The Enzyme Database

Your query returned 11 entries.    printer_iconPrintable version



EC 3.5.2.1     
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 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.1.95 (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 2.4.2.9, uracil phosphoribosyltransferase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9025-16-5
References:
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 3.5.2.1 created 1961, modified 2006]
 
 
EC 3.5.2.10     
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
References:
1.  Tsuru, D., Oka, I. and Yoshimoto, T. Creatinine decomposing enzymes in Pseudomonas putida. Agric. Biol. Chem. 40 (1976) 1011–1018.
[EC 3.5.2.10 created 1978]
 
 
EC 3.5.2.11     
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
References:
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 3.5.2.11 created 1981, modified 1989]
 
 
EC 3.5.2.12     
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
References:
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 3.5.2.12 created 1983]
 
 
EC 3.5.2.13     
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
References:
1.  Suzuki, Y. and Uchida, K. Multiple forms of α-glycosidase from pig duodenum. Agric. Biol. Chem. 49 (1985) 1573–1581.
[EC 3.5.2.13 created 1989]
 
 
EC 3.5.2.14     
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
References:
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 3.5.2.14 created 1989]
 
 
EC 3.5.2.15     
Accepted name: cyanuric acid amidohydrolase
Reaction: cyanuric acid + H2O = biuret + CO2
Glossary: cyanuric acid = 1,3,5-triazine-2,4,6(1H,3H,5H)-trione = 2,4,6-trihydroxy-s-triazine
biuret = imidodicarbonic diamide
Other name(s): AtzD
Systematic name: cyanuric acid amidohydrolase
Comments: Along with EC 3.5.1.54 (allophanate hydrolase) and EC 3.5.1.84 (biuret amidohydrolase), this enzyme forms part of the cyanuric-acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine], in bacteria. This is a key enzyme in the pathway, catalysing the ring cleavage of cyanuric acid. The enzyme is specific for cyanuric acid as substrate as neither the structurally related compounds ammeline (2,4-diamino-6-hydroxy-s-triazine) and ammelide (2-amino-4,6-dihydroxy-s-triazine) nor a number of pyrimidine compounds, such as uracil and cytosine, can act as substrates [3].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, UM-BBD, CAS registry number: 132965-78-7
References:
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]
[EC 3.5.2.15 created 2000, modified 2008]
 
 
EC 3.5.2.16     
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 3.5.2.2, dihydropyrimidinase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 9030-74-4
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. [PMID: 9030755]
[EC 3.5.2.16 created 2001]
 
 
EC 3.5.2.17     
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
References:
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 3.5.2.17 created 2004]
 
 
EC 3.5.2.18     
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 1.17.1.5 (nicotinate dehydrogenase), EC 1.3.7.1 (6-hydroxynicotinate reductase), EC 1.1.1.291 (2-hydroxymethylglutarate dehydrogenase), EC 5.4.99.4 (2-methyleneglutarate mutase), EC 5.3.3.6 (methylitaconate Δ-isomerase), EC 4.2.1.85 (dimethylmaleate hydratase) and EC 4.1.3.32 (2,3-dimethylmalate lyase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
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 3.5.2.18 created 2006]
 
 
EC 3.5.2.19     
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
References:
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 3.5.2.19 created 2011]
 
 


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