99173770]
Recommended name: homospermidine synthase
Reaction: 2 putrescine = sym-homospermidine + NH3
For reaction pathway click here.
Glossary
sym-homospermidine: N-(4-aminobutyl)butane-1,4-diamine
putrescine: butane-1,4-diamine
Systematic name: putrescine:putrescine 4-aminobutyltransferase (ammonia-forming)
Comments: The reaction of this enzyme occurs in three steps: (i) NAD-dependent dehydrogenation of putrescine, (ii) transfer of the 4-aminobutylidene group from dehydroputrescine to a second molecule of putrescine, (iii) reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. In the presence of putrescine, spermidine can function as a donor of the aminobutyl group, in which case, propane-1,3-diamine is released instead of ammonia. Differs from EC 2.5.1.45, homospermidine synthase (spermidine-specific), which cannot use putrescine as donor of the aminobutyl group.
References:
1. Tait, G.H. The formation of homospermidine by an enzyme from Rhodopseudomonas viridis. Biochem. Soc. Trans. 7 (1979) 199-200. [Medline UI: 79170251]
2. Böttcher, F., Ober, D. and Hartmann, T. Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation. Can. J. Chem. 72 (1994) 80-85.
3. Yamamoto, S., Nagata, S. and Kusaba, K. Purification and characterization of homospermidine synthase in Acinetobacter tartarogens ATCC 31105. J. Biochem. 114 (1993) 45-49. [Medline UI: 94012579]
4. Srivenugopal, K.S. and Adiga, P.R. Enzymatic synthesis of sym-homospermidine in Lathyrus sativus T (grass pea) seedlings. Biochem. J. 190 (1980) 461-464. [Medline UI: 81133501]
5. Ober, D., Tholl, D., Martin, W. and Hartmann, T. Homospermidine synthase of Rhodopseudomonas viridis: Substrate specificity and effects of the heterologously expressed enzyme on polyamine metabolism of Escherichi coli. J. Gen. Appl. Microbiol. 42 (1996) 411-419.
6. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [Medline UI: 20079558]
Recommended name: homospermidine synthase (spermidine-specific)
Reaction: spermidine + putrescine = sym-homospermidine + propane-1,3-diamine
For reaction pathway click here.
Glossary
sym-homospermidine: N-(4-aminobutyl)butane-1,4-diamine
putrescine: butane-1,4-diamine
spermidine: N-(3-aminopropyl)butane-1,4-diamine
Systematic name: spermidine:putrescine 4-aminobutyltransferase (propane-1,3-diamine-forming)
Comments: The reaction of this enzyme occurs in three steps: (i) NAD-dependent dehydrogenation of spermidine, (ii) transfer of the 4-aminobutylidene group from dehydrospermidine to putrescine, (iii) reduction of the imine intermediate to form homospermidine. Hence the overall reaction is transfer of a 4-aminobutyl group. This enzyme is more specific than EC 2.5.1.44, homospermidine synthase, which is found in bacteria, as it cannot use putrescine as donor of the 4-aminobutyl group. Forms part of the biosynthetic pathway of the poisonous pyrrolizidine alkaloids of the ragworts (Senecio).
References:
1. Böttcher, F., Ober, D. and Hartmann, T. Biosynthesis of pyrrolizidine alkaloids: putrescine and spermidine are essential substrates of enzymatic homospermidine formation. Can. J. Chem. 72 (1994) 80-85.
2. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved from deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [Medline UI: 20079558]
3. Ober, D., Harms, R. and Hartmann, T. Cloning and expression of homospermidine synthase from Senecio vulgaris: a revision. Phytochemistry 55 (2000) 311-316.
Recommended name: deoxyhypusine synthase
Reaction: [eIF5A-precursor]-lysine + spermidine = [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine
For reaction pathway click here.
Glossary
deoxyhypusine: N6-(4-aminobutyl)lysine
hypusine: N6-(4-amino-2-hydroxybutyl)lysine
spermidine: N-(3-aminopropyl)butane-1,4-diamine
Systematic name: spermidine:eIF5A-lysine 4-aminobutyltransferase (propane-1,3-diamine-forming)
Comments: The eukaryotic initiation factor eIF5A contains a hypusine residue that is essential for activity. This enzyme catalyses the first reaction of hypusine formation from one specific lysine residue of the eIF5A precursor, the second reaction being catalysed by EC 1.14.99.29, deoxyhypusine monooxygenase. The reaction of this enzyme occurs in four steps: (i) NAD-dependent dehydrogenation of spermidine, (ii) formation of an enzyme-imine intermediate by transfer of the 4-aminobutylidene group from dehydrospermidine to the active site lysine residue (Lys329 for the human enzyme), (iii) transfer of the same 4-aminobutylidene group from the enzyme intermediate to the e1F5A precursor, (iv) reduction of the e1F5A-imine intermediate to form a deoxyhypusine residue. Hence the overall reaction is transfer of a 4-aminobutyl group. For the plant enzyme, homospermidine can substitute for spermidine and putrescine can substitute for the lysine residue of the eIF5A precursor.
References:
1. Wolff, E.C., Park, M.H. and Folk, J.E. Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD+. J. Biol. Chem. 265 (1990) 4793-4799. [Medline UI: 90202924]
2. Wolff, E.C., Folk, J.E. and Park, M.H. Enzyme-substrate intermediate formation at lysine 329 of human deoxyhypusine synthase. J. Biol. Chem. 272 (1997) 15865-15871. [Medline UI: 97332674]
3. Chen, K.Y. and Liu, A.Y.C. Biochemistry and function of hypusine formation on eukaryotic initiation factor 5A. Biol. Signals 6 (1997) 105-109. [Medline UI: 97430993]
4. Ober, D. and Hartmann, T. Deoxyhypusine synthase from tobacco. cDNA isolation, characterization, and bacterial expression of an enzyme with extended substrate specificity. J. Biol. Chem. 274 (1999) 32040-32047. [Medline UI: 20011401]
5. Ober, D. and Hartmann, T. Homospermidine synthase, the first pathway-specific enzyme of pyrrolizidine alkaloid biosynthesis, evolved form deoxyhypusine synthase. Proc. Natl. Acad. Sci. USA 96 (1999) 14777-14782. [Medline UI: 20079558]
6. Wolff, E.C. and Park, M.H. Identification of lysine350 of yeast deoxyhypusine synthase as the site of enzyme intermediate formation. Yeast 15 (1999) 43-50. [Medline UI: 99152510]
7. Wolff, E.C., Wolff. J. and Park, M.H. Deoxyhypusine synthase generates and uses bound NADH in a transient hydride transfer mechanism. J. Biol. Chem. 275 (2000) 9170-9177. [Medline UI: 20200398]
8. Joe, Y.A., Wolff, E.C. and Park, M.H. Cloning and expression of human deoxyhypusine synthase cDNA: structure-function studies with the recombinant enzyme and mutant proteins. J. Biol. Chem. 270 (1995) 22386-22392. [Medline UI: 95403436]
9. Tao, Y. and Chen, K.Y. Molecular cloning and functional expression of Neurospora deoxyhypusine synthase cDNA and identification of yeast deoxyhypusine synthase cDNA. J. Biol. Chem. 270 (1995) 23984-23987. [Medline UI: 96025775]
Recommended name: 2-aminoethylphosphonate-pyruvate transaminase
Reaction: (2-aminoethyl)phosphonate + pyruvate = 2-phosphonoacetaldehyde + L-alanine
Other name(s): (2-aminoethyl)phosphonate transaminase; (2-aminoethyl)phosphonate aminotransferase; (2-aminoethyl)phosphonic acid aminotransferase; 2-aminoethylphosphonate-pyruvate aminotransferase; 2-aminoethylphosphonate aminotransferase
Systematic name: (2-aminoethyl)phosphonate:pyruvate aminotransferase
Comments: A pyridoxal-phosphate protein. 2-Aminoethylarsonate can replace 2-aminoethylphosphonate as a substrate.
References:
1. La Nauze, J.M. and Rosenberg, H. The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus. Biochim. Biophys. Acta 165 (1968) 438-447. [Medline UI: 70056996]
2. Dumora, C., Lacoste, A.-M. and Cassaigne, A. Purification and properties of 2-aminoethylphosphonate:pyruvate aminotransferase from Pseudomonas aeruginosa. Eur. J. Biochem. 133 (1983) 119-125. [Medline UI: 83209625]
3. Lacoste, A.-M., Dumora, C., Balas, L., Hammerschmidt, F. and Vercauteren, J. Stereochemistry of the reaction catalysed by 2-aminoethylphosphonate aminotransferase. A 1H-NMR study. Eur. J. Biochem. 215 (1993) 841-844. [Medline UI: 93358911]
4. Lacoste, A.-M., Dumora, C., Ali, B.R.S., Neuzil, E. and Dixon, H.B.F. Utilization of 2-aminoethylarsonic acid in Pseudomonas aeruginosa. J. Gen. Microbiol. 138 (1992) 1283-1287. [Medline UI: 92407501]
Recommended name: deoxynucleoside kinase
Reaction: ATP + 2'-deoxynucleoside = ADP + 2'-deoxynucleoside 5'-phosphate
Other names: multispecific deoxynucleoside kinase; ms-dNK; multisubstrate deoxyribonculeoside kinase; multifunctional deoxynucleoside kinase; D. melanogaster deoxynucleoside kinase; Dm-dNK
Systematic name: ATP:deoxynucleoside 5'-phosphotransferase
Comments: The enzyme from embryonic cells of Drosophila melanogaster differs from other deoxynucleoside kinases [EC 2.7.1.76 (deoxyadenosine kinase) and EC 2.7.1.113 (deoxyguanosine kinase)] in its broad specificity for all four common deoxynucleosides.
References:
1. Munch-Petersen, B., Piskur, J. and Søndergaard, L. Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase. J. Biol. Chem. 273 (1998) 3926-3931. [Medline UI: 98129796]
2. Munch-Petersen, B., Knecht, W., Lenz, C., Søndergaard, L. and Piskur, J. Functional expression of a multisubstrate deoxyribonculeoside kinase from Drosophila melanogaster and its C-terminal deletion. J. Biol. Chem. 275 (2000) 6673-6679. [Medline UI: 20158988]
*EC 3.2.1 Glycosidases, i.e. enzymes hydrolysing O- and S-glycosyl compounds
Recommended name: galactan 1,3-β-galactosidase
Reaction: Hydrolysis of terminal, non-reducing β-D-galactose residues in (13)-β-D-galactopyranans
Systematic name: galactan (13)-β-D-galactosidase
Comments: This enzyme removes not only free galactose, but also 6-glycosylated residues, e.g., (16)-β-D-galactobiose, and galactose bearing oligosaccharide chains on O-6. Hence, it releases branches from [arabino-galacto-(16)]-(13)-β-D-galactans.
References:
1. Tsumuraya, Y., Mochizuki, N., Hashimoto Y. and Kovac, P. Purification of exo-(13)-D-galactanase of Irpex lacteus (Polyporus tulipiferae) and its action on arabinogalactan-proteins. J. Biol. Chem. 265 (1990) 7207-7215. [Medline UI: 90237010]
2. Pellerin, P. and Brillouet, J.M. Purification and properties of an exo-(13)-β-D-galactanase from Aspergillus niger. Carbohydr. Res. 264 (1994) 281-291. [Medline UI: 95103561]
Recommended name: β-galactofuranosidase
Reaction: Hydrolysis of terminal non-reducing β-D-galactofuranosides, releasing galactose.
Other name(s): exo-β-galactofuranosidase; exo-β-D-galactofuranosidase; β-D-galactofuranosidase
Systematic name: β-D-galactofuranoside hydrolase
Comments: The enzyme from Helminthosporium sacchari detoxifies helminthosporoside, a bis(digalactosyl)terpene produced by this fungus, by releasing its four molecules of bound galactose.
References:
1. Rietschel-Berst, M., Jentoft, N.H., Rick, P.D., Pletcher, C., Fang, F. and Gander, J.E. Extracellular exo-β-galactofuranosidase from Penicillium charlesii: isolation, purification, and properties. J. Biol. Chem. 252 (1977) 3219-3226. [Medline UI: 77187789]
2. Daley, L.S. and Strobel, G.A. β-Galactofuranosidase activity in Helminthosporium sacchari and its relationship to the production of helminthosporoside. Plant Sci. Lett. 30 (1983) 145-154.
3. Cousin, M.A., Notermans, S., Hoogerhout, P. and Van Boom, J.H. Detection of β-galactofuranosidase production by Penicillium and Aspergillus species using 4-nitrophenyl β-D-galactofuranoside. J. Appl. Bacteriol. 66 (1989) 311-317. [Medline UI: 89327086]
4. Miletti , L.C., Marino, C., Marino, K., de Lederkremer, R.M., Colli, W. and Alves, M.J.M. Immobilized 4-aminophenyl-1-thio-β-D-galactofuranoside as a matrix for affinity purification of an exo-β-D-galactofuranosidase. Carbohydr. Res. 320 (1999) 176-182.
Recommended name: thioglucosidase
Reaction: H2O + a thioglucoside = a sugar + a thiol
Other name(s): myrosinase; sinigrinase; sinigrase
Systematic name: thioglucoside glucohydrolase
Comments: Has a wide specificity for thioglycosides.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9025-38-1
References:
1. Goodman, I., Fouts, J.R., Bresnick, E., Menegas, R. and Hitchings, G.H. A mammalian thioglucosidase. Science 130 (1959) 450-451.
2. Pigman, W.W. Action of almond emulsin on the phenyl glucosides of synthetic sugars and on β-thiophenyl d-glucoside. J. Res. Nat. Bur. Stand. 26 (1941) 197-204.
Recommended name: ribosylhomocysteinase
Reaction: H2O + S-ribosyl-L-homocysteine = D-ribose + L-homocysteine
Systematic name: S-ribosyl-L-homocysteine ribohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 37288-63-4
References:
1. Duerre, J.A. and Miller, C.H. Cleavage of S-ribosyl-L-homocysteine by extracts from Escherichia coli. J. Bacteriol. 91 (1966) 1210-1217. [Medline UI: 66120927]
[EC 3.2.3.1 Transferred entry: now EC 3.2.1.147 thioglucosidase (EC 3.2.3.1 created 1972, deleted 2001)]
*EC 3.3.1 Trialkylsulfonium Hydrolases
[EC 3.3.1.3 Transferred entry: now EC 3.2.1.148 ribosylhomocysteinase (EC 3.3.1.3 created 1972, deleted 2001)]
Recommended name: limonene-1,2-epoxide hydrolase
Reaction: limonene-1,2-epoxide + H2O = limonene-1,2-diol
Glossary:
limonene: a monoterpenoid
Other name(s): limonene oxide hydrolase
Systematic name: limonene-1,2-epoxide hydrolase
Comment: Involved in the monoterpene degradation pathway of the actinomycete Rhodococcus erythropolis. Enzyme hydrolyses several alicyclic and 1-methyl-substituted epoxides, such as 1-methylcyclohexene oxide, indene oxide and cyclohexene oxide. It differs from the previously described epoxide hydrolases [EC 3.3.2.3 (epoxide hydrolase), EC 3.3.2.4 (trans-epoxysuccinate hydrolase), EC 3.3.2.6 (leukotriene-A4 hydrolase) and EC 3.3.2.7 (hepoxilin-epoxide hydrolase)] as it is not inhibited by 2-bromo-4'-nitroacetophenone, diethyl pyrocarbonate, 4-fluorochalcone oxide or 1,10-phenanthroline.
References:
1. van der Werf, M.J., Overkamp, K.M. and de Bont, J.A.M. Limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis DCL14 belongs to a novel class of epoxide hydrolases. J. Bacteriol. 180 (1998) 5052-5057. [Medline UI: 98422456]
2. Barbirato, F., Verdoes, J.C., de Bont, J.A.M. and van der Werf, M.J. The Rhodococcus erythropolis DCL14 limonene-1,2-epoxide hydrolase gene encodes an enzyme belonging to a novel class of epoxide hydrolases. FEBS Lett. 438 (1998) 293-296. [Medline UI: 99043266]
Recommended name: maleimide hydrolase
Reaction: maleimide + H2O = maleamic acid
Other name(s): imidase; cyclic imide hydrolase
Systematic name: cyclic-imide amidohydrolase (decyclicizing)
Comment: Succinimide and glutarimide, and sulfur-containing cyclic imides, such as rhodanine, can also act as substrates for the enzyme from Blastobacter sp. A17p-4. The reverse, cyclization, reaction is also catalysed, but much more slowly. It has lower activity towards cyclic ureides, which are the substrates of EC 3.5.2.2, dihydropyrimidinase.
References:
1. Ogawa, J., Soong, C.L., Honda, M. and Shimizu, S. Imidase, a new dihydropyrimidinase-like enzyme involved in the metabolism of cyclic imides. Eur. J. Biochem. 243 (1997) 322-327. [Medline UI: 97182616]
Recommended name: phosphonoacetaldehyde hydrolase
Reaction: phosphonoacetaldehyde + H2O = acetaldehyde + phosphate
Other name(s): phosphonatase
Systematic name: 2-oxoethylphosphonate phosphonohydrolase
Comments: This enzyme destabilizes the C-P bond, by forming an imine between one of its lysine residues and the carbonyl group of the substrate, thus allowing this, normally stable, bond to be broken. The mechanism is similar to that used by EC 4.1.2.13, fructose-bisphosphate aldolase, to break a C-C bond.
References:
1. La Nauze, J.M. and Rosenberg, H. The identification of 2-phosphonoacetaldehyde as an intermediate in the degradation of 2-aminoethylphosphonate by Bacillus cereus. Biochim. Biophys. Acta 165 (1968) 438-447. [Medline UI: 70056996]
2. La Nauze, J.M., Rosenberg, H. and Shaw, D.C. The enzymic cleavage of the carbon-phosphorus bond: purification and properties of phosphonatase. Biochim. Biophys. Acta 212 (1970) 332-350. [Medline UI: 70275154]
3. La Nauze, J.M., Coggins, J.R. and Dixon, H.B.F. Aldolase-like imine formation in the mechanism of action of phosphonoacetaldehyde hydrolase. Biochem. J. 165 (1977) 409-411. [Medline UI: 78039850]
4. Olsen, D.B., Hepburn, T.W., Moos, M., Mariano, P.S. and Dunaway-Mariano, D. Substrate binding and catalytic groups of the P-C bond cleaving enzyme, phosphonoacetaldehyde hydrolase. Biochemistry 27 (1988) 2229-2234. [Medline UI: 88241058]
5. Baker, A.S., Ciocci, M.J., Metcalf, W.W., Kim, J., Babbitt, P.C., Wanner, B.L., Martin, B.M. and Dunaway-Mariano, D. Insights into the mechanism of catalysis by the P-C bond-cleaving enzyme phosphonoacetaldehyde hydrolase derived from gene sequence analysis and mutagenesis. Biochemistry 37 (1998) 9305-9315. [Medline UI: 98313265]
Recommended name: cyclohexa-1,5-dienecarbonyl-CoA hydratase
Reaction: cyclohexa-1,5-dienecarbonyl-CoA + H2O = 6-hydroxycyclohex-1-enecarbonyl-CoA
Other names: cyclohexa-1,5-diene-1-carbonyl-CoA hydratase; dienoyl-CoA hydratase
Systematic name: cyclohexa-1,5-dienecarbonyl-CoA hydro-lyase
Comments: Forms part of the anaerobic benzoate degradation pathway, which also includes EC 1.3.99.7 (glutaryl-CoA dehydrogenase), EC 1.3.99.15 (benzoyl-CoA reductase) and EC 4.2.1.55 (3-hydroyxbutyryl-CoA dehydratase).
Links to other databases: BRENDA, EXPASY, KEGG, UM-BBD, WIT, CAS registry number:
References:
1. Laempe, D., Eisenreich, W., Bacher, A. and Fuchs, G. Cyclohexa-1,5-diene-1-carboxyl-CoA hydratase, an enzyme involved in anaerobic metabolism of benzoyl-CoA in the denitrifying bacterium Thauera aromatica. Eur. J. Biochem. 255 (1998) 618-627. [Medline UI: 98409281] [Erratum Eur. J. Biochem. 257 (1998) 528 only]
2. Harwood, C.S. and Gibson, J. Shedding light on anaerobic benzene ring degradation: a process unique to prokaryotes? J. Bacteriol. 179 (1997) 301-309. [Medline UI: 97144512]
3. Koch, J., Eisenreich, W., Bacher, A. and Fuchs, G. Products of enzymatic reduction of benzoyl-CoA, a key reaction in anaerobic aromatic metabolism. Eur. J. Biochem. 211 (1993) 649-661. [Medline UI: 93170297]
[EC 4.2.1.102 Transferred entry: now EC 4.2.1.100 cyclohexa-1,5-diene-1-carbonyl-CoA hydratase (EC 4.2.1.102 created 2001, deleted 2001)]
Recommended name: phosphoglucosamine mutase
Reaction: D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Systematic name: D-glucosamine 1,6-phosphomutase
Comments: The enzyme is involved in the pathway for bacterial cell-wall peptidoglycan and lipopolysaccharide biosyntheses, being an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis. The enzyme from E. coli is activated by phosphorylation and can be autophosphorylated in vitro by glucosamine 1,6-bisphosphate, which is an intermediate in the reaction, glucose 1,6-bisphosphate or ATP. It can also catalyse the interconversion of glucose 1-phosphate and glucose 6-phosphate, although at a much lower rate.
References:
1. Mengin-Lecreulx, D. and van Heijenoort, J. Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. J. Biol. Chem. 271 (1996) 32-39. [Medline UI: 96132879]
2. de Reuse, H., Labigne, A. and Mengin-Lecreulx, D. The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase. J. Bacteriol. 179 (1997) 3488-3493. [Medline UI: 97315217]
3. Jolly, L., Wu, S., van Heijenoort, J., de Lencastre, H., Mengin-Lecreulx, D. and Tomas, A. The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase. J. Bacteriol. 179 (1997) 5321-5325. [Medline UI: 97431478]
4. Jolly, L., Ferrari, P., Blanot, D., van Heijenoort, J., Fassy, F. and Mengin-Lecreulx, D. Reaction mechanism of phosphoglucosamine mutase from Escherichia coli. Eur. J. Biochem. 262 (1999) 202-210. [Medline UI: 99248083]
5. Jolly, L., Pompeo, F., van Heijenoort, J., Fassy, F. and Mengin-Lecreulx, D. Autophosphorylation of phosphoglucosamine mutase from Escherichia coli. J. Bacteriol. 182 (2000) 1280-1285. [Medline UI: 20138152]
Recommended name: inositol-3-phosphate synthase
Reaction: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Other name(s): myo-inositol-1-phosphate synthase
Systematic name: 1L-myo-inositol-1-phosphate lyase (isomerizing)
Comments: Requires NAD, which dehydrogenates the -CHOH- group to -CO- at C-5 of the glucose 6-phosphate, making C-6 into an active methylene, able to condense with the -CHO at C-1. Finally, the enzyme-bound NADH2 reconverts C-5 into the -CHOH- form.
Links to other databases: BRENDA, EXPASY, KEGG, WIT, CAS registry number: 9032-95-5
References:
1. Eisenberg, P., Jr. D-myo-Inositol 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. [Medline UI: 67135042]
2. Sherman, W.R., Stewart, M.A. and Zinbo, M. Mass spectrometric study on the mechanism of D-glucose 6-phosphate-L-myo-inositol 1-phosphate cyclase. J. Biol. Chem. 244 (1969) 5703-5708. [Medline UI: 70027328]
3. Barnett, J.E.G. and Corina, D.L. The mechanism of glucose 6-phosphate-D-myo-inositol 1-phosphate cyclase of rat testis. The involvement of hydrogen atoms. Biochem. J. 108 (1968) 125-129. [Medline UI: 68310248]
4. Barnett, J.E.G., Rasheed, A. and Corina, D.L. Partial reactions of glucose 6-phosphate-1L-myo-inositol 1-phosphate cyclase. Biochem. J. 131 (1973) 21-30. [Medline UI: 73228139]
The product should be (1R,2S)-1,2-dihydronaphthalene-1,2-diol [not (1S,2S)-].
EC 1.14.12.13 CO2 is also produced in the reaction.
EC 3.1.11.1-4, EC 3.1.11.6, EC 3.1.13.3, EC 3.1.15.1
The product should be nucleoside 5'-phosphates [not 5'-phosphomononucleotides].
EC 3.1.13.1
The product should be nucleoside 5'-phosphates [not 3'-phosphomononucleotides].
EC 3.1.14.1, EC 3.1.16.1, EC 3.1.22.1-2, EC 3.1.27.1, EC 3.1.27.3-6, EC 3.1.31.1
The product should be nucleoside 3'-phosphates [not 3'-phosphomononucleotides].
EC 3.6.1.31
The reaction and sytematic name change phosphoribosyl to 1-(5-phosphoribosyl).
EC 4.2.3.12
Reactant correct spelling to 6-(L-erythro-1,2-dihydroxypropyl 3-triphosphate)-7,8-dihydropterin
Systematic name correct to 2-amino-4-oxo-6-(erythro-1',2',3'-trihydroxypropyl)-7,8-dihydroxypteridine triphosphate lyase
EC 5.4.99.11
Reference 2 date corrected to 1982.