The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version

Accepted name: barbiturase
Reaction: barbiturate + H2O = 3-oxo-3-ureidopropanoate
For diagram of pyrimidine catabolism, click here
Glossary: barbiturate = 6-hydroxyuracil
Systematic name: barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming)
Comments: Contains zinc and is specific for barbiturate as substrate [3]. Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC (uracil/thymine dehydrogenase) and EC (N-malonylurea hydrolase). It was previously thought that the end-products of the reaction were malonate and urea but this has since been disproved [2]. May be involved in the regulation of pyrimidine metabolism, along with EC, uracil phosphoribosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-16-5
1.  Hayaishi, O. and Kornberg, A. Metabolism of cytosine, thymine, uracil, and barbituric acid by bacterial enzymes. J. Biol. Chem. 197 (1952) 717–723. [PMID: 12981104]
2.  Soong, C.L., Ogawa, J. and Shimizu, S. Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase. Biochem. Biophys. Res. Commun. 286 (2001) 222–226. [DOI] [PMID: 11485332]
3.  Soong, C.L., Ogawa, J., Sakuradani, E. and Shimizu, S. Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism. J. Biol. Chem. 277 (2002) 7051–7058. [DOI] [PMID: 11748240]
[EC created 1961, modified 2006]
Accepted name: creatininase
Reaction: creatinine + H2O = creatine
Other name(s): creatinine hydrolase
Systematic name: creatinine amidohydrolase
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-13-2
1.  Tsuru, D., Oka, I. and Yoshimoto, T. Creatinine decomposing enzymes in Pseudomonas putida. Agric. Biol. Chem. 40 (1976) 1011–1018.
[EC created 1978]
Accepted name: L-lysine-lactamase
Reaction: (S)-2-aminohexano-6-lactam + H2O = L-lysine
Glossary: (S)-2-aminohexano-6-lactam = L-lysine 1,6-lactam
Other name(s): L-α-aminocaprolactam hydrolase; L-lysinamidase; L-lysine-1,6-lactam lactamhydrolase
Systematic name: (S)-2-aminohexano-6-lactam lactamhydrolase
Comments: Also hydrolyses L-lysinamide.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 52652-61-6
1.  Fukumura, T., Talbot, G., Misono, H., Teremura, Y., Kato, K. and Soda, K. Purification and properties of a novel enzyme, L- α-amino-ε-caprolactamase from Cryptococcus laurentii. FEBS Lett. 89 (1978) 298–300. [DOI] [PMID: 26602]
2.  Shvyadas, V.K., Galaev, I.Yu. and Kozlova, E.V. Preparation and characterization of L-α-aminocaprolactam hydrolase from cells of Cryptococcus laurentii. Biochemistry (Moscow) 49 (1984) 1268–1273.
[EC created 1981, modified 1989]
Accepted name: 6-aminohexanoate-cyclic-dimer hydrolase
Reaction: 1,8-diazacyclotetradecane-2,9-dione + H2O = N-(6-aminohexanoyl)-6-aminohexanoate
Systematic name: 1,8-diazacyclotetradecane-2,9-dione lactamhydrolase
Comments: The cyclic dimer of 6-aminohexanoate is converted to the linear dimer.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 60976-29-6
1.  Kinoshita, S., Negoro, S., Muramatsu, M., Bisaria, V.S., Sawada, S. and Okada, H. 6-Aminohexanoic acid cyclic dimer hydrolase. A new cyclic amide hydrolase produced by Achromobacter guttatus KI74. Eur. J. Biochem. 80 (1977) 489–495. [DOI] [PMID: 923591]
[EC created 1983]
Accepted name: 2,5-dioxopiperazine hydrolase
Reaction: 2,5-dioxopiperazine + H2O = glycylglycine
Other name(s): cyclo(Gly-Gly) hydrolase; cyclo(glycylglycine) hydrolase
Systematic name: 2,5-dioxopiperazine amidohydrolase
Comments: Highly specific; does not hydrolyse other dioxopiperazines, glycylglycine, proteins or barbiturates.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 97599-45-6
1.  Suzuki, Y. and Uchida, K. Multiple forms of α-glycosidase from pig duodenum. Agric. Biol. Chem. 49 (1985) 1573–1581.
[EC created 1989]
Accepted name: N-methylhydantoinase (ATP-hydrolysing)
Reaction: ATP + N-methylhydantoin + 2 H2O = ADP + phosphate + N-carbamoylsarcosine
For diagram of creatine biosynthesis, click here
Glossary: N-methylhydantoin = N-methylimidazolidine-2,4-dione
Other name(s): N-methylhydantoin amidohydrolase; methylhydantoin amidase; N-methylhydantoin hydrolase; N-methylhydantoinase; N-methylimidazolidine-2,4-dione amidohydrolase (ATP-hydrolysing)
Systematic name: N-methylhydantoin amidohydrolase (ATP-hydrolysing)
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 100785-00-0
1.  Kim, J.M., Shimizu, S. and Yamada, H. Amidohydrolysis of N-methylhydantoin coupled with ATP hydrolysis. Biochem. Biophys. Res. Commun. 142 (1987) 1006–1012. [DOI] [PMID: 3827889]
[EC created 1989]
Accepted name: cyanuric acid amidohydrolase
Reaction: cyanuric acid + H2O = 1-carboxybiuret
Glossary: cyanuric acid = 1,3,5-triazine-2,4,6(1H,3H,5H)-trione = 2,4,6-trihydroxy-s-triazine
1-carboxybiuret = N-[(carbamoylamino)carbonyl]carbamate
Other name(s): atzD (gene name); trzD (gene name)
Systematic name: cyanuric acid amidohydrolase
Comments: The enzyme catalyses the ring cleavage of cyanuric acid, an intermediate in the degradation of s-triazide herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is highly specific for cyanuric acid. The product was initially thought to be bioret, but was later shown to be 1-carboxybioret.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 132965-78-7
1.  Eaton, R.W. and Karns, J.S. Cloning and comparison of the DNA encoding ammelide aminohydrolase and cyanuric acid amidohydrolase from three s-triazine-degrading bacterial strains. J. Bacteriol. 173 (1991) 1363–1366. [DOI] [PMID: 1991731]
2.  Eaton, R.W. and Karns, J.S. Cloning and analysis of s-triazine catabolic genes from Pseudomonas sp. strain NRRLB-12227. J. Bacteriol. 173 (1991) 1215–1222. [DOI] [PMID: 1846859]
3.  Karns, J.S. Gene sequence and properties of an s-triazine ring-cleavage enzyme from Pseudomonas sp. strain NRRLB-12227. Appl. Environ. Microbiol. 65 (1999) 3512–3517. [PMID: 10427042]
4.  Fruchey, I., Shapir, N., Sadowsky, M.J. and Wackett, L.P. On the origins of cyanuric acid hydrolase: purification, substrates, and prevalence of AtzD from Pseudomonas sp. strain ADP. Appl. Environ. Microbiol. 69 (2003) 3653–3657. [DOI] [PMID: 12788776]
5.  Esquirol, L., Peat, T.S., Wilding, M., Liu, J.W., French, N.G., Hartley, C.J., Onagi, H., Nebl, T., Easton, C.J., Newman, J. and Scott, C. An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. J. Biol. Chem 293 (2018) 7880–7891. [PMID: 29523689]
[EC created 2000, modified 2008, modified 2019]
Accepted name: maleimide hydrolase
Reaction: maleimide + H2O = maleamic acid
Other name(s): imidase; cyclic imide hydrolase; cyclic-imide amidohydrolase (decyclicizing) [misprint]; cyclic-imide amidohydrolase (decyclizing)
Systematic name: cyclic-imide amidohydrolase (ring-opening)
Comments: 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, dihydropyrimidinase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-74-4
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. [PMID: 9030755]
[EC created 2001]
Accepted name: hydroxyisourate hydrolase
Reaction: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
For diagram of AMP catabolism, click here
Other name(s): HIUHase; 5-hydroxyisourate hydrolase
Systematic name: 5-hydroxyisourate amidohydrolase
Comments: The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 255885-20-2
1.  Raychaudhuri, A. and Tipton, P.A. A familiar motif in a new context: the catalytic mechanism of hydroxyisourate hydrolase. Biochemistry 42 (2003) 6848–6852. [DOI] [PMID: 12779339]
2.  Raychaudhuri, A. and Tipton, P.A. Cloning and expression of the gene for soybean hydroxyisourate hydrolase. Localization and implications for function and mechanism. Plant Physiol. 130 (2002) 2061–2068. [DOI] [PMID: 12481089]
3.  Sarma, A.D., Serfozo, P., Kahn, K. and Tipton, P.A. Identification and purification of hydroxyisourate hydrolase, a novel ureide-metabolizing enzyme. J. Biol. Chem. 274 (1999) 33863–33865. [DOI] [PMID: 10567345]
[EC created 2004]
Accepted name: enamidase
Reaction: 6-oxo-1,4,5,6-tetrahydronicotinate + 2 H2O = 2-formylglutarate + NH3
For diagram of nicotinate catabolism, click here
Systematic name: 6-oxo-1,4,5,6-tetrahydronicotinate amidohydrolase
Comments: Contains iron and Zn2+. Forms part of the nicotinate-fermentation catabolism pathway in Eubacterium barkeri. Other enzymes involved in this pathway are EC (nicotinate dehydrogenase), EC (6-hydroxynicotinate reductase), EC (2-hydroxymethylglutarate dehydrogenase), EC (2-methyleneglutarate mutase), EC (methylitaconate Δ-isomerase), EC (dimethylmaleate hydratase) and EC (2,3-dimethylmalate lyase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
1.  Alhapel, A., Darley, D.J., Wagener, N., Eckel, E., Elsner, N. and Pierik, A.J. Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri. Proc. Natl. Acad. Sci. USA 103 (2006) 12341–12346. [DOI] [PMID: 16894175]
[EC created 2006]
Accepted name: streptothricin hydrolase
Reaction: streptothricin-F + H2O = streptothricin-F acid
Other name(s): sttH (gene name)
Systematic name: streptothricin-F hydrolase
Comments: The enzyme also catalyses the hydrolysis of streptothricin-D to streptothricin-D acid [1]. The enzyme is responsible for streptothricin resistance in Streptomyces albulus and Streptomyces noursei [1,2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
1.  Maruyama, C. and Hamano, Y. The biological function of the bacterial isochorismatase-like hydrolase SttH. Biosci. Biotechnol. Biochem. 73 (2009) 2494–2500. [DOI] [PMID: 19897889]
2.  Hamano, Y., Matsuura, N., Kitamura, M. and Takagi, H. A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific. J. Biol. Chem. 281 (2006) 16842–16848. [DOI] [PMID: 16641084]
[EC created 2011]

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