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
gene bphD
UniProt
Manually annotated by BRENDA team
gene bphD
UniProt
Manually annotated by BRENDA team
S93 B1
-
-
Manually annotated by BRENDA team
LD2
-
-
Manually annotated by BRENDA team
P20
-
-
Manually annotated by BRENDA team
2 isofunctional hydrolases H1 and H2
-
-
Manually annotated by BRENDA team
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 25°C
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, 25°C
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
-
-
11.2
(2E,4E)-6-(3,5-chlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid
-
-
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
-
-
0.00059
(2E,4Z)-4-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
-
-
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
-
-
1.11
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate
-
at 60°C
0.066 - 26
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
6.3
4-nitrophenyl benzoate
-
pH 7.5, 25°C
0.33
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
pH 7.5, 25°C
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
9 - 32
2-Hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid
1.1
8-(2-chlorophenyl)-2-hydroxy-5-methyl-6-oxoocta-2,4-dienoic acid
pH 7.5, 25°C
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
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 25°C
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
Q84II3
Janthinobacterium sp. (strain J3);
Paraburkholderia xenovorans (strain LB400);
Q75WN8
Rhodococcus jostii (strain RHA1);
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, 20°C, 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 20°C, 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
-
25°C, 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
-20°C or -70°C, buffer containing 30% glycerol, stable for 1 week
-
-80°C, 12 months
-
4°C, 48 h, 10% loss of isoenzyme H1 activity, 20% loss of isoenzyme H2 activity
-
4°C, 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
-
site-directed mutagenesis of the non-active-site residue
-
M148D
-
site-directed mutagenesis of the non-active-site residue
-
M148L
-
site-directed mutagenesis of the non-active-site residue
-
M148P
-
site-directed mutagenesis of the non-active-site residue
-
M148W
-
site-directed mutagenesis of the non-active-site residue
-
C261A
-
2fold decreased turnover rate, Cys-261 seems to be not involved in catalysis
F173D
-
1.5fold increased Km value, 100fold decreased turnover rate
F173G
-
8fold increased Km value, 3.5fold decreased turnover rate
H114A
-
reduced activity, is able to accept the 6-phenyl-containing substrate, on a shorter time scale
H263A
-
overal structure similar, but asymmetry of the enzyme dimer more pronounced than for the native enzyme
N109A
-
similar Km value as wild-type, 200fold decreased turnover rate
N109H
-
similar Km value as wild-type, 350fold decreased turnover rate
R188K
-
5fold increased Km value,35fold decreased turnover rate
R188Q
-
first step of enzyme reaction, keto-enol tautomerization, becomes rate-limiting, 11fold increased Km value, 300fold decreased turnover rate
W264G
-
16fold increased Km value, 10fold decreased turnover rate
D237N
-
reduced activity
R190K
-
similar Km value as wild-type, 700fold decreased turnover rate
R190Q
-
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
-
lower enzyme activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
molecular biology
Show AA Sequence (414 entries)
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