Pyrethroid hydrolase

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Pyrethroid hydrolase
Identifiers
EC no. 3.1.1.88
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The enzyme pyrethroid hydrolase (EC 3.1.1.88, pyrethroid-hydrolyzing carboxylesterase, pyrethroid-hydrolysing esterase, pyrethroid-hydrolyzing esterase, pyrethroid-selective esterase, pyrethroid-cleaving enzyme, permethrinase, PytH, EstP; systematic name pyrethroid-ester hydrolase) [1] [2] [3] [4] [5] [6] catalyses the reaction

trans-permethrin + H2O (3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate

The enzyme is involved in degradation of pyrethroid pesticides.

Related Research Articles

Hydrolase is a class of enzymes that commonly perform as biochemical catalysts that use water to break a chemical bond, which typically results in dividing a larger molecule into smaller molecules. Some common examples of hydrolase enzymes are esterases including lipases, phosphatases, glycosidases, peptidases, and nucleosidases.

<span class="mw-page-title-main">Monoacylglycerol lipase</span> Class of enzymes

Monoacylglycerol lipase is an enzyme that, in humans, is encoded by the MGLL gene. MAGL is a 33-kDa, membrane-associated member of the serine hydrolase superfamily and contains the classical GXSXG consensus sequence common to most serine hydrolases. The catalytic triad has been identified as Ser122, His269, and Asp239.

Paenarthrobacter ureafaciens KI72, popularly known as nylon-eating bacteria, is a strain of Paenarthrobacter ureafaciens that can digest certain by-products of nylon 6 manufacture. It uses a set of enzymes to digest nylon, popularly known as nylonase.

Cauxin is a carboxylesterase that is excreted in large amounts in cat urine. There is also evidence that it can serve as a peptide hydrolase in the production of cat pheromone precursors. Cauxin has a mass of 70 kilodaltons and is composed of 545 amino acids. The protein can also exist as a multimeric protein complex connected by disulfide bonds with a mass of 300-350 kilodaltons. This is its primary form in non-reducing conditions. The proximal tubules of epithelial cells in the kidney express cauxin. This protein is secreted into the urine from the renal tubular cells. The gene for the protein is also found in several other mammalian genomes in various organs. However, the only mammals that have cauxin present in urine are cats. It is also the first carboxylesterase to be found in urine.

The enzyme acetylsalicylate deacetylase (EC 3.1.1.55) catalyzes the reaction

<span class="mw-page-title-main">Aryldialkylphosphatase</span>

Aryldialkylphosphatase is a metalloenzyme that hydrolyzes the triester linkage found in organophosphate insecticides:

The enzyme carboxylesterase (or carboxylic-ester hydrolase, EC 3.1.1.1; systematic name carboxylic-ester hydrolase) catalyzes reactions of the following form:

The enzyme feruloyl esterase (EC 3.1.1.73) catalyzes the reaction

The enzyme lysophospholipase (EC 3.1.1.5) catalyzes the reaction

The enzyme tannase (EC 3.1.1.20) catalyzes the following reaction:

<span class="mw-page-title-main">Carboxylesterase 1</span> Protein-coding gene in the species Homo sapiens

Liver carboxylesterase 1 also known as carboxylesterase 1 is an enzyme that in humans is encoded by the CES1 gene. The protein is also historically known as serine esterase 1 (SES1), monocyte esterase and cholesterol ester hydrolase (CEH). Three transcript variants encoding three different isoforms have been found for this gene. The various protein products from isoform a, b and c range in size from 568, 567 and 566 amino acids long, respectively.

<span class="mw-page-title-main">Carboxylesterase 2</span> Enzyme hydrolysing long-chain fatty esters

Carboxylesterase 2 is an enzyme that in humans is encoded by the CES2 gene. It is a member of the alpha/beta fold hydrolase family.

<span class="mw-page-title-main">Lactonase</span>

Lactonase (EC 3.1.1.81, acyl-homoserine lactonase; systematic name N-acyl-L-homoserine-lactone lactonohydrolase) is a metalloenzyme, produced by certain species of bacteria, which targets and inactivates acylated homoserine lactones (AHLs). It catalyzes the reaction

<span class="mw-page-title-main">Triacylglycerol lipase</span>

The enzyme triacylglycerol lipase (also triglyceride lipase, EC 3.1.1.3;systematic name triacylglycerol acylhydrolase) catalyses the hydrolysis of ester linkages of triglycerides:

The enzyme cocaine esterase (EC 3.1.1.84, CocE, hCE2, hCE-2, human carboxylesterase 2; systematic name cocaine benzoylhydrolase) catalyses the reaction

The enzyme Pimelyl-[acyl-carrier protein] methyl ester esterase (EC 3.1.1.85, BioH; systematic name pimelyl-[acyl-carrier protein] methyl ester hydrolase catalyses the reaction

<span class="mw-page-title-main">ABHD6</span> Protein-coding gene in the species Homo sapiens

alpha/beta-Hydrolase domain containing 6 (ABHD6), also known as monoacylglycerol lipase ABHD6 or 2-arachidonoylglycerol hydrolase is an enzyme that in humans is encoded by the ABHD6 gene.

<span class="mw-page-title-main">Juvenile hormone epoxide hydrolase</span>

Juvenile hormone epoxide hydrolase (JHEH) is an enzyme that inactivates insect juvenile hormones. This inactivation is accomplished through hydrolysis of the epoxide functional group contained within these hormones into diols. JHEH is one of two enzymes involved in the termination of signaling properties of the various juvenile hormones. The other is juvenile-hormone esterase, or JHE.

Streptomyces diastaticus is an alkaliphilic and thermophilic bacterium species from the genus of Streptomyces. Streptomyces diastaticus produces oligomycin A, oligomycin C, rimocidin and the leukotriene-A4 hydrolase-inhibitor 8(S)-amino-2(R)-methyl-7-oxononanoic acid. Streptomyces diastaticus also produces gougerotin and diastaphenazine and the antibiotic ruticin.

Sphingobacterium olei is a Gram-stain-negative, rod-shaped, and non-motile bacterium. It was first isolated from oil-contaminated soil in Daqing oil field, China. S. olei has been found to be able to degrade herbicides quizalofop-p-ethyl and diclofop-methyl. Before a name was given, S. olei was designated as strain HAL-9T. The species name olei means "of oil" in Latin.

References

  1. Wang BZ, Guo P, Hang BJ, Li L, He J, Li SP (September 2009). "Cloning of a novel pyrethroid-hydrolyzing carboxylesterase gene from Sphingobium sp. strain JZ-1 and characterization of the gene product". Applied and Environmental Microbiology. 75 (17): 5496–500. doi:10.1128/aem.01298-09. PMC   2737939 . PMID   19581484.
  2. Wu PC, Liu YH, Wang ZY, Zhang XY, Li H, Liang WQ, Luo N, Hu JM, Lu JQ, Luan TG, Cao LX (February 2006). "Molecular cloning, purification, and biochemical characterization of a novel pyrethroid-hydrolyzing esterase from Klebsiella sp. strain ZD112". Journal of Agricultural and Food Chemistry. 54 (3): 836–42. doi:10.1021/jf052691u. PMID   16448191.
  3. Liang WQ, Wang ZY, Li H, Wu PC, Hu JM, Luo N, Cao LX, Liu YH (September 2005). "Purification and characterization of a novel pyrethroid hydrolase from Aspergillus niger ZD11". Journal of Agricultural and Food Chemistry. 53 (19): 7415–20. doi:10.1021/jf051460k. PMID   16159167.
  4. Stok JE, Huang H, Jones PD, Wheelock CE, Morisseau C, Hammock BD (July 2004). "Identification, expression, and purification of a pyrethroid-hydrolyzing carboxylesterase from mouse liver microsomes". The Journal of Biological Chemistry. 279 (28): 29863–9. doi: 10.1074/jbc.m403673200 . PMID   15123619.
  5. Maloney SE, Maule A, Smith AR (July 1993). "Purification and preliminary characterization of permethrinase from a pyrethroid-transforming strain of Bacillus cereus". Applied and Environmental Microbiology. 59 (7): 2007–13. PMC   182228 . PMID   8357241.
  6. Guo, P.; Wang, B.; Hang, B.; Li, L.; Ali, W.; He, J.; Li, S. (2009). "Pyrethroid-degrading Sphingobium sp. JZ-2 and the purification and characterization of a novel pyrethroid hydrolase". Int. Biodeter. Biodegrad. 63 (8): 1107–1112. doi:10.1016/j.ibiod.2009.09.008.