Carboxylesterase family

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Carboxylesterase
PDB 1xlv EBI.jpg
Structure of ethylphosphorylated Butyrylcholinesterase.[1]
Identifiers
Symbol COesterase
Pfam PF00135
InterPro IPR002018
PROSITE PDOC00112
SCOP 1acj
SUPERFAMILY 1acj
OPM superfamily 135
OPM protein 1p0i

Carboxylesterase, type B is a family of evolutionarily related proteins.

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. This family belongs to the superfamily of proteins with the Alpha/beta hydrolase fold.

Subfamilies[edit]

Examples[edit]

Human genes that encode proteins containing the carboxylesterase domain include:

See also[edit]

References[edit]

  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. 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. 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. 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. 

External links[edit]