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Information on EC 3.1.1.45 - carboxymethylenebutenolidase and Organism(s) Pseudomonas knackmussii and UniProt Accession P0A115

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.45 carboxymethylenebutenolidase
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This record set is specific for:
Pseudomonas knackmussii
UNIPROT: P0A115 not found.
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The taxonomic range for the selected organisms is: Pseudomonas knackmussii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dienelactone hydrolase, trans-dienelactone hydrolase, carboxymethylenebutenolidase, trans-dlh, carboxymethylenebutenolidase homolog, 4-carboxymethylenebut-2-en-4-olide hydrolase, cis-dienelactone hydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4-carboxymethylenebut-2-en-4-olide hydrolase
-
-
-
-
carboxymethylene butenolidase
-
-
-
-
carboxymethylene butenolide hydrolase
-
-
-
-
dienelactone hydrolase
-
-
-
-
maleylacetate enol-lactonase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-carboxymethylenebut-2-en-4-olide + H2O = 4-oxohex-2-enedioate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-carboxymethylenebut-2-en-4-olide lactonohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
76689-22-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl acetate + H2O
4-nitrophenol + acetate
show the reaction diagram
-
-
-
?
4-carboxymethylenebut-2-en-4-olide + H2O
?
show the reaction diagram
4-fluoro-muconolactone + H2O
?
show the reaction diagram
-
-
-
-
?
cis-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
show the reaction diagram
p-nitrophenyl acetate + H2O
p-nitrophenol + acetate
show the reaction diagram
-
esterase activity
-
-
?
protoanemonin + H2O
cis-acetylacrylate
show the reaction diagram
-
-
-
?
trans-4-carboxymethylenebut-2-en-4-olide + H2O
4-oxohex-2-enedioate
show the reaction diagram
trans-cinnamoyl imidazole + H2O
trans-cinnamate + imidazole
show the reaction diagram
-
esterase activity
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-carboxymethylenebut-2-en-4-olide + H2O
?
show the reaction diagram
additional information
?
-
-
it seems likely, that dienelactone hydrolase has the additional function of detoxification of minor amounts of protoanemonin that may be formed during chloroaromatic degradation
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
no requirement
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dienelactam
EDTA
-
no inactivation
p-chloromercuribenzoate
protoanemonin
-
competitive inhibitor of the transformation of cis-dienelactone
additional information
-
no inactivation by iodoacetamide, iodoacetate, chloroacetamide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no requirement
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.014
4-nitrophenyl acetate
0.381 - 0.4
cis-4-carboxymethylenebut-2-en-4-olide
0.415
protoanemonin
-
-
0.015 - 9.9
trans-4-Carboxymethylenebut-2-en-4-olide
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.57 - 0.61
4-nitrophenyl acetate
30
4-carboxymethylenebut-2-en-4-olide
-
-
260
cis-4-carboxymethylenebut-2-en-4-olide
-
-
2.08
protoanemonin
-
-
2.67 - 15
trans-4-Carboxymethylenebut-2-en-4-olide
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
43 - 49
4-nitrophenyl acetate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.58
-
substrate protoanemonin
58.8
-
substrate cis-4-carboxymethylenebut-2-en-4-olide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25400 - 25800
-
predicted from DNA sequences
25490
-
calculated from nucleotide sequence of the clcD gene product
28500
-
gel filtration and nondenaturing PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
inhibitor, dienelactam, bound to DLH C123S
-
refined crystal structure at 1.8 A resolution
-
refined crystal structure of DLH at 1.8 A, C123S DLH at 2.2 A, C123A at 2.0 A resolution
-
x-ray crystallographic structure at 2.8 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Q35H/F38L/C123S/Y137C/Y145C/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/C123S/Y145C/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/C123S/Y145C/N154D/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/Q110L/C123S/Y137C/Y145C/N154D/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/Q110L/C123S/Y145C/E199G/S208G/G211D
mutations do not influence the kinetic properties
Q35H/F38L/Q110L/C123S/Y145C/N154D/E199G/S208G/G211D
mutations do not influence the kinetic properties
C123A
-
inactive
C123S
C60S
-
no reduction in activity
D171N
-
no detectable activity
E36A
-
no detectable activity
additional information
the surface mutations Q110L, Y137C and N154D do not influence the kinetic properties. Mutations Q110L and N154D have stabilizing effects, the Y137C mutation alone is destabilizing. The three mutations together increase the melting temperature by 3.4 degrees
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51.5
melting temperature, mutant Q35H/F38L/C123S/Y145C/E199G/S208G/G211D
54.9
melting temperature, mutant Q35H/F38L/Q110L/C123S/Y137C/Y145C/N154D/E199G/S208G/G211D
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 20 mM Tris-HCl, pH 7.4, 10 micromol dithiothreitol, stable for over 6 months
-
4°C, converted to microcrystals, ammonium sulfate to 30% saturation, stable for more than 1 year
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3-chlorobenzoate-grown cells
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and Pseudomonas putida
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schmidt, E.; Knackmuss, H.J.
Chemical structure and biodegradability of halogenated aromatic compounds. Conversion of chlorinated muconic acids into maleoylacetic acid
Biochem. J.
192
339-347
1980
Pseudomonas knackmussii
Manually annotated by BRENDA team
Ngai, K.L.; Schlmann, M.; Knackmuss, H.J.; Ornston, L.N.
Dienelactone hydrolase from Pseudomonas sp. strain B13
J. Bacteriol.
169
699-703
1987
Pseudomonas knackmussii
Manually annotated by BRENDA team
Ollis, D.L.; Ngai, K.L.
Crystallization and preliminary x-ray crystallographic data of dienelactone hydrolase from Pseudomonas sp. B13
J. Biol. Chem.
260
9818-9819
1985
Burkholderia cepacia, Cupriavidus necator, Pseudomonas knackmussii
Manually annotated by BRENDA team
Bruckmann, M.; Blasco, R.; Timmis, K.N.; Pieper, D.H.
Detoxification of protoanemonin by dienelactone hydrolase
J. Bacteriol.
180
400-402
1998
Burkholderia cepacia, Pseudomonas knackmussii, Pseudomonas putida
Manually annotated by BRENDA team
Pathak, D.; Ollis, D.
Refined structure of dienelactone hydrolase at 1.8 A
J. Mol. Biol.
214
497-525
1990
Pseudomonas knackmussii
Manually annotated by BRENDA team
Pathak, D.; Ashley, G.; Ollis, D.
Thiol protease-like active site found in the enzyme dienelactone hydrolase: localization using biochemical, genetic, and structural tools
Proteins Struct. Funct. Genet.
9
267-279
1991
Pseudomonas knackmussii
Manually annotated by BRENDA team
Cheah, E.; Austin, C.; Ashley, G.W.; Ollis, D.
Substrate-induced activation of dienelactone hydrolase: an enzyme with a naturally occurring Cys-His-Asp triad
Protein Eng.
6
575-583
1993
Pseudomonas knackmussii
Manually annotated by BRENDA team
Cheah, E.; Ashley, G.W.; Gary, J.; Ollis, D.
Catalysis by dienelactone hydrolase: a variation on the protease mechanism
Proteins Struct. Funct. Genet.
16
64-78
1993
Pseudomonas knackmussii
Manually annotated by BRENDA team
Beveridge, A.J.; Ollis, D.L.
A theoretical study of substrate-induced activation of dienelactone hydrolase
Protein Eng.
8
135-142
1995
Pseudomonas knackmussii
Manually annotated by BRENDA team
Schlmann, M.; Schmidt, E.; Knackmuss, H.J.
Different types of dienelactone hydrolase in 4-fluorobenzoate-utilizing bacteria
J. Bacteriol.
172
5112-5118
1990
Alcaligenes sp., Alcaligenes sp. A7, Burkholderia cepacia, Cupriavidus necator, Pseudomonas knackmussii
Manually annotated by BRENDA team
Frantz, B.; Ngai, K.L.; Chatterjee, D.K.; Ornston, L.N.; Chakrabarty, A.M.
Nucleotide sequence and expression of clcD, a plasmid-borne dienelactone hydrolase gene from Pseudomonas sp. strain B13
J. Bacteriol.
169
704-709
1987
Pseudomonas knackmussii, Pseudomonas putida
Manually annotated by BRENDA team
Pathak, D.; Ngai, K.L.; Ollis, D.
X-ray crystallographic structure of dienelactone hydrolase at 2.8 A
J. Mol. Biol.
204
435-445
1988
Pseudomonas knackmussii
Manually annotated by BRENDA team
Schlmann, M.
Evolution of chlorocatechol catabolic pathways. Conclusions to be drawn from comparisons of lactone hydrolases
Biodegradation
5
301-321
1994
Burkholderia cepacia, Cupriavidus necator, Pseudomonas knackmussii, Pseudomonas putida, Pseudomonas sp. P51, Rhodococcus opacus
Manually annotated by BRENDA team
Porter, J.L.; Collyer, C.A.; Ollis, D.L.
Compensatory stabilizing role of surface mutations during the directed evolution of dienelactone hydrolase for enhanced activity
Protein J.
34
82-89
2015
Pseudomonas knackmussii (P0A115), Pseudomonas knackmussii DSM 6978 (P0A115)
Manually annotated by BRENDA team