Information on EC 3.7.1.8 - 2,6-dioxo-6-phenylhexa-3-enoate hydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.7.1.8
-
RECOMMENDED NAME
GeneOntology No.
2,6-dioxo-6-phenylhexa-3-enoate hydrolase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2,6-dioxo-6-phenylhexa-3-enoate + H2O = benzoate + 2-oxopent-4-enoate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of C-C bonds in ketonic substances
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
2,2'-dihydroxybiphenyl degradation
-
-
2-hydroxybiphenyl degradation
-
-
biphenyl degradation
-
-
dibenzofuran degradation
-
-
Dioxin degradation
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
SYSTEMATIC NAME
IUBMB Comments
2,6-dioxo-6-phenylhexa-3-enoate benzoylhydrolase
Cleaves the products from biphenol, 3-isopropylcatechol and 3-methylcatechol produced by EC 1.13.11.39 biphenyl-2,3-diol 1,2-dioxygenase, by ring-fission at a -CO-C bond. Involved in the breakdown of biphenyl-related compounds by Pseudomonas sp.
CAS REGISTRY NUMBER
COMMENTARY hide
102925-38-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain JF8
-
-
Manually annotated by BRENDA team
strain JF8
-
-
Manually annotated by BRENDA team
strain LB400
-
-
Manually annotated by BRENDA team
strain LB400
-
-
Manually annotated by BRENDA team
strain B-356
Uniprot
Manually annotated by BRENDA team
gene bphD
UniProt
Manually annotated by BRENDA team
gene bphD
UniProt
Manually annotated by BRENDA team
S93 B1
-
-
Manually annotated by BRENDA team
strain DJ-12
-
-
Manually annotated by BRENDA team
LD2
-
-
Manually annotated by BRENDA team
P20
-
-
Manually annotated by BRENDA team
strain P6
-
-
Manually annotated by BRENDA team
strain P6
-
-
Manually annotated by BRENDA team
strain RW1, 2 isofunctional hydrolases H1 and H2
-
-
Manually annotated by BRENDA team
strain RW1, 2 isofunctional hydrolases H1 and H2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
-
rapid acylation of the H265Q variant during C-C bond cleavage suggests that the serinate forms via a substrate-assisted mechanism in the reaction
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid + H2O
4-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
2-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
(2E,4E)-6-(3,4-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3,4-dichlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3,5-dichlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid + H2O
3-chlorobenzoate + (2E)-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-2,4-dihydroxypenta-2,4-dienoic acid
show the reaction diagram
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E)-4-chloro-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2E,4Z)-5-chloro-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + (2Z)-3-chloro-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
2,6-dihydroxy-6-phenylhexa-2,4-dienoate
benzaldehyde + (2E)-2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxy-6-oxo-6-(2,3-dihydroxyphenyl)-hexa-2,4-dienoate + H2O
2,3-dihydroxybenzoate + 2-oxopent-4-enoate + H+
show the reaction diagram
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid + H2O
2-aminobenzoic acid + 2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate + H+
show the reaction diagram
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate
show the reaction diagram
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
benzoate + 2-hydroxypenta-2,4-dienoate
show the reaction diagram
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H2O
benzoate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
show the reaction diagram
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
?
show the reaction diagram
-
i.e. HOPDA
-
-
?
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
benzoate + 2-hydroxypenta-2,4-dienoic acid
show the reaction diagram
-
-
-
-
?
3-isopropylcatechol + H2O
?
show the reaction diagram
3-methylcatechol + H2O
?
show the reaction diagram
4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid + H2O
3-[(7aR)-7a-hydroxy-1,5-dioxooctahydro-1H-inden-4-yl]propanoic acid + (2Z,4Z)-5-hydroxyhexa-2,4-dienoic acid
show the reaction diagram
4-nitrophenyl benzoate + H2O
4-nitrophenol + benzoate
show the reaction diagram
-
the serine nucleophile is activated by the His-Asp dyad
-
-
?
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
show the reaction diagram
biphenyl-2,3-diol + H2O
?
show the reaction diagram
catechol + H2O
?
show the reaction diagram
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate + H2O
benzoate + ethyl 2-(acetyloxy)penta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate + H2O
benzoate + ethyl-2-(acetyloxy)penta-2,4-dienoate
show the reaction diagram
-
-
-
-
?
meta-ring fission intermediate + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,6-dioxo-6-phenylhexa-3-enoate + H2O
benzoate + 2-oxopent-4-enoate
show the reaction diagram
2-hydroxy-6-oxo-6-(2-hydroxyphenyl)-hexa-2,4-dienoate + H2O
2-oxopent-4-enoate + salicylate + H+
show the reaction diagram
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid + H2O
2-hydroxypenta-2,4-dienoic acid + benzoate
show the reaction diagram
P47229
i.e. HOPDA
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
no cofactor requirement
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
competitively inhibits
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
PMSF
inhibition of semipurified enzyme
additional information
-
no effects by n-propanol and 2-propanol
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00013 - 0.00065
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid
0.00019 - 0.00047
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.00033 - 0.0129
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
0.00075
(2E,4E)-6-(3,4-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.00104
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
0.00043 - 0.00046
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
0.00095 - 0.0044
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.0036 - 0.004
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.0049 - 0.018
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.00054 - 0.0069
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.00028 - 0.0051
2,6-dioxo-6-phenylhexa-3-enoate
0.0046
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid
-
at 25C
0.00071 - 0.00085
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
0.0002 - 0.008
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.31
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
pH 7.5, 25C
0.0017 - 0.0373
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
0.002 - 0.077
meta-ring fission intermediate
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.13 - 33.7
(2E,4E)-2-hydroxy-6-(4-chlorophenyl)-6-oxohexa-2,4-dienoic acid
4.18 - 7.6
(2E,4E)-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
1.74 - 2.1
(2E,4E)-6-(2-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
29
(2E,4E)-6-(3,4-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
Rhodococcus globerulus
-
-
11.2
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
Rhodococcus globerulus
-
-
3.9 - 15.3
(2E,4E)-6-(3-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
0.0055
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
Burkholderia cepacia
-
-
0.00059
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
Burkholderia cepacia
-
-
1.03 - 1.53
(2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.0089 - 0.0172
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
0.13 - 9.9
2,6-dioxo-6-phenylhexa-3-enoate
1300
2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid
Pseudomonas sp.
-
-
1.11
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
Bacillus sp.
-
at 60C
0.066 - 26
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
6.3
4-nitrophenyl benzoate
Paraburkholderia xenovorans
-
pH 7.5, 25C
0.33
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
Mycobacterium tuberculosis
P9WNH5
pH 7.5, 25C
0.0009 - 6.5
ethyl-2-acetoxy-6-keto-6-phenylhexa-2,4-dienoate
0.009 - 12
meta-ring fission intermediate
-
additional information
additional information
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
440 - 16100
2,6-dioxo-6-phenylhexa-3-enoate
95692
9 - 32
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
3589
1.1
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
Mycobacterium tuberculosis
P9WNH5
pH 7.5, 25C
15228
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00095
(2E,4Z)-2,4-dihydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.0036
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
0.00057
(2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.34
-
at 60C
6.4
-
purified enzyme
13.2
-
purified enzyme
2600
-
in 0.05 mM 2-hydroxy-6-oxo-6-(2-aminophenyl)hexa-2,4-dienoic acid, 50 mM Tris, pH 7.5 at 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.7
-
pH 6.5: about 65% of maximal activity, pH 8.7: about 25% of maximal activity
6.5 - 10.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 25
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 85
-
-
PDB
SCOP
CATH
ORGANISM
UNIPROT
Janthinobacterium sp. (strain J3)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Paraburkholderia xenovorans (strain LB400)
Rhodococcus jostii (strain RHA1)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
Sphingomonas wittichii (strain RW1 / DSM 6014 / JCM 10273)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
1 * 31000, isoenzyme H1, SDS-PAGE
32000
x * 32000, recombinant His-tagged enzyme, SDS-PAGE
32231
-
2 * 32231, native enzyme, predicted from peptide sequence
32580
-
by HPLC-ESMS analysis
33000
-
x * 33000, SDS-PAGE
37000 - 40000
-
isoenzyme H1, gel filtration, non-denaturing PAGE
41000 - 48000
-
isoenzyme H2, gel filtration, non-denaturing PAGE
55000
-
gel filtration
160000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
octamer
crystal structure
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
H263 mutant by hanging drop vapor diffusion, to 2 A resolution
-
mutant S114A in complex with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, 8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid, or 4,5-9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oic acid, sitting drop vapor diffusion, 0.001 ml of 8 mg/ml protein solution is mixed with 0.001 ml of precipitant solution containing 200 mM KSCN, 24% PEG 3350, and 100 mM bis-tris propane, pH 7.0, soaking of S114A crystals in 0.01 ml of precipitant solution supplemented with 15 mM of each ligand for 30-60 min, X-ray diffractin structure determination and analysis at 1.8-2.1 A resolution, molecular replacement
BphD H265Q and S112A/H265Q mutants in complex with substrate 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid, sitting drop vapour diffusion method, 0.001 ml of protein solution containing 4 mg/ml protein in 20 mM HEPES, pH 7.5, 20C, 9 days, is mixed with 0.001 ml of reservoir solution containing 2.4 M malonate at pH 6.0-7.0, X-ray diffraction structure determination and analysis at 1.3 A and 1.9 A resolutions, respectively
enzyme structure determination and analysis, PDB IDs 2OG1, 2PU5, 2RI6, 2PU7, 2PUH and 2PUJ
S112A and H265Q mutants crystal structure analysis, PDB IDs 2PUH and 3V1N, modeling
-
wild-type, the S112C variant and S112C incubated with 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid by hanging drop vapor diffusion method at 20C, to 1.6 A resolution, interaction between conserved active side residues and dienoate moiety of the substrate, the residue His265 is hydrogen-bonded to the 2-hydroxy/oxo substituent of the substrate, consistent with a role in catalyzing ketonization
-
at 2.4 A resolution, active-site residues are Ser110, Asp235 and His263, situated inside the cavity between the core and the lid domains, this substrate binding pocket has a hydrophobic and hydrophilic region
enzyme structure determination and analysis, PDB ID 1C4X
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 11
-
25C, 6 h, stable
247041
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20
-
1 h, stable
60
-
pH 7.4, 5 min, 75% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C or -70C, buffer containing 30% glycerol, stable for 1 week
-
-80C, 12 months
-
4C, 48 h, 10% loss of isoenzyme H1 activity, 20% loss of isoenzyme H2 activity
-
4C, pH 7.4, 10% loss of activity after 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 isofunctional hydrolases H1 and H2
-
BphD mutants purified by affinity chromatography to more than 95% homogeneity
-
by metal affinity chromatography
-
by metal affinity chromatography, to more than 90% homogeneity
-
gel filtration, to homogeneity
-
MhpC mutants purified by anion exchange chromatography to more than 95% homogeneity
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
standard method
to apparent homogeneity
-
to more than 90% homogeneitiy
-
to more than 99% homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
BphD mutants expressed in a pET-14b vector as an N-terminal His6 fusion protein
-
expression from pBUPH2 in Escherichia coli MV1184
-
expression in Escherichia coli
expression in Escherichia coli HB101
-
gene bphD, DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
gene bphD, expression of wild-type and mutant BphDs
into the pET-14b vector, overexpression in Escherichia coli BL21(DE3) cells
-
overexpression in Escherichia coli
-
overexpression in Escherichia coli BL21(DE3)(pLysS1)/pAIA51
-
overexpression in Pseudomonas putida KT2442 containing vector pSS316
-
overexpression of wild-type and mutant BphDs in Escherichia coli strain Rosetta(DE3)pLysS
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S112A
inactive enzyme
M148A
site-directed mutagenesis of the non-active-site residue
M148C
site-directed mutagenesis of the non-active-site residue
M148D
site-directed mutagenesis of the non-active-site residue
M148E
site-directed mutagenesis of the non-active-site residue
M148F
site-directed mutagenesis of the non-active-site residue
M148G
site-directed mutagenesis of the non-active-site residue
M148H
site-directed mutagenesis of the non-active-site residue
M148I
site-directed mutagenesis of the non-active-site residue
M148K
site-directed mutagenesis of the non-active-site residue
M148L
site-directed mutagenesis of the non-active-site residue
M148N
site-directed mutagenesis of the non-active-site residue
M148P
site-directed mutagenesis of the non-active-site residue
M148Q
site-directed mutagenesis of the non-active-site residue
M148R
site-directed mutagenesis of the non-active-site residue
M148S
site-directed mutagenesis of the non-active-site residue
M148T
site-directed mutagenesis of the non-active-site residue
M148V
site-directed mutagenesis of the non-active-site residue
M148W
site-directed mutagenesis of the non-active-site residue
M148Y
site-directed mutagenesis of the non-active-site residue
M148A
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site-directed mutagenesis of the non-active-site residue
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M148D
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site-directed mutagenesis of the non-active-site residue
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M148L
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site-directed mutagenesis of the non-active-site residue
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M148P
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site-directed mutagenesis of the non-active-site residue
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M148W
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site-directed mutagenesis of the non-active-site residue
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C261A
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2fold decreased turnover rate, Cys-261 seems to be not involved in catalysis
F173D
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1.5fold increased Km value, 100fold decreased turnover rate
F173G
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8fold increased Km value, 3.5fold decreased turnover rate
H114A
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reduced activity, is able to accept the 6-phenyl-containing substrate, on a shorter time scale
H263A
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overal structure similar, but asymmetry of the enzyme dimer more pronounced than for the native enzyme
N109A
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similar Km value as wild-type, 200fold decreased turnover rate
N109H
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similar Km value as wild-type, 350fold decreased turnover rate
R188K
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5fold increased Km value,35fold decreased turnover rate
R188Q
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first step of enzyme reaction, keto-enol tautomerization, becomes rate-limiting, 11fold increased Km value, 300fold decreased turnover rate
W264G
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16fold increased Km value, 10fold decreased turnover rate
D237N
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reduced activity
R190K
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similar Km value as wild-type, 700fold decreased turnover rate
R190Q
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14fold increased Km value, 400fold decreased turnover rate
S112A/H265Q
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
S112C
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lower enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
molecular biology
Show AA Sequence (312 entries)
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