EzCatDB: S00348

DB codeS00348
RLCP classification1.19.30000.41
CATH domainDomain 13.40.50.1820Catalytic domain
E.C.3.1.1.45
CSA1din

CATH domainRelated DB codes (homologues)
3.40.50.1820S00544,S00344,S00517,S00525,S00526,S00720,S00723,S00724,S00725,S00919,S00057,S00374,S00345,S00347,S00346,S00350,S00352,S00353,S00355,S00356,S00358,D00189,D00210,D00539,T00253

Enzyme Name
Swiss-protKEGG

P0A114P0A115
Protein nameCarboxymethylenebutenolidaseCarboxymethylenebutenolidasecarboxymethylenebutenolidase
maleylacetate enol-lactonase
dienelactone hydrolase
carboxymethylene butenolide hydrolase
SynonymsEC 3.1.1.45
Dienelactone hydrolase
DLH
EC 3.1.1.45
Dienelactone hydrolase
DLH

KEGG pathways
MAP codePathways
MAP00361gamma-Hexachlorocyclohexane degradation
MAP00364Fluorobenzoate degradation
MAP006271,4-Dichlorobenzene degradation

Swiss-prot:Accession NumberP0A114P0A115
Entry nameCLCD_PSEPUCLCD_PSESB
Activity4-carboxymethylenebut-2-en-4-olide + H(2)O = 4-oxohex-2-enedioate.4-carboxymethylenebut-2-en-4-olide + H(2)O = 4-oxohex-2-enedioate.
SubunitMonomer.Monomer.
Subcellular location

Cofactor



SubstratesProducts
KEGG-idC04431C00001C02222
Compound4-Carboxymethylenebut-2-en-4-olideH2O4-Oxohex-2-enedioate
Typecarbohydrate,carboxyl groupH2Ocarbohydrate,carboxyl group
1dinAUnbound
Unbound
1ggvAUnbound
Unbound

Active-site residues
pdbCatalytic residuesModified residuescomment
1dinAASP 171;HIS 202
CSD 123(modified CYS)

1ggvAASP 171;HIS 202
SEB 123(O-benzylsulfonyl-serine)
mutant C123S

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Fig.127

references
[1]
CommentsX-ray crystallography (2.8 Angstroms)
Medline ID89125597
PubMed ID3221394
JournalJ Mol Biol
Year1988
Volume204
Pages435-45
AuthorsPathak D, Ngai KL, Ollis D
TitleX-ray crystallographic structure of dienelactone hydrolase at 2.8 A.
[2]
CommentsX-ray crystallography (1.8 Angstroms)
Medline ID90339491
PubMed ID2380986
JournalJ Mol Biol
Year1990
Volume214
Pages497-525
AuthorsPathak D, Ollis D
TitleRefined structure of dienelactone hydrolase at 1.8 A.
Related PDB1din
[3]
Commentscatalysis
PubMed ID1866431
JournalProteins
Year1991
Volume9
Pages267-79
AuthorsPathak D, Ashley G, Ollis D
TitleThiol protease-like active site found in the enzyme dienelactone hydrolase: localization using biochemical, genetic, and structural tools.
[4]
Commentscatalysis
PubMed ID8497485
JournalProteins
Year1993
Volume16
Pages64-78
AuthorsCheah E, Ashley GW, Gary J, Ollis D
TitleCatalysis by dienelactone hydrolase: a variation on the protease mechanism.
[5]
Commentscatalysis(theoritical study)
PubMed ID7630883
JournalProtein Eng
Year1995
Volume8
Pages135-42
AuthorsBeveridge AJ, Ollis DL
TitleA theoretical study of substrate-induced activation of dienelactone hydrolase.
[6]
CommentsNMR, catalysis
PubMed ID8647073
JournalEur J Biochem
Year1996
Volume237
Pages357-66
AuthorsPrucha M, Wray V, Pieper DH
TitleMetabolism of 5-chlorosubstituted muconolactones.
[7]
CommentsX-ray crystallography (1.8 Angstroms)
PubMed ID9438866
JournalStructure
Year1997
Volume5
Pages1571-84
AuthorsKim KK, Song HK, Shin DH, Hwang KY, Choe S, Yoo OJ, Suh SW
TitleCrystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity.
Related PDB1auo,1aur
[8]
CommentsX-ray crystallography (2.5 Angstroms)
PubMed ID11053834
JournalActa Crystallogr D
Year2000
Volume56
Pages1376-84
AuthorsRobinson A, Edwards KJ, Carr PD, Barton JD, Ewart GD, Ollis DL
TitleStructure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF).
Related PDB1ggv

comments
According to the literature [4], The mechanism of this enzyme, DLH, appears to differ from the other homologous proteases in the two ways. Firstly, DLH seems to protonate the incipient leaving group only after the collapse of the first tetrahedral intermediate, rendering DLH incapable of hydrolyzing amide analogues of its ester substrate. Secondly, the histidine residue in the catalytic triad probably does not protonate the leaving group (enolate) or deprotonate the water for deacylation; rather, the enolate anion itself abstracts a proton from water, thereby supplying the hydroxyl for deacylation.

createdupdated
2002-07-042009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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