EC |
3.2.1.124 |
Accepted name: |
3-deoxy-2-octulosonidase |
Reaction: |
Endohydrolysis of the β-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonate in capsular polysaccharides |
Other name(s): |
2-keto-3-deoxyoctonate hydrolase; octulosylono hydrolase; octulofuranosylono hydrolase; octulopyranosylonohydrolase |
Systematic name: |
capsular-polysaccharide 3-deoxy-D-manno-2-octulosonohydrolase |
Comments: |
The enzyme from a bacteriophage catalyses the depolymerization of capsular polysaccharides containing 3-deoxy-2-octulosonide in the cell wall of Escherichia coli. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 103171-48-8 |
References: |
1. |
Altmann, F., Kwiatkowski, B., Stirm, S., März, L. and Unger, F.M. A bacteriophage-associated glycanase cleaving β-pyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid (KDO). Biochem. Biophys. Res. Commun. 136 (1986) 329–335. [DOI] [PMID: 3707579] |
|
[EC 3.2.1.124 created 1989] |
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|
|
|
EC |
3.2.1.144 |
Accepted name: |
3-deoxyoctulosonase |
Reaction: |
3-deoxyoctulosonyl-lipopolysaccharide + H2O = 3-deoxyoctulosonic acid + lipopolysaccharide |
Other name(s): |
α-Kdo-ase |
Systematic name: |
3-deoxyoctulosonyl-lipopolysaccharide hydrolase |
Comments: |
Releases Kdo (α- and β-linked 3-deoxy-D-manno-octulosonic acid) from different lipopolysaccharides, including Re-LPS from Escherichia coli and Salmonella, Rd-LPS from S. minnesota, and de-O-acyl-re-LPS. 4-Methylumbelliferyl-α-Kdo (α-Kdo-OMec) is also a substrate. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 199128-67-1 |
References: |
1. |
Li, Y.T., Wang, L.X., Pavlova, N.V., Li, S.C. and Lee, Y.C. α-KDOase activity in oyster and synthesis of α- and β-4-methylumbelliferyl ketosides of 3-deoxy-D-manno-octulosonic acid (KDO). J. Biol. Chem. 272 (1997) 26419–26424. [DOI] [PMID: 9334217] |
|
[EC 3.2.1.144 created 2000] |
|
|
|
|
EC |
3.4.19.9 |
Accepted name: |
folate γ-glutamyl hydrolase |
Reaction: |
tetrahydropteroyl-(γ-glutamyl)n + (n-1) H2O = 5,6,7,8-tetrahydrofolate + (n-1) L-glutamate |
|
For diagram of folate biosynthesis (late stages), click here |
Other name(s): |
GGH (gene name); conjugase; folate conjugase; lysosomal γ-glutamyl carboxypeptidase; γ-Glu-X carboxypeptidase; pteroyl-poly-γ-glutamate hydrolase; carboxypeptidase G; folic acid conjugase; poly(γ-glutamic acid) endohydrolase; polyglutamate hydrolase; poly(glutamic acid) hydrolase II; pteroylpoly-γ-glutamyl hydrolase; γ-glutamyl hydrolase |
Systematic name: |
tetrahydropteroyl-poly-γ-glutamyl γ-glutamyl hydrolase |
Comments: |
The enzyme, which occurs only in animals and plants, can be either endo- and/or exopeptidase. It acts on tetrahydropteroyl polyglutamates and their modified forms, as well as the polyglutamates of the folate breakdown product N-(4-aminobenzoyl)-L-glutamate (pABA-Glu). The initial cleavage may release either monoglutamate or poly-γ-glutamate of two or more residues, depending on the specific enzyme. For example, GGH1 from the plant Arabidopsis thaliana cleaves pentaglutamates, mainly to di- and triglutamates, whereas GGH2 from the same organism yields mainly monoglutamates. The enzyme is lysosomal (and secreted) in animals and vacuolar in plants. In peptidase family C26. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9074-87-7 |
References: |
1. |
McGuire, J.J. and Coward, J.K. Pteroylpolyglutamates: biosynthesis, degradation and function.. In: Blakley, R.L. and Benkovic, S.J. (Ed.), Folates and Pterins, John Wiley and Sons, New York, 1984, pp. 135–191. |
2. |
Wang, Y., Nimec, Z., Ryan, T.J., Dias, J.A. and Galivan, J. The properties of the secreted γ-glutamyl hydrolases from H35 hepatoma cells. Biochim. Biophys. Acta 1164 (1993) 227–235. [DOI] [PMID: 8343522] |
3. |
Yao, R., Rhee, M.S. and Galivan, J. Effects of γ-glutamyl hydrolase on folyl and antifolylpolyglutamates in cultured H35 hepatoma cells. Mol. Pharmacol. 48 (1995) 505–511. [PMID: 7565632] |
4. |
Yao, R., Schneider, E., Ryan, T.J. and Galivan, J. Human γ-glutamyl hydrolase: cloning and characterization of the enzyme expressed in vitro. Proc. Natl. Acad. Sci. USA 93 (1996) 10134–10138. [DOI] [PMID: 8816764] |
5. |
Yao, R., Nimec, Z., Ryan, T.J. and Galivan, J. Identification, cloning, and sequencing of a cDNA coding for rat γ-glutamyl hydrolase. J. Biol. Chem. 271 (1996) 8525–8528. [DOI] [PMID: 8621474] |
6. |
Orsomando, G., de la Garza, R.D., Green, B.J., Peng, M., Rea, P.A., Ryan, T.J., Gregory, J.F., 3rd and Hanson, A.D. Plant γ-glutamyl hydrolases and folate polyglutamates: characterization, compartmentation, and co-occurrence in vacuoles. J. Biol. Chem. 280 (2005) 28877–28884. [PMID: 15961386] |
7. |
Akhtar, T.A., McQuinn, R.P., Naponelli, V., Gregory, J.F., 3rd, Giovannoni, J.J. and Hanson, A.D. Tomato γ-glutamylhydrolases: expression, characterization, and evidence for heterodimer formation. Plant Physiol. 148 (2008) 775–785. [PMID: 18757550] |
|
[EC 3.4.19.9 created 1972 as EC 3.4.12.10, transferred 1978 to EC 3.4.22.12, transferred 1992 to EC 3.4.19.9, modified 1997, modified 2018] |
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|
|
|
EC |
3.4.21.97 |
Accepted name: |
assemblin |
Reaction: |
Cleaves -Ala┼Ser- and -Ala┼Ala- bonds in the scaffold protein |
Comments: |
Involved in the breakdown of the scaffold protein during the late stages of assembly of the herpes-virus virion. Inhibited by diisopropyl fluorophosphate. Type example of peptidase family S21. Catalytic residues are His, Ser, His, a combination not known for any other peptidase, and the protein fold also is unique. Known from herpes viruses of several types, cytomegalovirus, Epstein-Barr virus and human herpesvirus 3 |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 139691-88-6 |
References: |
1. |
Chen, P., Tsuge, H., Almassy, R.J., Gribskov, C.L., Katoh, S., Vanderpool, D.L., Margosiak, S.A., Pinko, C., Matthews, D.A. and Kan, C.C. Structure of the human cytomegalovirus protease catalytic domain reveals a novel serine protease fold and catalytic triad. Cell 86 (1996) 477–483. [DOI] [PMID: 8797829] |
2. |
Darke, P.L. Herpesvirus assemblin. In: Barrett, A.J., Rawlings, N.D. and Woessner, J.F. (Ed.), Handbook of Proteolytic Enzymes, Academic Press, London, 1998, pp. 470–472. |
|
[EC 3.4.21.97 created 2000] |
|
|
|
|
EC |
3.5.1.7 |
Accepted name: |
ureidosuccinase |
Reaction: |
N-carbamoyl-L-aspartate + H2O = L-aspartate + CO2 + NH3 |
Systematic name: |
N-carbamoyl-L-aspartate amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9024-81-1 |
References: |
1. |
Lieberman, I. and Kornberg, A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. III. Ureidosuccinase. J. Biol. Chem. 212 (1955) 909–920. [PMID: 14353892] |
|
[EC 3.5.1.7 created 1961] |
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|
|
|
EC |
3.5.1.29 |
Accepted name: |
2-(acetamidomethylene)succinate hydrolase |
Reaction: |
2-(acetamidomethylene)succinate + 2 H2O = acetate + succinate semialdehyde + NH3 + CO2 |
Other name(s): |
α-(N-acetylaminomethylene)succinic acid hydrolase |
Systematic name: |
2-(acetamidomethylene)succinate amidohydrolase (deaminating, decarboxylating) |
Comments: |
Involved in the degradation of pyridoxin in Pseudomonas. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37289-09-1 |
References: |
1. |
Huynh, M.S. and Snell, E.E. Enzymes of vitamin B6 degradation. Purification and properties of two N-acetylamidohydrolases. J. Biol. Chem. 260 (1985) 2379–2383. [PMID: 3972793] |
2. |
Nyns, E.J., Zach, D. and Snell, E.E. The bacterial oxidation of vitamin B6. 8. Enzymatic breakdown of α-(N-acetylaminomethylene) succinic acid. J. Biol. Chem. 244 (1969) 2601–2605. [PMID: 5769993] |
|
[EC 3.5.1.29 created 1972] |
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|
|
EC |
3.5.2.3 |
Accepted name: |
dihydroorotase |
Reaction: |
(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate |
|
For diagram of pyrimidine biosynthesis, click here |
Other name(s): |
carbamoylaspartic dehydrase; dihydroorotate hydrolase |
Systematic name: |
(S)-dihydroorotate amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9024-93-5 |
References: |
1. |
Cooper, C. and Wilson, D.W. Biosynthesis of pyrimidines. Fed. Proc. 13 (1954) 194. |
2. |
Lieberman, I. and Kornberg, A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. II. Dihydroorotic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin. J. Biol. Chem. 207 (1954) 911–924. [PMID: 13163076] |
|
[EC 3.5.2.3 created 1961] |
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|
EC |
3.5.2.4 |
Accepted name: |
carboxymethylhydantoinase |
Reaction: |
L-5-carboxymethylhydantoin + H2O = N-carbamoyl-L-aspartate |
Other name(s): |
hydantoin hydrolase |
Systematic name: |
L-5-carboxymethylhydantoin amidohydrolase |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, CAS registry number: 9025-14-3 |
References: |
1. |
Lieberman, I. and Kornberg, A. Enzymatic synthesis and breakdown of a pyrimidine, orotic acid. II. Dihydroorotic acid, ureidosuccinic acid, and 5-carboxymethylhydantoin. J. Biol. Chem. 207 (1954) 911–924. [PMID: 13163076] |
|
[EC 3.5.2.4 created 1961] |
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|
|
EC |
3.7.1.8 |
Accepted name: |
2,6-dioxo-6-phenylhexa-3-enoate hydrolase |
Reaction: |
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate |
Other name(s): |
HOHPDA hydrolase |
Systematic name: |
2,6-dioxo-6-phenylhexa-3-enoate benzoylhydrolase |
Comments: |
Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase, by ring-fission at a -CO-C bond. Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp. |
Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 102925-38-2 |
References: |
1. |
Omori, T., Sugimura, K., Ishigooka, H. and Minoda, Y. Purification and some properties of a 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid hydrolyzing enzyme from Pseudomonas cruciviae S93 B1 involved in the degradation of biphenyl. Agric. Biol. Chem. 50 (1986) 931–937. |
|
[EC 3.7.1.8 created 1989] |
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|
|
|
EC |
4.1.2.4 |
Accepted name: |
deoxyribose-phosphate aldolase |
Reaction: |
2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde |
|
For diagram of reaction, click here |
Other name(s): |
phosphodeoxyriboaldolase; deoxyriboaldolase; deoxyribose-5-phosphate aldolase; 2-deoxyribose-5-phosphate aldolase; 2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase |
Systematic name: |
2-deoxy-D-ribose-5-phosphate acetaldehyde-lyase (D-glyceraldehyde-3-phosphate-forming) |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9026-97-5 |
References: |
1. |
Hoffee, P.A. 2-Deoxyribose-5-phosphate aldolase of Salmonella typhimurium: purification and properties. Arch. Biochem. Biophys. 126 (1968) 795–802. [DOI] [PMID: 4879701] |
2. |
Jedziniak, J.A. and Lionetti, F.J. Purification and properties of deoxyriboaldolase from human erythrocytes. Biochim. Biophys. Acta 212 (1970) 478–487. [DOI] [PMID: 4989681] |
3. |
Racker, E. Enzymatic synthesis and breakdown of desoxyribose phosphate. J. Biol. Chem. 196 (1952) 347–365. [PMID: 12980976] |
4. |
Hoffee, P. Rosen, O.M. and Horecker, B.L. The mechanism of action of aldolases. VI. Crystallization of deoxyribose 5-phosphate aldolase and the number of active sites. J. Biol. Chem. 240 (1965) 1512–1516. [PMID: 14285485] |
|
[EC 4.1.2.4 created 1961] |
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|
|
|
EC |
4.1.2.23 |
Accepted name: |
3-deoxy-D-manno-octulosonate aldolase |
Reaction: |
3-deoxy-D-manno-octulosonate = pyruvate + D-arabinose |
Other name(s): |
2-keto-3-deoxyoctonate aldolase; KDOaldolase; 3-deoxyoctulosonic aldolase; 2-keto-3-deoxyoctonic aldolase; 3-deoxy-D-manno-octulosonic aldolase; 3-deoxy-D-manno-octulosonate D-arabinose-lyase |
Systematic name: |
3-deoxy-D-manno-octulosonate D-arabinose-lyase (pyruvate-forming) |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9026-95-3 |
References: |
1. |
Ghalambor, M.A. and Heath, E.C. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. V. Purification and properties of 3-deoxy-D-manno-octulosonate aldolase. J. Biol. Chem. 241 (1966) 3222–3227. [PMID: 5912115] |
|
[EC 4.1.2.23 created 1972] |
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|
|
EC |
4.1.2.63 |
Accepted name: |
2-hydroxyacyl-CoA lyase |
Reaction: |
(1) a 2-hydroxy-3-methyl-Cn-fatty-acyl-CoA = a 2-methyl-branched Cn-1-fatty aldehyde + formyl-CoA (2) a (2R)-2-hydroxy-Cn-long-chain fatty acyl-CoA = a Cn-1-long-chain fatty aldehyde + formyl-CoA |
Other name(s): |
HACL1 (gene name); 2-hydroxyphytanoyl-CoA lyase; 2-HPCL |
Systematic name: |
2-hydroxy-3-methyl fatty-CoA formyl-CoA lyase (2-methyl branched fatty aldehyde-forming) |
Comments: |
Requires Mg2+ and thiamine diphosphate. This peroxisomal enzyme, found in animals, is involved in the α-oxidation of 3-methyl-branched fatty acids like phytanic acid and the shortening of 2-hydroxy long-chain fatty acids. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Foulon, V., Antonenkov, V.D., Croes, K., Waelkens, E., Mannaerts, G.P., Van Veldhoven, P.P. and Casteels, M. Purification, molecular cloning, and expression of 2-hydroxyphytanoyl-CoA lyase, a peroxisomal thiamine pyrophosphate-dependent enzyme that catalyzes the carbon-carbon bond cleavage during α-oxidation of 3-methyl-branched fatty acids. Proc. Natl. Acad. Sci. USA 96 (1999) 10039–10044. [DOI] [PMID: 10468558] |
2. |
Foulon, V., Sniekers, M., Huysmans, E., Asselberghs, S., Mahieu, V., Mannaerts, G.P., Van Veldhoven, P.P. and Casteels, M. Breakdown of 2-hydroxylated straight chain fatty acids via peroxisomal 2-hydroxyphytanoyl-CoA lyase: a revised pathway for the α-oxidation of straight chain fatty acids. J. Biol. Chem. 280 (2005) 9802–9812. [DOI] [PMID: 15644336] |
3. |
Casteels, M., Sniekers, M., Fraccascia, P., Mannaerts, G.P. and Van Veldhoven, P.P. The role of 2-hydroxyacyl-CoA lyase, a thiamin pyrophosphate-dependent enzyme, in the peroxisomal metabolism of 3-methyl-branched fatty acids and 2-hydroxy straight-chain fatty acids. Biochem Soc Trans. 35 (2007) 876–880. [DOI] [PMID: 17956236] |
|
[EC 4.1.2.63 created 2021] |
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|
|
|
EC |
4.4.1.28 |
Accepted name: |
L-cysteine desulfidase |
Reaction: |
L-cysteine + H2O = sulfide + NH3 + pyruvate (overall reaction) (1a) L-cysteine = 2-aminoprop-2-enoate + sulfide (1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous) (1c) 2-iminopropanoate + H2O = pyruvate + NH3 (spontaneous) |
Other name(s): |
L-cysteine desulfhydrase |
Systematic name: |
L-cysteine sulfide-lyase (deaminating; pyruvate-forming) |
Comments: |
The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1, cystathionine γ-lyase). It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia. The same reaction can also be catalysed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1, cystathionine γ-lyase). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
References: |
1. |
Tchong, S.I., Xu, H. and White, R.H. L-Cysteine desulfidase: an [4Fe-4S] enzyme isolated from Methanocaldococcus jannaschii that catalyzes the breakdown of L-cysteine into pyruvate, ammonia, and sulfide. Biochemistry 44 (2005) 1659–1670. [DOI] [PMID: 15683250] |
|
[EC 4.4.1.28 created 2014] |
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|
|
|
EC |
4.6.1.13 |
Accepted name: |
phosphatidylinositol diacylglycerol-lyase |
Reaction: |
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol |
|
For diagram of 1-phosphatidyl-myo-inositol metabolism, click here |
Other name(s): |
monophosphatidylinositol phosphodiesterase; phosphatidylinositol phospholipase C; 1-phosphatidylinositol phosphodiesterase; 1-phosphatidyl-D-myo-inositol inositolphosphohydrolase (cyclic-phosphate-forming); 1-phosphatidyl-1D-myo-inositol diacylglycerol-lyase (1,2-cyclic-phosphate-forming) |
Systematic name: |
1-phosphatidyl-1D-myo-inositol 1,2-diacyl-sn-glycerol-lyase (1D-myo-inositol-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, MetaCyc, PDB, 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. [DOI] [PMID: 4294905] |
3. |
Irvine, R.F. The enzymology of stimulated inositol lipid turnover. Cell Calcium 3 (1982) 295–309. [DOI] [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. [DOI] [PMID: 236918] |
5. |
Low, M.G. and Finean, J.B. Release of alkaline phosphatase from membranes by a
phosphatidylinositol-specific 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. [DOI] [PMID: 3194218] |
|
[EC 4.6.1.13 created 1972 as EC 3.1.4.10, modified 1976, transferred 2002 to EC 4.6.1.13] |
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|
|
|
EC |
4.8.1.5 |
Accepted name: |
thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming) |
Reaction: |
an N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfate + sulfur |
Glossary: |
an N-(sulfonatooxy)alkanimidothioate = a thiohydroximate-O-sulfate |
Other name(s): |
NSP (gene name); nitrile-specifier protein |
Systematic name: |
thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming) |
Comments: |
The enzyme is involved in the breakdown of glucosinolates. It can act on both aliphatic and aromatic glucosinolates, and forms nitrile-containing products. cf. EC 4.8.1.6, N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming), and EC 4.8.1.7, phenyl-N-(sulfonatooxy)methanimidothioate sulfolyase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kissen, R. and Bones, A.M. Nitrile-specifier proteins involved in glucosinolate hydrolysis in Arabidopsis thaliana. J. Biol. Chem. 284 (2009) 12057–12070. [DOI] [PMID: 19224919] |
2. |
Burow, M., Losansky, A., Muller, R., Plock, A., Kliebenstein, D.J. and Wittstock, U. The genetic basis of constitutive and herbivore-induced ESP-independent nitrile formation in Arabidopsis. Plant Physiol. 149 (2009) 561–574. [DOI] [PMID: 18987211] |
|
[EC 4.8.1.5 created 2022] |
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|
|
EC |
4.8.1.6 |
Accepted name: |
N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming) |
Reaction: |
N-(sulfonatooxy)alkenimidothioic acid with a terminal double bond = an epithionitrile + sulfate |
Other name(s): |
ESP (gene name); epithionitrile-specifier protein; epithiospecifier protein |
Systematic name: |
N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming) |
Comments: |
The enzyme is involved in the breakdown of glucosinolates. It acts only on aliphatic N-(sulfonatooxy)alkenimidothioic acids produced from ω-alkenyl-glucosinolates, and forms epithionitrile-containing products. cf. EC 4.8.1.5, thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming), and EC 4.8.1.7, phenyl-N-(sulfonatooxy)methanimidothioate sulfolyase. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Lambrix, V., Reichelt, M., Mitchell-Olds, T., Kliebenstein, D.J. and Gershenzon, J. The Arabidopsis epithiospecifier protein promotes the hydrolysis of glucosinolates to nitriles and influences Trichoplusia ni herbivory. Plant Cell 13 (2001) 2793–2807. [DOI] [PMID: 11752388] |
2. |
Zabala M. de, T., Grant, M., Bones, A.M., Bennett, R., Lim, Y.S., Kissen, R. and Rossiter, J.T. Characterisation of recombinant epithiospecifier protein and its over-expression in Arabidopsis thaliana. Phytochemistry 66 (2005) 859–867. [DOI] [PMID: 15845404] |
|
[EC 4.8.1.6 created 2022] |
|
|
|
|
EC |
4.8.1.7 |
Accepted name: |
phenyl-N-(sulfonatooxy)methanimidothioate sulfolyase |
Reaction: |
phenyl-N-(sulfonatooxy)methanimidothioate = benzylthiocyanate + sulfate |
|
For diagram of glucotropeolin biosynthesis and catabolism, click here |
Glossary: |
glucotropaeolin = 1-S-[(1Z)-2-phenyl-N-(sulfonatooxy)ethanimidoyl]-1-thio-β-D-glucopyranose |
Other name(s): |
TFP (gene name) (ambiguous); thiocyanate-forming protein (ambiguous) |
Systematic name: |
phenyl-N-(sulfonatooxy)methanimidothioate sulfate-lyase (benzylthiocyanate-forming) |
Comments: |
The enzyme, characterized from the plant Lepidium sativum, is involved in the breakdown of the glucosinolate glucotropaeolin. Depending on the substrate, it can also form simple nitrile- and epithionitrile-containing products. cf. EC 4.8.1.5, thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming), and EC 4.8.1.6, N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Burow, M., Bergner, A., Gershenzon, J. and Wittstock, U. Glucosinolate hydrolysis in Lepidium sativum - identification of the thiocyanate-forming protein. Plant Mol. Biol. 63 (2007) 49–61. [DOI] [PMID: 17139450] |
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[EC 4.8.1.7 created 2022] |
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EC |
4.8.1.8 |
Accepted name: |
N-(sulfonatooxy)prop-2-enimidothioate sulfolyase |
Reaction: |
(1) N-(sulfonatooxy)prop-2-enimidothioate = prop-2-enylthiocyanate + sulfate (2) N-(sulfonatooxy)prop-2-enimidothioate = 2-(thiiran-2-yl)acetonitrile + sulfate |
Other name(s): |
TFP (gene name) (ambiguous); thiocyanate-forming protein (ambiguous) |
Systematic name: |
N-(sulfonatooxy)prop-2-enimidothioate sulfate-lyase (prop2-enylthiocyanate-forming) |
Comments: |
The enzyme, characterized from the plant Thlaspi arvense, is involved in the breakdown of the glucosinolate sinigrin. Depending on the substrate, it can also form simple nitrile-containing products. cf. EC 4.8.1.5, thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming) and EC 4.8.1.6, N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming). |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Kuchernig, J.C., Backenkohler, A., Lubbecke, M., Burow, M. and Wittstock, U. A thiocyanate-forming protein generates multiple products upon allylglucosinolate breakdown in Thlaspi arvense. Phytochemistry 72 (2011) 1699–1709. [DOI] [PMID: 21783213] |
2. |
Gumz, F., Krausze, J., Eisenschmidt, D., Backenkohler, A., Barleben, L., Brandt, W. and Wittstock, U. The crystal structure of the thiocyanate-forming protein from Thlaspi arvense, a kelch protein involved in glucosinolate breakdown. Plant Mol. Biol. 89 (2015) 67–81. [DOI] [PMID: 26260516] |
3. |
Eisenschmidt-Bonn, D., Schneegans, N., Backenkohler, A., Wittstock, U. and Brandt, W. Structural diversification during glucosinolate breakdown: mechanisms of thiocyanate, epithionitrile and simple nitrile formation. Plant J. 99 (2019) 329–343. [DOI] [PMID: 30900313] |
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[EC 4.8.1.8 created 2022] |
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EC |
5.3.1.13 |
Accepted name: |
arabinose-5-phosphate isomerase |
Reaction: |
D-arabinose 5-phosphate = D-ribulose 5-phosphate |
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For diagram of D-arabinose catabolism, click here |
Other name(s): |
kdsD (gene name); gutQ (gene name); arabinose phosphate isomerase; phosphoarabinoisomerase; D-arabinose-5-phosphate ketol-isomerase |
Systematic name: |
D-arabinose-5-phosphate aldose-ketose-isomerase |
Comments: |
The enzyme is involved in the pathway for synthesis of 3-deoxy-D-manno-octulosonate (Kdo), a component of bacterial lipopolysaccharides and plant call walls. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9023-86-3 |
References: |
1. |
Volk, W.A. Purification and properties of phosphoarabinoisomerase from Propionibacterium pentosaceum. J. Biol. Chem. 235 (1960) 1550–1553. |
2. |
Lim, R. and Cohen, S.S. D-Phosphoarabinoisomerase and D-ribulokinase in Escherichia coli. J. Biol. Chem. 241 (1966) 4304–4315. [PMID: 5332197] |
3. |
Meredith, T.C. and Woodard, R.W. Identification of GutQ from Escherichia coli as a D-arabinose 5-phosphate isomerase. J. Bacteriol. 187 (2005) 6936–6942. [DOI] [PMID: 16199563] |
4. |
Gourlay, L.J., Sommaruga, S., Nardini, M., Sperandeo, P., Deho, G., Polissi, A. and Bolognesi, M. Probing the active site of the sugar isomerase domain from E. coli arabinose-5-phosphate isomerase via X-ray crystallography. Protein Sci. 19 (2010) 2430–2439. [DOI] [PMID: 20954237] |
5. |
Chiu, H.J., Grant, J.C., Farr, C.L., Jaroszewski, L., Knuth, M.W., Miller, M.D., Elsliger, M.A., Deacon, A.M., Godzik, A., Lesley, S.A. and Wilson, I.A. Structural analysis of arabinose-5-phosphate isomerase from Bacteroides fragilis and functional implications. Acta Crystallogr. D Biol. Crystallogr. 70 (2014) 2640–2651. [DOI] [PMID: 25286848] |
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[EC 5.3.1.13 created 1965] |
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EC |
6.2.1.4 |
Accepted name: |
succinate—CoA ligase (GDP-forming) |
Reaction: |
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA |
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For diagram of the citric-acid cycle, click here |
Other name(s): |
succinyl-CoA synthetase (GDP-forming); succinyl coenzyme A synthetase (guanosine diphosphate-forming); succinate thiokinase (ambiguous); succinic thiokinase (ambiguous); succinyl coenzyme A synthetase (ambiguous); succinate-phosphorylating enzyme (ambiguous); P-enzyme; SCS (ambiguous); G-STK; succinyl coenzyme A synthetase (GDP-forming); succinyl CoA synthetase (ambiguous) |
Systematic name: |
succinate:CoA ligase (GDP-forming) |
Comments: |
Itaconate can act instead of succinate, and ITP instead of GTP. |
Links to other databases: |
BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9014-36-2 |
References: |
1. |
Hager, L.P. Succinyl CoA synthetase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Ed.), The Enzymes, 2nd edn, vol. 6, Academic Press, New York, 1962, pp. 387–399. |
2. |
Kaufman, S., Gilvarg, C., Cori, O. and Ochoa, S. Enzymatic oxidation of α-ketoglutarate and coupled phosphorylation. J. Biol. Chem. 203 (1953) 869–888. [PMID: 13084656] |
3. |
Mazumder, R., Sanadi, D.R. and Rodwell, W.V. Purification and properties of hog kidney succinic thiokinase. J. Biol. Chem. 235 (1960) 2546–2550. [PMID: 13768680] |
4. |
Sanadi, D.R., Gibson, D.M. and Ayengar, P. Guanosine triphosphate, the primary product of phosphorylation coupled to the breakdown of succinyl coenzyme A. Biochim. Biophys. Acta 14 (1954) 434–436. [DOI] [PMID: 13181903] |
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[EC 6.2.1.4 created 1961] |
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EC |
6.2.1.7 |
Accepted name: |
cholate—CoA ligase |
Reaction: |
(1) ATP + cholate + CoA = AMP + diphosphate + choloyl-CoA (2) ATP + (25R)-3α,7α,12α-trihydroxy-5β-cholestan-26-oate + CoA = AMP + diphosphate + (25R)-3α,7α,12α-trihydroxy-5β-cholestanoyl-CoA |
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For diagram of cholic acid conjugates biosynthesis, click here and for diagram of cholic acid biosynthesis (sidechain), click here |
Glossary: |
cholate = 3α,7α,12α-trihydroxy-5β-cholan-24-oate
trihydroxycoprostanoate = 3α,7α,12α-trihydroxy-5β-cholestan-26-oate |
Other name(s): |
BAL; bile acid CoA ligase; bile acid coenzyme A ligase; choloyl-CoA synthetase; choloyl coenzyme A synthetase; cholic thiokinase; cholate thiokinase; cholic acid:CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoyl coenzyme A synthetase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanoate-CoA synthetase; THCA-CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate—CoA ligase; 3α,7α,12α-trihydroxy-5β-cholestanate:CoA ligase (AMP-forming); cholyl-CoA synthetase; trihydroxycoprostanoyl-CoA synthetase |
Systematic name: |
cholate:CoA ligase (AMP-forming) |
Comments: |
Requires Mg2+ for activity. The mammalian enzyme is membrane-bound and catalyses the first step in the conjugation of bile acids with amino acids, converting bile acids into their acyl-CoA thioesters. Chenodeoxycholate, deoxycholate, lithocholate and trihydroxycoprostanoate can also act as substrates [7]. The bacterial enzyme is soluble and participates in an anaerobic bile acid 7 α-dehydroxylation pathway [5]. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9027-90-1 |
References: |
1. |
Elliott, W.H. The enzymic activation of cholic acid by guinea-pig-liver microsomes. Biochem. J. 62 (1956) 427–433. [PMID: 13303991] |
2. |
Elliott, W.H. The breakdown of adenosine triphosphate accompanying cholic acid activation by guinea-pig liver microsomes. Biochem. J. 65 (1957) 315–321. [PMID: 13403911] |
3. |
Prydz, K., Kase, B.F., Björkhem, I. and Pedersen, J.I. Subcellular localization of 3α,7α-dihydroxy- and 3α,7α,12α-trihydroxy-5β-cholestanoyl-coenzyme A ligase(s) in rat liver. J. Lipid Res. 29 (1988) 997–1004. [PMID: 3183523] |
4. |
Schepers, L., Casteels, M., Verheyden, K., Parmentier, G., Asselberghs, S., Eyssen, H.J. and Mannaerts, G.P. Subcellular distribution and characteristics of trihydroxycoprostanoyl-CoA synthetase in rat liver. Biochem. J. 257 (1989) 221–229. [PMID: 2521999] |
5. |
Mallonee, D.H., Adams, J.L. and Hylemon, P.B. The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase. J. Bacteriol. 174 (1992) 2065–2071. [DOI] [PMID: 1551828] |
6. |
Wheeler, J.B., Shaw, D.R. and Barnes, S. Purification and characterization of a rat liver bile acid coenzyme A ligase from rat liver microsomes. Arch. Biochem. Biophys. 348 (1997) 15–24. [DOI] [PMID: 9390170] |
7. |
Falany, C.N., Xie, X., Wheeler, J.B., Wang, J., Smith, M., He, D. and Barnes, S. Molecular cloning and expression of rat liver bile acid CoA ligase. J. Lipid Res. 43 (2002) 2062–2071. [PMID: 12454267] |
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[EC 6.2.1.7 created 1961 (EC 6.2.1.29 created 1992, incorporated 2005), modified 2005] |
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EC |
6.2.1.34 |
Accepted name: |
trans-feruloyl-CoA synthase |
Reaction: |
ferulic acid + CoA + ATP = feruloyl-CoA + products of ATP breakdown |
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For diagram of reaction, click here |
Other name(s): |
trans-feruloyl-CoA synthetase; trans-ferulate:CoASH ligase (ATP-hydrolysing); ferulate:CoASH ligase (ATP-hydrolysing) |
Systematic name: |
ferulate:CoA ligase (ATP-hydrolysing) |
Comments: |
Requires Mg2+. It has not yet been established whether AMP + diphosphate or ADP + phosphate are formed in this reaction. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc |
References: |
1. |
Narbad, A. and Gasson, M.J. Metabolism of ferulic acid via vanillin using a novel CoA-dependent pathway in a newly-isolated strain of Pseudomonas fluorescens. Microbiology 144 (1998) 1397–1405. [DOI] [PMID: 9611814] |
2. |
Pometto, A.L. and Crawford, D.L. Whole-cell bioconversion of vanillin to vanillic acid by Streptomyces viridosporus. Appl. Environ. Microbiol. 45 (1983) 1582–1585. [PMID: 6870241] |
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[EC 6.2.1.34 created 2000] |
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EC |
6.3.2.18 |
Accepted name: |
γ-glutamylhistamine synthase |
Reaction: |
ATP + L-glutamate + histamine = products of ATP breakdown + Nα-γ-L-glutamylhistamine |
Other name(s): |
γ-glutaminylhistamine synthetase; γ-GHA synthetase |
Systematic name: |
L-glutamate:histamine ligase |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 82904-08-3 |
References: |
1. |
Stein, C. and Weinreich, D. An in vitro characterization of γ-glutamylhistamine synthetase: a novel enzyme catalyzing histamine metabolism in the central nervous system of the marine mollusk, Aplysia californica. J. Neurochem. 38 (1982) 204–214. [DOI] [PMID: 6125565] |
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[EC 6.3.2.18 created 1986] |
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