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Carboxylesterase type B

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(Redirected from Carboxylesterase family)
Carboxylesterase
Structure of ethylphosphorylated Butyrylcholinesterase.[1]
Identifiers
SymbolCOesterase
PfamPF00135
InterProIPR002018
PROSITEPDOC00112
SCOP21acj / SCOPe / SUPFAM
OPM superfamily127
OPM protein1p0i
CDDcd00312
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Carboxylesterase, type B is a family of evolutionarily related proteins that belongs to the superfamily of proteins with the Alpha/beta hydrolase fold.

Higher eukaryotes have many distinct esterases. The different types include those that act on carboxylic esters (EC 3.1.1). Carboxyl-esterases have been classified into three categories (A, B and C) on the basis of differential patterns of inhibition by organophosphates. The sequence of a number of type-B carboxylesterases indicates[2][3][4] that the majority are evolutionarily related. As is the case for lipases and serine proteases, the catalytic apparatus of esterases involves three residues (catalytic triad): a serine, a glutamate or aspartate and a histidine.

Subfamilies

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Examples

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Human genes that encode proteins containing the carboxylesterase domain include:

See also

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References

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  1. ^ Nachon F, Asojo OA, Borgstahl GE, Masson P, Lockridge O (February 2005). "Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging". Biochemistry. 44 (4): 1154–62. CiteSeerX 10.1.1.529.7283. doi:10.1021/bi048238d. PMID 15667209.
  2. ^ Myers M, Richmond RC, Oakeshott JG (1988). "On the origins of esterases". Mol. Biol. Evol. 5 (2): 113–119. doi:10.1093/oxfordjournals.molbev.a040485. PMID 3163407.
  3. ^ Chatonnet A, Krejci E, Duval N, Vincens P, Massoulie J (1991). "Cholinesterase-like domains in enzymes and structural proteins: functional and evolutionary relationships and identification of a catalytically essential aspartic acid". Proc. Natl. Acad. Sci. U.S.A. 88 (15): 6647–6651. Bibcode:1991PNAS...88.6647K. doi:10.1073/pnas.88.15.6647. PMC 52145. PMID 1862088.
  4. ^ Sussman JL, Cygler M, Harel M, Silman I, Schrag JD, Doctor BP, Gentry MK (1993). "Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins". Protein Sci. 2 (3): 366–382. doi:10.1002/pro.5560020309. PMC 2142374. PMID 8453375.
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