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0.344 - 6.517
maleylpyruvate
0.344
maleylpyruvate
-
mutant enzyme R109A, in 50 mM phosphate buffer, pH 8.0, at 22°C
0.346
maleylpyruvate
-
mutant enzyme N108A, in 50 mM phosphate buffer, pH 8.0, at 22°C
0.407
maleylpyruvate
-
mutant enzyme H104A, in 50 mM phosphate buffer, pH 8.0, at 22°C
0.566
maleylpyruvate
-
wild type enzyme, in 50 mM phosphate buffer, pH 8.0, at 22°C
0.69
maleylpyruvate
-
mutant enzyme T11A, in 50 mM phosphate buffer, pH 8.0, at 22°C
1.029
maleylpyruvate
-
mutant enzyme R8A, in 50 mM phosphate buffer, pH 8.0, at 22°C
2.355
maleylpyruvate
-
mutant enzyme R176A, in 50 mM phosphate buffer, pH 8.0, at 22°C
3.339
maleylpyruvate
-
mutant enzyme R8A/R176A, in 50 mM phosphate buffer, pH 8.0, at 22°C
6.517
maleylpyruvate
-
mutant enzyme Q49A, in 50 mM phosphate buffer, pH 8.0, at 22°C
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0.54 - 120.9
maleylpyruvate
0.54
maleylpyruvate
-
mutant enzyme R109A, in 50 mM phosphate buffer, pH 8.0, at 22°C
1.06
maleylpyruvate
-
mutant enzyme R8A/R176A, in 50 mM phosphate buffer, pH 8.0, at 22°C
11.11
maleylpyruvate
-
mutant enzyme H104A, in 50 mM phosphate buffer, pH 8.0, at 22°C
13.45
maleylpyruvate
-
mutant enzyme Q49A, in 50 mM phosphate buffer, pH 8.0, at 22°C
22.59
maleylpyruvate
-
mutant enzyme R8A, in 50 mM phosphate buffer, pH 8.0, at 22°C
31.47
maleylpyruvate
-
mutant enzyme N108A, in 50 mM phosphate buffer, pH 8.0, at 22°C
51.45
maleylpyruvate
-
mutant enzyme R176A, in 50 mM phosphate buffer, pH 8.0, at 22°C
101.3
maleylpyruvate
-
wild type enzyme, in 50 mM phosphate buffer, pH 8.0, at 22°C
120.9
maleylpyruvate
-
mutant enzyme T11A, in 50 mM phosphate buffer, pH 8.0, at 22°C
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0.316 - 179.1
maleylpyruvate
0.316
maleylpyruvate
-
mutant enzyme R8A/R176A, in 50 mM phosphate buffer, pH 8.0, at 22°C
1.579
maleylpyruvate
-
mutant enzyme R109A, in 50 mM phosphate buffer, pH 8.0, at 22°C
2.063
maleylpyruvate
-
mutant enzyme Q49A, in 50 mM phosphate buffer, pH 8.0, at 22°C
21.84
maleylpyruvate
-
mutant enzyme R176A, in 50 mM phosphate buffer, pH 8.0, at 22°C
21.96
maleylpyruvate
-
mutant enzyme R8A, in 50 mM phosphate buffer, pH 8.0, at 22°C
27.31
maleylpyruvate
-
mutant enzyme H104A, in 50 mM phosphate buffer, pH 8.0, at 22°C
91.31
maleylpyruvate
-
mutant enzyme N108A, in 50 mM phosphate buffer, pH 8.0, at 22°C
175.1
maleylpyruvate
-
mutant enzyme T11A, in 50 mM phosphate buffer, pH 8.0, at 22°C
179.1
maleylpyruvate
-
wild type enzyme, in 50 mM phosphate buffer, pH 8.0, at 22°C
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C61A
site directed mutagenesis
D151A
site directed mutagenesis, completely inactive
E144A
site directed mutagenesis, completely inactive
E85A
site directed mutagenesis
H148A
site directed mutagenesis, completely inactive
H48A
site directed mutagenesis
H52A
site directed mutagenesis, completely inactive
N56A
site directed mutagenesis, completely inactive
R141A
site directed mutagenesis, completely inactive
R222A
site directed mutagenesis, completely inactive
R82A
site directed mutagenesis, partially inactive
S78A
site directed mutagenesis, almost completely inactive
W44A
site directed mutagenesis, completely inactive
Y76A
site directed mutagenesis, completely inactive
D102A
-
completely inactive
H104A
-
the mutant shows 15.25% catalytic efficiency compared to the wild type enzyme
H38A
-
completely inactive
N108A
-
the mutant shows 50.83% catalytic efficiency compared to the wild type enzyme
P53A
-
completely inactive
Q49A
-
the mutant shows 1.15% catalytic efficiency compared to the wild type enzyme
Q64A
-
completely inactive
R109A
-
the mutant shows 0.88% catalytic efficiency compared to the wild type enzyme
R110A
-
completely inactive
R176A
-
the mutant shows 12.2% catalytic efficiency compared to the wild type enzyme
R8A
-
the mutant shows 12.26% catalytic efficiency compared to the wild type enzyme
R8A/R176A
-
the mutant shows 0.18% catalytic efficiency compared to the wild type enzyme
S9A
-
completely inactive
T11A
-
the mutant shows 97.81% catalytic efficiency compared to the wild type enzyme
D102A
-
completely inactive
-
H104A
-
the mutant shows 15.25% catalytic efficiency compared to the wild type enzyme
-
Q64A
-
completely inactive
-
R176A
-
the mutant shows 12.2% catalytic efficiency compared to the wild type enzyme
-
S9A
-
completely inactive
-
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Lack, L.
Enzymic cis-trans isomerization of maleylpyruvic acid
J. Biol. Chem.
236
2835-2840
1961
Pseudomonas sp.
brenda
Tomasek, P.H.; Crawford, R.L.
Initial reactions of xanthone biodegradation by an Arthrobacter sp.
J. Bacteriol.
167
818-827
1986
Arthrobacter sp.
brenda
Hagedorn, S.R.; Bradley, G.; Chapman, P.J.
Glutathione-independent isomerization of maleylpyruvate by Bacillus megaterium and other gram-positive bacteria
J. Bacteriol.
163
640-647
1985
Acinetobacter sp., Cupriavidus necator, Arthrobacter sp., Geobacillus stearothermophilus, Priestia megaterium, Bacillus sp. (in: Bacteria), Delftia acidovorans, Corynebacterium sp., Moraxella sp., Nocardia globerula, Rhodococcus rhodnii, Nocardia sp., Rhodococcus sp., Bacillus sp. (in: Bacteria) B4, Priestia megaterium 410, Moraxella sp. OA3, Geobacillus stearothermophilus 6T-5, Rhodococcus sp. A81, Nocardia sp. 3CS, Arthrobacter sp. 4CB/2-1, Acinetobacter sp. CHC, Delftia acidovorans 16
brenda
Clark, J.S.; Buswell, J.A.
Catabolism of gentisic acid by two strains of Bacillus stearothermophilus
J. Gen. Microbiol.
112
191-195
1979
Geobacillus stearothermophilus
-
brenda
Crawford, R.L.; Olson, P.E.
Catabolism of 2-hydroxybenzoate by Bacillus species
FEMS Microbiol. Lett.
5
193-195
1979
Bacillus sp. (in: Bacteria)
-
brenda
Robson, N.D.; Parrott, S.; Cooper, R.A.
In vitro formation of a catabolic plasmid carrying Klebsiella pneumoniae DNA that allows growth of Escherichia coli K-12 on 3-hydroxybenzoate
Microbiology
142
2115-2120
1996
Klebsiella pneumoniae
brenda
Jones, D.C.N.; Cooper, R.A.
Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1
Arch. Microbiol.
154
489-495
1990
Klebsiella pneumoniae, Klebsiella pneumoniae M5a1
brenda
Goetz, F.E.; Harmuth, L.J.
Gentisatwe pathway in Salmonella typhimurium: metabolism of m-hydroxybenzoate and gentisate
FEMS Microbiol. Lett.
97
45-50
1992
Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Suemori, A.; Nakajima, K.; Kurane, R.; Nakamura, Y.
o-, m- and p-Hydroxybenzoate degradative pathways in Rhodococcus erythropolis
FEMS Microbiol. Lett.
125
31-36
1995
Rhodococcus erythropolis, Rhodococcus erythropolis S1
brenda
Jain, R.K.
The molecular cloning of genes specifying some enzymes of the 3,5-xylenol degradative pathway
Appl. Microbiol. Biotechnol.
45
502-508
1996
Pseudomonas putida
-
brenda
Shen, X.H.; Jiang, C.Y.; Huang, Y.; Liu, Z.P.; Liu, S.J.
Functional identification of novel genes involved in the glutathione-independent gentisate pathway in Corynebacterium glutamicum
Appl. Environ. Microbiol.
71
3442-3452
2005
Corynebacterium glutamicum
brenda
Feng, J.; Che, Y.; Milse, J.; Yin, Y.J.; Liu, L.; Rueckert, C.; Shen, X.H.; Qi, S.W.; Kalinowski, J.; Liu, S.J.
The gene ncgl2918 encodes a novel maleylpyruvate isomerase that needs mycothiol as cofactor and links mycothiol biosynthesis and gentisate assimilation in Corynebacterium glutamicum
J. Biol. Chem.
281
10778-10785
2006
Corynebacterium glutamicum (Q8NLC1), Corynebacterium glutamicum
brenda
Wang, R.; Yin, Y.J.; Wang, F.; Li, M.; Feng, J.; Zhang, H.M.; Zhang, J.P.; Liu, S.J.; Chang, W.R.
Crystal structures and site-directed mutagenesis of a mycothiol-dependent enzyme reveal a novel folding and molecular basis for mycothiol-mediated maleylpyruvate isomerization
J. Biol. Chem.
282
16288-16294
2007
Corynebacterium glutamicum (Q8NLC1), Corynebacterium glutamicum
brenda
Rong, L.; Guo, X.; Chen, K.; Zhu, J.; Li, S.; Jiang, J.
Isolation of an isocarbophos-degrading strain of Arthrobacter sp. scl-2 and identification of the degradation pathway
J. Microbiol. Biotechnol.
19
1439-1446
2009
Arthrobacter sp., Arthrobacter sp. scl-2
brenda
Liu, T.T.; Xu, Y.; Liu, H.; Luo, S.; Yin, Y.J.; Liu, S.J.; Zhou, N.Y.
Functional characterization of a gene cluster involved in gentisate catabolism in Rhodococcus sp. strain NCIMB 12038
Appl. Microbiol. Biotechnol.
90
671-678
2010
Rhodococcus sp., Rhodococcus sp. NCIMB 12038
brenda
Fang, T.; Li, D.F.; Zhou, N.Y.
Identification and clarification of the role of key active site residues in bacterial glutathione S-transferase zeta/maleylpyruvate isomerase
Biochem. Biophys. Res. Commun.
410
452-456
2011
Ralstonia sp., Ralstonia sp. U2
brenda
Liu, T.T.; Zhou, N.Y.
Novel L-cysteine-dependent maleylpyruvate isomerase in the gentisate pathway of Paenibacillus sp. strain NyZ101
J. Bacteriol.
194
3987-3994
2012
Paenibacillus sp. (H6TG59), Paenibacillus sp., Paenibacillus sp. NyZ101 (H6TG59)
brenda
Liu, K.; Xu, Y.; Zhou, N.Y.
Identification of a specific maleate hydratase in the direct hydrolysis route of the gentisate pathway
Appl. Environ. Microbiol.
81
5753-5760
2015
Pseudomonas alcaligenes, Pseudomonas alcaligenes NCIMB 9867
brenda