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InterPro: IPR019819 Carboxylesterase type B, conserved site

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1513 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession

IPR019819 Carboxylesterase_B_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00941	CARBOXYLESTERASE_B_2	1513
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000997 Cholinesterase
IPR001445 Acetylcholinesterase, insect
IPR002018 Carboxylesterase, type B
IPR016324 Thyroglobulin

InterPro annotation

Entry Details in BioMart

Abstract

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.

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 entry represents a well conserved site located in the N-terminal section, which contains a cysteine involved in a disulphide bond. Human esterase-D, also a type-B carboxylesterase, does not seem to be evolutionary related.

Structural links Help

PDB - click here

SCOP: c.69.1.1 , c.69.1.17

CATH: 3.40.50.1820

Database links Help

Enzyme: EC:3.1.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR019819

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P06276 Cholinesterase

P07140 Acetylcholinesterase

P21836 Acetylcholinesterase

P37967 Para-nitrobenzyl esterase

P38433 Acetylcholinesterase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002018	Carboxylesterase, type B
IPR019819	Carboxylesterase type B, conserved site
IPR001445	Acetylcholinesterase, insect
IPR019826	Carboxylesterase type B, active site
IPR000997	Cholinesterase
IPR014788	Acetylcholinesterase, tetramerisation
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Myers M, Richmond RC, Oakeshott JG. On the origins of esterases. Mol. Biol. Evol. 5 113-9 1988 [PubMed: 3163407] http://mbe.oxfordjournals.org/cgi/content/abstract/5/2/113.pdf
2.	Krejci E, Duval N, Chatonnet A, Vincens P, Massoulie J. 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 6647-51 1991 [PubMed: 1862088] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=1862088
3.	Cygler M, Schrag JD, Sussman JL, Harel M, Silman I, Gentry MK, Doctor BP. Relationship between sequence conservation and three-dimensional structure in a large family of esterases, lipases, and related proteins. Protein Sci. 2 366-82 1993 [PubMed: 8453375] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=8453375

Additional Reading Open in usermanual
	Wang CS, Hartsuck JA. Bile salt-activated lipase. A multiple function lipolytic enzyme. Biochim. Biophys. Acta 1166 1993 1-19 [PubMed: 8431483] http://dx.doi.org/10.1016/0005-2760(93)90277-G
	Koehnke J, Jin X, Budreck EC, Posy S, Scheiffele P, Honig B, Shapiro L. Crystal structure of the extracellular cholinesterase-like domain from neuroligin-2. Proc. Natl. Acad. Sci. U.S.A. 105 2008 1873-8 [PubMed: 18250328] http://dx.doi.org/10.1073/pnas.0711701105
	Chen X, Liu H, Shim AH, Focia PJ, He X. Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. Nat. Struct. Mol. Biol. 15 2008 50-6 [PubMed: 18084303] http://dx.doi.org/10.1038/nsmb1350
	Colletier JP, Bourgeois D, Sanson B, Fournier D, Sussman JL, Silman I, Weik M. Shoot-and-Trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography. Proc. Natl. Acad. Sci. U.S.A. 105 2008 11742-7 [PubMed: 18701720] http://dx.doi.org/10.1073/pnas.0804828105
	Harel M, Sonoda LK, Silman I, Sussman JL, Rosenberry TL. Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site. J. Am. Chem. Soc. 130 2008 7856-61 [PubMed: 18512913] http://dx.doi.org/10.1021/ja7109822
	Fleming CD, Edwards CC, Kirby SD, Maxwell DM, Potter PM, Cerasoli DM, Redinbo MR. Crystal structures of human carboxylesterase 1 in covalent complexes with the chemical warfare agents soman and tabun. Biochemistry 46 2007 5063-71 [PubMed: 17407327] http://dx.doi.org/10.1021/bi700246n
	Lockridge O. Structure of human serum cholinesterase. Bioessays 9 1988 125-8 [PubMed: 3067729] http://dx.doi.org/10.1002/bies.950090406

InterPro 24.0