The Enzyme Database

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EC 3.5.1.54     
Accepted name: allophanate hydrolase
Reaction: urea-1-carboxylate + H2O = 2 CO2 + 2 NH3
For diagram of atrazine catabolism, click here
Glossary: allophanate = urea-1-carboxylate
Other name(s): allophanate lyase; AtzF; TrzF
Systematic name: urea-1-carboxylate amidohydrolase
Comments: Along with EC 3.5.2.15 (cyanuric acid amidohydrolase) 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. The yeast enzyme (but not that from green algae) also catalyses the reaction of EC 6.3.4.6, urea carboxylase, thus bringing about the hydrolysis of urea to CO2 and NH3 in the presence of ATP and bicarbonate. The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate [6].
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9076-72-6
References:
1.  Maitz, G.S., Haas, E.M. and Castric, P.A. Purification and properties of the allophanate hydrolase from Chlamydomonas reinhardii. Biochim. Biophys. Acta 714 (1982) 486–491.
2.  Roon, R.J. and Levenberg, B. Urea amidolyase. I. Properties of the enzyme from Candida utilis. J. Biol. Chem. 247 (1972) 4107–4113. [PMID: 4556303]
3.  Sumrada, R.A. and Cooper, T.G. Urea carboxylase and allophanate hydrolase are components of a multifunctional protein in yeast. J. Biol. Chem. 257 (1982) 9119–9127. [PMID: 6124544]
4.  Kanamori, T., Kanou, N., Kusakabe, S., Atomi, H. and Imanaka, T. Allophanate hydrolase of Oleomonas sagaranensis involved in an ATP-dependent degradation pathway specific to urea. FEMS Microbiol. Lett. 245 (2005) 61–65. [DOI] [PMID: 15796980]
5.  Cheng, G., Shapir, N., Sadowsky, M.J. and Wackett, L.P. Allophanate hydrolase, not urease, functions in bacterial cyanuric acid metabolism. Appl. Environ. Microbiol. 71 (2005) 4437–4445. [DOI] [PMID: 16085834]
6.  Shapir, N., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of allophanate hydrolase (AtzF) from Pseudomonas sp. strain ADP. J. Bacteriol. 187 (2005) 3731–3738. [DOI] [PMID: 15901697]
7.  Shapir, N., Cheng, G., Sadowsky, M.J. and Wackett, L.P. Purification and characterization of TrzF: biuret hydrolysis by allophanate hydrolase supports growth. Appl. Environ. Microbiol. 72 (2006) 2491–2495. [DOI] [PMID: 16597948]
[EC 3.5.1.54 created 1986, modified 2008]
 
 
EC 3.5.1.84     
Accepted name: biuret amidohydrolase
Reaction: biuret + H2O = urea-1-carboxylate + NH3
For diagram of atrazine catabolism, click here
Glossary: biuret = imidodicarbonic diamide
allophanate = urea-1-carboxylate
Other name(s): biuH (gene name)
Systematic name: biuret amidohydrolase
Comments: The enzyme, characterized from the bacterium Rhizobium leguminosarum bv. viciae 3841, participates in the degradation 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 substrate, biuret, forms by the spontaneous decarboxylation of 1-carboxybiuret in the absence of EC 3.5.1.131, 1-carboxybiuret hydrolase.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 95567-88-7
References:
1.  Cameron, S.M., Durchschein, K., Richman, J.E., Sadowsky, M.J. and Wackett, L.P. A new family of biuret hydrolases involved in s-triazine ring metabolism. ACS Catal. 2011 (2011) 1075–1082. [PMID: 21897878]
2.  Esquirol, L., Peat, T.S., Wilding, M., Lucent, D., French, N.G., Hartley, C.J., Newman, J. and Scott, C. Structural and biochemical characterization of the biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminosarum bv. viciae 3841. PLoS One 13:e0192736 (2018). [PMID: 29425231]
3.  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. [DOI] [PMID: 29523689]
[EC 3.5.1.84 created 2000, modified 2008, modified 2019]
 
 
EC 3.5.1.131     
Accepted name: 1-carboxybiuret hydrolase
Reaction: 1-carboxybiuret + H2O = urea-1,3-dicarboxylate + NH3
For diagram of atrazine catabolism, click here
Glossary: carboxybiuret = carbamoylcarbamoylcarbamic acid
Other name(s): atzEG (gene names)
Systematic name: 1-carboxybiuret amidohydrolase
Comments: The enzyme, characterized from the bacterium Pseudomonas sp. ADP, participates in the degradation of cyanuric acid, an intermediate in the degradation of s-triazine herbicides such as atrazine [2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine]. The enzyme is a heterotetramer composed of a catalytic subunit (AtzE) and an accessory subunit (AtzG) that stabilizes the complex.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  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. [DOI] [PMID: 29523689]
[EC 3.5.1.131 created 2019]
 
 
EC 3.5.2.15     
Accepted name: cyanuric acid amidohydrolase
Reaction: cyanuric acid + H2O = 1-carboxybiuret
For diagram of atrazine catabolism, click here
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 biuret, but was later shown to be 1-carboxybiuret.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, 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. [DOI] [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. [DOI] [PMID: 29523689]
[EC 3.5.2.15 created 2000, modified 2008, modified 2019]
 
 
EC 3.5.4.42     
Accepted name: N-isopropylammelide isopropylaminohydrolase
Reaction: N-isopropylammelide + H2O = cyanuric acid + isopropylamine
For diagram of atrazine catabolism, click here
Glossary: N-isopropylammelide = 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine
cyanuric acid = s-triazine-2,4,6-triol
Other name(s): atzC (gene name)
Systematic name: N-isopropylammelide isopropylaminohydrolase
Comments: Requires Zn2+. This bacterial enzyme is involved in degradation of the herbicide atrazine. It can hydrolyse other N-substituted amino dihydroxy-s-triazine molecules, and prefers substrates with linear N-alkyl groups to those with branched alkyl groups.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 203810-02-0
References:
1.  Sadowsky, M.J., Tong, Z., de Souza, M. and Wackett, L.P. AtzC is a new member of the amidohydrolase protein superfamily and is homologous to other atrazine-metabolizing enzymes. J. Bacteriol. 180 (1998) 152–158. [PMID: 9422605]
2.  Shapir, N., Osborne, J.P., Johnson, G., Sadowsky, M.J. and Wackett, L.P. Purification, substrate range, and metal center of AtzC: the N-isopropylammelide aminohydrolase involved in bacterial atrazine metabolism. J. Bacteriol. 184 (2002) 5376–5384. [DOI] [PMID: 12218024]
3.  Balotra, S., Warden, A.C., Newman, J., Briggs, L.J., Scott, C. and Peat, T.S. X-ray structure and mutagenesis studies of the N-isopropylammelide isopropylaminohydrolase, AtzC. PLoS One 10:e0137700 (2015). [DOI] [PMID: 26390431]
[EC 3.5.4.42 created 2000 as EC 3.5.99.4, transferred 2016 to EC 3.5.4.42]
 
 
EC 3.5.4.43     
Accepted name: hydroxydechloroatrazine ethylaminohydrolase
Reaction: hydroxyatrazine + H2O = N-isopropylammelide + ethylamine
For diagram of atrazine catabolism, click here
Glossary: hydroxyatrazine = 4-(ethylamino)-6-(isopropylamino)-1,3,5-triazin-2-ol
N-isopropylammelide = 6-(isopropylamino)-1,3,5-triazine-2,4-diol
Other name(s): atzB (gene name); 2,4-dihydroxy-6-(isopropylamino)-1,3,5-triazine ethylaminohydrolase
Systematic name: hydroxyatrazine ethylaminohydrolase
Comments: Contains Zn2+. This bacterial enzyme is involved in degradation of the herbicide atrazine. The enzyme has a broad substrate range, and requires a monohydroxylated s-triazine ring with a minimum of one primary or secondary amine substituent and either a chloride or amine leaving group. It catalyses both deamination and dechlorination reactions.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc
References:
1.  Boundy-Mills, K.L., de Souza, M.L., Mandelbaum, R.T., Wackett, L.P. and Sadowsky, M.J. The atzB gene of Pseudomonas sp. strain ADP encodes the second enzyme of a novel atrazine degradation pathway. Appl. Environ. Microbiol. 63 (1997) 916–923. [PMID: 9055410]
2.  Seffernick, J.L., Aleem, A., Osborne, J.P., Johnson, G., Sadowsky, M.J. and Wackett, L.P. Hydroxyatrazine N-ethylaminohydrolase (AtzB): an amidohydrolase superfamily enzyme catalyzing deamination and dechlorination. J. Bacteriol. 189 (2007) 6989–6997. [DOI] [PMID: 17660279]
[EC 3.5.4.43 created 2000 as EC 3.5.99.3, transferred 2016 to EC 3.5.4.43]
 
 
EC 3.5.4.45     
Accepted name: melamine deaminase
Reaction: (1) melamine + H2O = ammeline + NH3
(2) ammeline + H2O = ammelide + NH3
Glossary: melamine = 2,4,6-triamino-1,3,5-triazine
ammeline = 4,6-diamino-1,3,5-triazin-2-ol
ammelide = 6-amino-1,3,5-triazine-2,4-diol
Other name(s): triA (gene name)
Systematic name: melamine aminohydrolase
Comments: The enzyme, isolated from the bacterium Acidovorax citrulli, performs the deamination of melamine 15-fold faster than the deamination of ammeline. It also has activity with 2-chloro-4,6-diamino-s-triazine, but has no activity toward halo-substituted triazine ring compounds such as atrazine (cf. EC 3.8.1.8, atrazine chlorohydrolase).
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Seffernick, J.L., Souza, M.L., Sadowsky, M.J. and Wackett, L.P. Melamine deaminase and atrazine chlorohydrolase: 98 percent identical but functionally different. J. Bacteriol. 183 (2001) 2405–2410. [DOI] [PMID: 11274097]
[EC 3.5.4.45 created 2017]
 
 
EC 3.5.99.3      
Transferred entry: hydroxydechloroatrazine ethylaminohydrolase. Now EC 3.5.4.43, hydroxydechloroatrazine ethylaminohydrolase
[EC 3.5.99.3 created 2000, deleted 2016]
 
 
EC 3.5.99.4      
Transferred entry: N-isopropylammelide isopropylaminohydrolase. Now EC 3.5.4.42, N-isopropylammelide isopropylaminohydrolase
[EC 3.5.99.4 created 2000, deleted 2016]
 
 
EC 3.8.1.8     
Accepted name: atrazine chlorohydrolase
Reaction: atrazine + H2O = hydroxyatrazine + chloride
For diagram of atrazine catabolism, click here
Glossary: atrazine = 6-chloro-N-ethyl-N′-isopropyl-1,3,5-triazine-2,4-diamine
hydroxyatrazine = 4-(ethylamino)-6-(isopropylamino)-1,3,5-triazin-2-ol
Other name(s): AtzA
Systematic name: atrazine chlorohydrolase
Comments: Involved in the degradation of the herbicide atrazine, 2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5-triazine, in bacteria.
Links to other databases: BRENDA, EAWAG-BBD, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 168680-16-8
References:
1.  de Souza, M.L., Wackett, L.P., Boundy-Mills, K.L., Mandelbaum, R.T. and Sadowsky, M.J. Cloning, characterization, and expression of a gene region from Pseudomonas sp. strain ADP involved in the dechlorination of atrazine. Appl. Environ. Microbiol. 61 (1995) 3373–3378. [PMID: 7574646]
2.  de Souza, M.L., Sadowsky, M.J. and Wackett, L.P. Atrazine chlorohydrolase from Pseudomonas sp. strain ADP: gene sequence, enzyme purification, and protein characterization. J. Bacteriol. 178 (1996) 4894–4900. [DOI] [PMID: 8759853]
[EC 3.8.1.8 created 2000, modified 2011]
 
 


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