ExplorEnz: EC 3.5.4.42

Your query returned 1 entry. Printable version

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, Gene, 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]