ExplorEnz: EC 3.5.1.137

Your query returned 1 entry. Printable version

3.5.1.137

Accepted name:

N-methylcarbamate hydrolase

Reaction:

an N-methyl carbamate ester + H₂O = an alcohol + methylamine + CO₂

Glossary:

carbaryl = N-methyl-1-naphthyl carbamate

Other name(s):

mcbA (gene name); cehA (gene name); cfdJ (gene name); carbaryl hydrolase; carbofuran hydrolase

Systematic name:

N-methyl carbamate ester hydrolase

Comments:

The enzyme catalyses the first step in the degradation of several carbamate insecticides such as carbaryl, carbofuran, isoprocarb, propoxur, aldicarb and oxamyl. It catalyses the cleavage of the ester bond to release N-methylcarbamate, which spontaneously hydrolyses to methylamine and CO₂. The enzymes from several Gram-negative bacteria were shown to be located in the periplasm.

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc

References:

1.	Mulbry, W.W. and Eaton, R.W. Purification and characterization of the N-methylcarbamate hydrolase from Pseudomonas strain CRL-OK. Appl. Environ. Microbiol. 57 (1991) 3679–3682. [PMID: 1785941]
2.	Hayatsu, M. and Nagata, T. Purification and characterization of carbaryl hydrolase from Blastobacter sp. strain M501. Appl. Environ. Microbiol. 59 (1993) 2121–2125. [PMID: 16348989]
3.	Chapalmadugu, S. and Chaudhry, G.R. Isolation of a constitutively expressed enzyme for hydrolysis of carbaryl in Pseudomonas aeruginosa. J. Bacteriol. 175 (1993) 6711–6716. [DOI] [PMID: 8407847]
4.	Hayatsu, M., Mizutani, A., Hashimoto, M., Sato, K. and Hayano, K. Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100. FEMS Microbiol. Lett. 201 (2001) 99–103. [DOI] [PMID: 11445174]
5.	Hashimoto, M., Fukui, M., Hayano, K. and Hayatsu, M. Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100. Appl. Environ. Microbiol. 68 (2002) 1220–1227. [DOI] [PMID: 11872471]
6.	Zhang, Q., Liu, Y. and Liu, Y.H. Purification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168. FEMS Microbiol. Lett. 228 (2003) 39–44. [DOI] [PMID: 14612234]
7.	Ozturk, B., Ghequire, M., Nguyen, T.P., De Mot, R., Wattiez, R. and Springael, D. Expanded insecticide catabolic activity gained by a single nucleotide substitution in a bacterial carbamate hydrolase gene. Environ. Microbiol. 18 (2016) 4878–4887. [DOI] [PMID: 27312345]
8.	Kamini, Shetty, D., Trivedi, V.D., Varunjikar, M. and Phale, P.S. Compartmentalization of the carbaryl degradation pathway: molecular characterization of inducible periplasmic carbaryl hydrolase from Pseudomonas spp. Appl. Environ. Microbiol. 84:e02115-17 (2018). [DOI] [PMID: 29079626]
9.	Yan, X., Jin, W., Wu, G., Jiang, W., Yang, Z., Ji, J., Qiu, J., He, J., Jiang, J. and Hong, Q. Hydrolase CehA and monooxygenase CfdC are responsible for carbofuran degradation in Sphingomonas sp. strain CDS-1. Appl. Environ. Microbiol. 84 (2018) . [DOI] [PMID: 29884759]
10.	Jiang, W., Gao, Q., Zhang, L., Wang, H., Zhang, M., Liu, X., Zhou, Y., Ke, Z., Wu, C., Qiu, J. and Hong, Q. Identification of the key amino acid sites of the carbofuran hydrolase CehA from a newly isolated carbofuran-degrading strain Sphingbium sp. CFD-1. Ecotoxicol Environ Saf 189:109938 (2020). [DOI] [PMID: 31759739]

[EC 3.5.1.137 created 2021]