Carboxylesterase family

From Wikipedia, the free encyclopedia

Carboxylesterase
Identifiers
Symbol COesterase
Pfam PF00135
InterPro IPR002018
PROSITE PDOC00112
SCOP 1acj
OPM family 135
OPM protein 1p0i
Available PDB structures:

1xlvA:29-550 1ehqA:30-550 1xlwA:29-550 1p0iA:29-550 1ehoA:30-550 1kcjA:30-550 1p0qA:29-550 1p0pA:29-550 1xluA:29-550 1p0mA:29-550 1j07A:32-563 1mahA:35-563 1n5mA:32-563 1n5rB:32-563 1c2oB:36-563 1q83A:32-563 1q84A:32-563 2c0qB:32-563 1maaA:32-563 1ku6A:32-563 2c0pA:32-563 1j06B:32-563 1c2bA:35-563 1puwA:37-563 1f8uA:32-563 1puvA:37-563 1b41A:36-563 2clj :35-563 1ea5A:22-545 1cfjA:22-545 1w76A:22-545 1vxoA:22-545 1gpnA:22-545 1jgbA:25-545 1qidA:22-545 2dfpA:23-545 2ace :25-545 2ack :25-545 1qiiA:22-545 1hbjA:22-545 1zgcA:22-545 1zgbA:22-545 1e66A:22-545 1eeaA:22-545 1qigA:22-545 1acl :25-545 1w4lA:22-545 1acj :25-545 1odcA:22-545 1qijA:22-545 1oce :25-545 1dx6A:22-545 1gpkA:22-545 1qihA:22-545 1qikA:22-545 1qtiA:22-545 1fssA:25-545 1e3qA:22-545 1w6rA:25-545 1qimA:22-545 1eve :23-545 1h23A:22-545 1ax9 :25-545 1qifA:22-545 1jgaA:25-545 1u65A:22-545 1w75B:22-545 1vot :25-545 1h22A:22-545 1vxrA:22-545 1gqrA:25-545 1ut6A:22-545 1jjbA:25-545 1qieA:22-545 1amn :25-545 1gqsA:25-545 1dx4A:39-601 1qo9A:39-601 1qonA:39-601 1k4yA:23-546 1yajD:21-547 1ya8A:21-547 1mx9G:19-547 1mx1B:19-547 1mx5C:19-547 1ya4B:21-547 1yahA:21-547 1jmyA:21-538 1f6wA:21-542 1akn :19-540 1aqlA:19-540 2bce :19-540 1qe3A:2-485 1c7jA:2-485 1c7iA:2-485 1thg :26-548 1llfB:16-533 1cleA:16-533 1lpo :16-533 1lps :16-533 1lpm :16-533 1trh :16-533 1lpn :16-533 1crl :16-533 1lpp :16-533 1gz7C:15-532 1ukcA:17-529


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

Higher eukaryotes have many distinct esterases. Among the different types are those which 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[1][2][3] that the majority are evolutionary 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.

Contents

[edit] Subfamilies

[edit] Human proteins containing this domain

ACHE; ARACHE; BCHE; CEL; CES; CES1; CES2; CES3; CES4; CES7; NLGN1; NLGN2; NLGN3; NLGN4X; NLGN4Y; TG;

[edit] References

  1. ^ Myers M, Richmond RC, Oakeshott JG (1988). "On the origins of esterases". Mol. Biol. Evol. 5 (2): 113–119. PMID 3163407. 
  2. ^ 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. PMID 1862088. 
  3. ^ 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. PMID 8453375. 

[edit] External links

 This membrane protein-related article is a stub. You can help Wikipedia by expanding it.