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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]

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]

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]

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]

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]

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]