KEGG ENZYME: 3.5.1.137

EC 3.5.1.137                Enzyme                                 


Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides

N-methyl carbamate ester hydrolase

an N-methyl carbamate ester + H2O = an alcohol + methylamine + CO2 [RN:R12942]

N-methyl carbamate ester [CPD:C22461];
H2O [CPD:C00001]

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.

EC 3.5.1.137 created 2021

Mulbry WW, Eaton RW.

Purification and characterization of the N-methylcarbamate hydrolase from Pseudomonas strain CRL-OK.

Hayatsu M, Nagata T.

Purification and Characterization of Carbaryl Hydrolase from Blastobacter sp. Strain M501.

Chapalmadugu S, Chaudhry GR.

Isolation of a constitutively expressed enzyme for hydrolysis of carbaryl in Pseudomonas aeruginosa.

Hayatsu M, Mizutani A, Hashimoto M, Sato K, Hayano K.

Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100.

Hashimoto M, Fukui M, Hayano K, Hayatsu M.

Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100.

Zhang Q, Liu Y, Liu YH.

Purification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168.

Ozturk B, Ghequire M, Nguyen TP, De Mot R, Wattiez R, Springael D.

Expanded insecticide catabolic activity gained by a single nucleotide substitution in a bacterial carbamate hydrolase gene.

Kamini, Shetty D, Trivedi VD, Varunjikar M, Phale PS.

Compartmentalization of the Carbaryl Degradation Pathway: Molecular Characterization of Inducible Periplasmic Carbaryl Hydrolase from Pseudomonas spp.

Yan X, Jin W, Wu G, Jiang W, Yang Z, Ji J, Qiu J, He J, Jiang J, Hong Q.

Hydrolase CehA and Monooxygenase CfdC Are Responsible for Carbofuran Degradation in Sphingomonas sp. Strain CDS-1.

Jiang W, Gao Q, Zhang L, Wang H, Zhang M, Liu X, Zhou Y, Ke Z, Wu C, Qiu J, 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.