DB code: S00348

RLCP classification 1.19.30000.41 : Hydrolysis
CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 3.1.1.45
CSA 1din
M-CSA 1din
MACiE

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

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P0A114 Carboxymethylenebutenolidase
EC 3.1.1.45
Dienelactone hydrolase
DLH
PF01738 (DLH)
[Graphical View]
P0A115 Carboxymethylenebutenolidase
EC 3.1.1.45
Dienelactone hydrolase
DLH
PF01738 (DLH)
[Graphical View]

KEGG enzyme name
carboxymethylenebutenolidase
maleylacetate enol-lactonase
dienelactone hydrolase
carboxymethylene butenolide hydrolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P0A114 CLCD_PSEPU 4-carboxymethylenebut-2-en-4-olide + H(2)O = 4-oxohex-2-enedioate. Monomer.
P0A115 CLCD_PSESB 4-carboxymethylenebut-2-en-4-olide + H(2)O = 4-oxohex-2-enedioate. Monomer.

KEGG Pathways
Map code Pathways E.C.
MAP00361 gamma-Hexachlorocyclohexane degradation
MAP00364 Fluorobenzoate degradation
MAP00627 1,4-Dichlorobenzene degradation

Compound table
Substrates Products Intermediates
KEGG-id C04431 C00001 C02222
E.C.
Compound 4-Carboxymethylenebut-2-en-4-olide H2O 4-Oxohex-2-enedioate
Type carbohydrate,carboxyl group H2O carbohydrate,carboxyl group
ChEBI 18371
 18371
 		15377
 15377
 		1184
 1184
PubChem 5459914
 5459914
 		22247451
 962
 22247451
 962
 		5280500
 5280500
1dinA Unbound Unbound
1ggvA Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1dinA ASP 171;HIS 202 CSD 123(modified CYS)
1ggvA ASP 171;HIS 202 SEB 123(O-benzylsulfonyl-serine) mutant C123S

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
Fig.12 7

References
[1]
Resource
Comments X-ray crystallography (2.8 Angstroms)
Medline ID 89125597
PubMed ID 3221394
Journal J Mol Biol
Year 1988
Volume 204
Pages 435-45
Authors Pathak D, Ngai KL, Ollis D
Title X-ray crystallographic structure of dienelactone hydrolase at 2.8 A.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-ray crystallography (1.8 Angstroms)
Medline ID 90339491
PubMed ID 2380986
Journal J Mol Biol
Year 1990
Volume 214
Pages 497-525
Authors Pathak D, Ollis D
Title Refined structure of dienelactone hydrolase at 1.8 A.
Related PDB 1din
Related UniProtKB
[3]
Resource
Comments catalysis
Medline ID
PubMed ID 1866431
Journal Proteins
Year 1991
Volume 9
Pages 267-79
Authors Pathak D, Ashley G, Ollis D
Title Thiol protease-like active site found in the enzyme dienelactone hydrolase: localization using biochemical, genetic, and structural tools.
Related PDB
Related UniProtKB
[4]
Resource
Comments catalysis
Medline ID
PubMed ID 8497485
Journal Proteins
Year 1993
Volume 16
Pages 64-78
Authors Cheah E, Ashley GW, Gary J, Ollis D
Title Catalysis by dienelactone hydrolase: a variation on the protease mechanism.
Related PDB
Related UniProtKB
[5]
Resource
Comments catalysis(theoritical study)
Medline ID
PubMed ID 7630883
Journal Protein Eng
Year 1995
Volume 8
Pages 135-42
Authors Beveridge AJ, Ollis DL
Title A theoretical study of substrate-induced activation of dienelactone hydrolase.
Related PDB
Related UniProtKB
[6]
Resource
Comments NMR, catalysis
Medline ID
PubMed ID 8647073
Journal Eur J Biochem
Year 1996
Volume 237
Pages 357-66
Authors Prucha M, Wray V, Pieper DH
Title Metabolism of 5-chlorosubstituted muconolactones.
Related PDB
Related UniProtKB
[7]
Resource
Comments X-ray crystallography (1.8 Angstroms)
Medline ID
PubMed ID 9438866
Journal Structure
Year 1997
Volume 5
Pages 1571-84
Authors Kim KK, Song HK, Shin DH, Hwang KY, Choe S, Yoo OJ, Suh SW
Title Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity.
Related PDB 1auo 1aur
Related UniProtKB
[8]
Resource
Comments X-ray crystallography (2.5 Angstroms)
Medline ID
PubMed ID 11053834
Journal Acta Crystallogr D
Year 2000
Volume 56
Pages 1376-84
Authors Robinson A, Edwards KJ, Carr PD, Barton JD, Ewart GD, Ollis DL
Title Structure of the C123S mutant of dienelactone hydrolase (DLH) bound with the PMS moiety of the protease inhibitor phenylmethylsulfonyl fluoride (PMSF).
Related PDB 1ggv
Related UniProtKB

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.

Created Updated
2002-07-04 2009-02-26