The Enzyme Database

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EC 4.1.3.1     
Accepted name: isocitrate lyase
Reaction: isocitrate = succinate + glyoxylate
For diagram of the glyoxylate cycle, click here
Glossary: isocitrate = (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate (previously known as threo-Ds-isocitrate)
Other name(s): isocitrase; isocitritase; isocitratase; threo-Ds-isocitrate glyoxylate-lyase; isocitrate glyoxylate-lyase
Systematic name: isocitrate glyoxylate-lyase (succinate-forming)
Comments: The isomer of isocitrate involved is (1R,2S)-1-hydroxypropane-1,2,3-tricarboxylate [3].
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9045-78-7
References:
1.  McFadden, B.A. and Howes, W.V. Crystallisation and some properties of isocitrate lyase from Pseudomonas indigofera. J. Biol. Chem. 238 (1963) 1737–1742.
2.  Shiio, I., Shiio, T. and McFadden, B.A. Isocitrate lyase from Pseudomonas indigofera. I. Preparation, amino acid composition and molecular weight. Biochim. Biophys. Acta 96 (1965) 114–122. [DOI] [PMID: 14285253]
3.  Vickery, H.B. A suggested new nomenclature for the isomers of isocitric acid. J. Biol. Chem. 237 (1962) 1739–1741. [PMID: 13925783]
[EC 4.1.3.1 created 1961]
 
 
EC 4.1.3.10      
Transferred entry: 3-ethylmalate synthase. Now EC 2.3.3.7, 3-ethylmalate synthase
[EC 4.1.3.10 created 1965, modified 1983, deleted 2002]
 
 
EC 4.1.3.11      
Transferred entry: 3-propylmalate synthase. Now EC 2.3.3.12, 3-propylmalate synthase
[EC 4.1.3.11 created 1972, deleted 2002]
 
 
EC 4.1.3.12      
Transferred entry: 2-isopropylmalate synthase. Now EC 2.3.3.13, 2-isopropylmalate synthase
[EC 4.1.3.12 created 1972, deleted 2002]
 
 
EC 4.1.3.13     
Accepted name: oxalomalate lyase
Reaction: 3-oxalomalate = oxaloacetate + glyoxylate
Other name(s): 3-oxalomalate glyoxylate-lyase
Systematic name: 3-oxalomalate glyoxylate-lyase (oxaloacetate-forming)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-63-4
References:
1.  Sekizawa, Y., Maragoudakis, M.E., King, T.E. and Cheldelin, V.H. Glutamate biosynthesis in an organism lacking a Krebs tricarboxylic acid cycle. V. Isolation of α-hydroxy-γ-ketoglutarate (HKG) in Acetobacter suboxydans. Biochemistry 5 (1966) 2392–2398. [PMID: 6005666]
[EC 4.1.3.13 created 1972]
 
 
EC 4.1.3.14     
Accepted name: L-erythro-3-hydroxyaspartate aldolase
Reaction: L-erythro-3-hydroxy-aspartate = glycine + glyoxylate
Other name(s): L-erythro-β-hydroxyaspartate aldolase; L-erythro-β-hydroxyaspartate glycine-lyase; erythro-3-hydroxy-Ls-aspartate glyoxylate-lyase
Systematic name: L-erythro-3-hydroxy-aspartate glyoxylate-lyase (glycine-forming)
Comments: A pyridoxal-phosphate protein. The enzyme, purified from the bacterium Paracoccus denitrificans NCIMB 8944, is strictly specific for the L-erythro stereoisomer of 3-hydroxyaspartate. Different from EC 4.1.3.41, erythro-3-hydroxy-D-aspartate aldolase. Requires a divalent cation.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-64-5
References:
1.  Gibbs, R.G. and Morris, J.G. Assay and properties of β-hydroxyaspartate aldolase from Micrococcus denitrificans. Biochim. Biophys. Acta 85 (1964) 501–503. [PMID: 14194868]
[EC 4.1.3.14 created 1972, modified 2011]
 
 
EC 4.1.3.15      
Transferred entry: 2-hydroxy-3-oxoadipate synthase. Now EC 2.2.1.5, 2-hydroxy-3-oxoadipate synthase
[EC 4.1.3.15 created 1972, deleted 2002]
 
 
EC 4.1.3.16     
Accepted name: 4-hydroxy-2-oxoglutarate aldolase
Reaction: 4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
Other name(s): 2-oxo-4-hydroxyglutarate aldolase; hydroxyketoglutaric aldolase; 4-hydroxy-2-ketoglutaric aldolase; 2-keto-4-hydroxyglutaric aldolase; 4-hydroxy-2-ketoglutarate aldolase; 2-keto-4-hydroxyglutarate aldolase; 2-oxo-4-hydroxyglutaric aldolase; DL-4-hydroxy-2-ketoglutarate aldolase; hydroxyketoglutarate aldolase; 2-keto-4-hydroxybutyrate aldolase; 4-hydroxy-2-oxoglutarate glyoxylate-lyase; KHGA
Systematic name: 4-hydroxy-2-oxoglutarate glyoxylate-lyase (pyruvate-forming)
Comments: The enzymes from rat liver and bovine liver act on both enantiomers of 4-hydroxy-2-oxoglutarate. cf. EC 4.1.3.42, (4S)-4-hydroxy-2-oxoglutarate aldolase.
Links to other databases: BRENDA, EXPASY, GTD, KEGG, MetaCyc, PDB, CAS registry number: 9030-81-3
References:
1.  Kuratomi, K. and Fukunaga, K. The metabolism of γ-hydroxyglutamate in rat liver. I. Enzymic synthesis of γ-hydroxy-α-ketoglutarate from pyruvate and glyoxalate. Biochim. Biophys. Acta 78 (1963) 617–628. [DOI] [PMID: 14089442]
2.  Kobes, R.D. and Dekker, E.E. 2-Keto-4-hydroxyglutarate aldolase of bovine liver. Purification, criteria of purity, and general properties. J. Biol. Chem. 244 (1969) 1919–1925. [PMID: 5780845]
3.  Lane, R.S., Shapley, A. and Dekker, E.E. 2-keto-4-hydroxybutyrate aldolase. Identification as 2-keto-4-hydroxyglutarate aldolase, catalytic properties, and role in the mammalian metabolism of L-homoserine. Biochemistry 10 (1971) 1353–1364. [PMID: 5580656]
4.  Scholtz, J.M. and Schuster, S.M. Regulation of rat liver 4-hydroxy-2-ketoglutarate aldolase. Biochim. Biophys. Acta 869 (1986) 192–196. [DOI] [PMID: 3942759]
[EC 4.1.3.16 created 1972 (EC 4.1.2.1 created 1961, incorporated 1972, EC 4.1.2.31 created 1978, incorporated 1982)]
 
 
EC 4.1.3.17     
Accepted name: 4-hydroxy-4-methyl-2-oxoglutarate aldolase
Reaction: (1) 4-hydroxy-4-methyl-2-oxoglutarate = 2 pyruvate
(2) 2-hydroxy-4-oxobutane-1,2,4-tricarboxylate = oxaloacetate + pyruvate
For diagram of the protocatechuate 3,4-cleavage pathway, click here
Other name(s): pyruvate aldolase; γ-methyl-γ-hydroxy-α-ketoglutaric aldolase; 4-hydroxy-4-methyl-2-ketoglutarate aldolase; 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase; HMG aldolase; CHA aldolase; 4-carboxy-4-hydroxy-2-oxoadipate aldolase
Systematic name: 4-hydroxy-4-methyl-2-oxoglutarate pyruvate-lyase (pyruvate-forming)
Comments: Requires a divalent metal ion [3]. This enzyme participates in the degradation of 3,4-dihydroxybenzoate (via the meta-cleavage pathway), phthalate, syringate and 3,4,5-trihydroxybenzoate [1-3]. The enzyme from Pseudomonas straminea can also catalyse the activity of EC 4.1.3.16, 4-hydroxy-2-oxoglutarate aldolase, and the decarboxylation of oxaloacetate [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37290-65-6
References:
1.  Tack, B.F., Chapman, P.J. and Dagley, S. Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase. J. Biol. Chem. 247 (1972) 6444–6449. [PMID: 5076765]
2.  Wood, W.A. 2-Keto-3-deoxy-6-phosphogluconic and related aldolases. In: Boyer, P.D. (Ed.), The Enzymes, 3rd edn, vol. 7, Academic Press, New York, 1972, pp. 281–302.
3.  Maruyama, K. Purification and properties of 4-hydroxy-4-methyl-2-oxoglutarate aldolase from Pseudomonas ochraceae grown on phthalate. J. Biochem. 108 (1990) 327–333. [PMID: 2229032]
4.  Nogales, J., Canales, A., Jiménez-Barbero, J., Serra B., Pingarrón, J. M., García, J. L. and Díaz, E. Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Mol. Microbiol. 79 (2011) 359–374. [DOI] [PMID: 21219457]
[EC 4.1.3.17 created 1972, modified 2012]
 
 
EC 4.1.3.18      
Transferred entry: acetolactate synthase. Now EC 2.2.1.6, acetolactate synthase
[EC 4.1.3.18 created 1972, deleted 2002]
 
 
EC 4.1.3.19      
Transferred entry: N-acetylneuraminate synthase. Now EC 2.5.1.56, N-acetylneuraminate synthase
[EC 4.1.3.19 created 1972, deleted 2002]
 
 


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