KEGG   ENZYME: 3.5.1.137
Entry
EC 3.5.1.137                Enzyme                                 
Name
N-methylcarbamate hydrolase;
mcbA (gene name);
cehA (gene name);
cfdJ (gene name);
carbaryl hydrolase;
carbofuran hydrolase
Class
Hydrolases;
Acting on carbon-nitrogen bonds, other than peptide bonds;
In linear amides
Sysname
N-methyl carbamate ester hydrolase
Reaction(IUBMB)
an N-methyl carbamate ester + H2O = an alcohol + methylamine + CO2 [RN:R12942]
Reaction(KEGG)
R12942
Substrate
N-methyl carbamate ester [CPD:C22461];
H2O [CPD:C00001]
Product
alcohol [CPD:C00069];
methylamine [CPD:C00218];
CO2 [CPD:C00011]
Comment
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.
History
EC 3.5.1.137 created 2021
Orthology
K25604  N-methylcarbamate hydrolase
Genes
SPHBEP837_03959
Reference
1  [PMID:1785941]
  Authors
Mulbry WW, Eaton RW.
  Title
Purification and characterization of the N-methylcarbamate hydrolase from Pseudomonas strain CRL-OK.
  Journal
Appl Environ Microbiol 57:3679-82 (1991)
DOI:10.1128/aem.57.12.3679-3682.1991
Reference
2  [PMID:16348989]
  Authors
Hayatsu M, Nagata T.
  Title
Purification and Characterization of Carbaryl Hydrolase from Blastobacter sp. Strain M501.
  Journal
Appl Environ Microbiol 59:2121-5 (1993)
DOI:10.1128/aem.59.7.2121-2125.1993
Reference
3  [PMID:8407847]
  Authors
Chapalmadugu S, Chaudhry GR.
  Title
Isolation of a constitutively expressed enzyme for hydrolysis of carbaryl in Pseudomonas aeruginosa.
  Journal
J Bacteriol 175:6711-6 (1993)
DOI:10.1128/jb.175.20.6711-6716.1993
Reference
4  [PMID:11445174]
  Authors
Hayatsu M, Mizutani A, Hashimoto M, Sato K, Hayano K.
  Title
Purification and characterization of carbaryl hydrolase from Arthrobacter sp. RC100.
  Journal
FEMS Microbiol Lett 201:99-103 (2001)
DOI:10.1111/j.1574-6968.2001.tb10739.x
Reference
5  [PMID:11872471]
  Authors
Hashimoto M, Fukui M, Hayano K, Hayatsu M.
  Title
Nucleotide sequence and genetic structure of a novel carbaryl hydrolase gene (cehA) from Rhizobium sp. strain AC100.
  Journal
Appl Environ Microbiol 68:1220-7 (2002)
DOI:10.1128/AEM.68.3.1220-1227.2002
  Sequence
Reference
6  [PMID:14612234]
  Authors
Zhang Q, Liu Y, Liu YH.
  Title
Purification and characterization of a novel carbaryl hydrolase from Aspergillus niger PY168.
  Journal
FEMS Microbiol Lett 228:39-44 (2003)
DOI:10.1016/S0378-1097(03)00718-3
Reference
7  [PMID:27312345]
  Authors
Ozturk B, Ghequire M, Nguyen TP, De Mot R, Wattiez R, Springael D.
  Title
Expanded insecticide catabolic activity gained by a single nucleotide substitution in a bacterial carbamate hydrolase gene.
  Journal
Environ Microbiol 18:4878-4887 (2016)
DOI:10.1111/1462-2920.13409
  Sequence
Reference
8  [PMID:29079626]
  Authors
Kamini, Shetty D, Trivedi VD, Varunjikar M, Phale PS.
  Title
Compartmentalization of the Carbaryl Degradation Pathway: Molecular Characterization of Inducible Periplasmic Carbaryl Hydrolase from Pseudomonas spp.
  Journal
Appl Environ Microbiol 84:e02115-17 (2018)
DOI:10.1128/AEM.02115-17
Reference
9  [PMID:29884759]
  Authors
Yan X, Jin W, Wu G, Jiang W, Yang Z, Ji J, Qiu J, He J, Jiang J, Hong Q.
  Title
Hydrolase CehA and Monooxygenase CfdC Are Responsible for Carbofuran Degradation in Sphingomonas sp. Strain CDS-1.
  Journal
Appl Environ Microbiol 84:e00805-18 (2018)
DOI:10.1128/AEM.00805-18
Reference
10 [PMID:31759739]
  Authors
Jiang W, Gao Q, Zhang L, Wang H, Zhang M, Liu X, Zhou Y, Ke Z, Wu C, Qiu J, Hong Q.
  Title
Identification of the key amino acid sites of the carbofuran hydrolase CehA from a newly isolated carbofuran-degrading strain Sphingbium sp. CFD-1.
  Journal
Ecotoxicol Environ Saf 189:109938 (2020)
DOI:10.1016/j.ecoenv.2019.109938
Other DBs
ExplorEnz - The Enzyme Database: 3.5.1.137
IUBMB Enzyme Nomenclature: 3.5.1.137
ExPASy - ENZYME nomenclature database: 3.5.1.137
BRENDA, the Enzyme Database: 3.5.1.137

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