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show all sequences of 1.1.1.154

Novel insights into E. colis hexuronate metabolism: KduI facilitates the conversion of galacturonate and glucuronate under osmotic stress conditions

Rothe, M.; Alpert, C.; Loh, G.; Blaut, M.; PLoS ONE 8, e56906 (2013)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expresed as a His-tagged fusion protein in Escherichia coli
Escherichia coli
Crystallization (Commentary)
Crystallization
Organism
crystal structure of AllD in its apo form is determined at 2.13 A resolution, as well as a binary complex at 1.64 A resolution with the NADH cofactor, and a ternary complex at 1.77 A resolution with NADH and glyoxylate, a product yielded from the spontaneous degradation of oxalurate
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
D141A
Km ((S)-ureidoglycolate) increased, kcat (S-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) similar to wo wild-type
Escherichia coli
D141E
Km ((S)-ureidoglycolate) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) decreased compared to wild-type
Escherichia coli
D141N
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
H116A
mutant(S)-ureidoglycolate shows no activity
Escherichia coli
H44A
Km ((S)-ureidoglycolate) increased, kcat (S-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) equal to wild-type
Escherichia coli
M251A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
R259A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
R48A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
S140A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
S43A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
Y52F
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.37
-
NAD+
mutant D141E, pH 8.1, 30C
Escherichia coli
0.52
-
NAD+
mutant D141A, pH 8.1, 30C
Escherichia coli
0.56
-
NAD+
wild-type, pH 8.1, 30C
Escherichia coli
0.65
-
NAD+
mutant H44A, pH 8.1, 30C
Escherichia coli
0.81
-
NAD+
mutant D141N, pH 8.1, 30C
Escherichia coli
0.93
-
NAD+
mutant M251A, pH 8.1, 30C
Escherichia coli
1.06
-
(S)-ureidoglycolate
wild-type, pH 8.1, 30C
Escherichia coli
1.26
-
NAD+
mutant Y52F, pH 8.1, 30C
Escherichia coli
1.39
-
NAD+
mutant S140A, pH 8.1, 30C
Escherichia coli
1.49
-
NAD+
mutant R259A, pH 8.1, 30C
Escherichia coli
2.28
-
NAD+
mutant S43A, pH 8.1, 30C
Escherichia coli
5.27
-
(S)-ureidoglycolate
mutant D141A, pH 8.1, 30C
Escherichia coli
5.87
-
(S)-ureidoglycolate
mutant D141N, pH 8.1, 30C
Escherichia coli
10.75
-
(S)-ureidoglycolate
mutant S43A, pH 8.1, 30C
Escherichia coli
11.47
-
(S)-ureidoglycolate
mutant R259A, pH 8.1, 30C
Escherichia coli
12.38
-
(S)-ureidoglycolate
mutant S140A, pH 8.1, 30C
Escherichia coli
13.15
-
(S)-ureidoglycolate
mutant M251A, pH 8.1, 30C
Escherichia coli
14.13
-
(S)-ureidoglycolate
mutant D141E, pH 8.1, 30C
Escherichia coli
16.82
-
(S)-ureidoglycolate
mutant Y52F, pH 8.1, 30C
Escherichia coli
16.94
-
(S)-ureidoglycolate
mutant H44A, pH 8.1, 30C
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
-
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-ureidoglycolate + NAD+
-
726324
Escherichia coli
oxalureate + NADH
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
gel filtration
Escherichia coli
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.02
-
NAD+
mutant S140A, pH 8.1, 30C
Escherichia coli
0.87
-
NAD+
mutant D141E, pH 8.1, 30C
Escherichia coli
1.03
-
NAD+
mutant H44A, pH 8.1, 30C
Escherichia coli
1.06
-
NAD+
mutant D141A, pH 8.1, 30C
Escherichia coli
1.29
-
(S)-ureidoglycolate
mutant S140A, pH 8.1, 30C
Escherichia coli
1.37
-
(S)-ureidoglycolate
mutant S43A, pH 8.1, 30C
Escherichia coli
1.47
-
NAD+
mutant D141N, pH 8.1, 30C
Escherichia coli
1.62
-
(S)-ureidoglycolate
mutant D141A, pH 8.1, 30C
Escherichia coli
1.67
-
(S)-ureidoglycolate
mutant D141E, pH 8.1, 30C
Escherichia coli
1.76
-
(S)-ureidoglycolate
mutant H44A, pH 8.1, 30C
Escherichia coli
1.9
-
NAD+
mutant Y52F, pH 8.1, 30C
Escherichia coli
1.92
-
(S)-ureidoglycolate
mutant Y52F, pH 8.1, 30C
Escherichia coli
1.97
-
(S)-ureidoglycolate
mutant D141N, pH 8.1, 30C
Escherichia coli
2.51
-
NAD+
mutant S43A, pH 8.1, 30C
Escherichia coli
9.29
-
NAD+
mutant R259A, pH 8.1, 30C
Escherichia coli
11.98
-
(S)-ureidoglycolate
mutant R259A, pH 8.1, 30C
Escherichia coli
30.65
-
NAD+
mutant M251A, pH 8.1, 30C
Escherichia coli
45.98
-
(S)-ureidoglycolate
mutant M251A, pH 8.1, 30C
Escherichia coli
57
-
(S)-ureidoglycolate
wild-type, pH 8.1, 30C
Escherichia coli
62
-
NAD+
wild-type, pH 8.1, 30C
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
assay at
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expresed as a His-tagged fusion protein in Escherichia coli
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Escherichia coli
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure of AllD in its apo form is determined at 2.13 A resolution, as well as a binary complex at 1.64 A resolution with the NADH cofactor, and a ternary complex at 1.77 A resolution with NADH and glyoxylate, a product yielded from the spontaneous degradation of oxalurate
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
D141A
Km ((S)-ureidoglycolate) increased, kcat (S-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) similar to wo wild-type
Escherichia coli
D141E
Km ((S)-ureidoglycolate) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) decreased compared to wild-type
Escherichia coli
D141N
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
H116A
mutant(S)-ureidoglycolate shows no activity
Escherichia coli
H44A
Km ((S)-ureidoglycolate) increased, kcat (S-ureidoglycolate) or (NAD+) decreased compared to wild-type, Km (NAD+) equal to wild-type
Escherichia coli
M251A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
R259A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
R48A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
S140A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
S43A
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
Y52F
Km ((S)-ureidoglycolate) or (NAD+) increased, kcat ((S)-ureidoglycolate) or (NAD+) decreased compared to wild-type
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.37
-
NAD+
mutant D141E, pH 8.1, 30C
Escherichia coli
0.52
-
NAD+
mutant D141A, pH 8.1, 30C
Escherichia coli
0.56
-
NAD+
wild-type, pH 8.1, 30C
Escherichia coli
0.65
-
NAD+
mutant H44A, pH 8.1, 30C
Escherichia coli
0.81
-
NAD+
mutant D141N, pH 8.1, 30C
Escherichia coli
0.93
-
NAD+
mutant M251A, pH 8.1, 30C
Escherichia coli
1.06
-
(S)-ureidoglycolate
wild-type, pH 8.1, 30C
Escherichia coli
1.26
-
NAD+
mutant Y52F, pH 8.1, 30C
Escherichia coli
1.39
-
NAD+
mutant S140A, pH 8.1, 30C
Escherichia coli
1.49
-
NAD+
mutant R259A, pH 8.1, 30C
Escherichia coli
2.28
-
NAD+
mutant S43A, pH 8.1, 30C
Escherichia coli
5.27
-
(S)-ureidoglycolate
mutant D141A, pH 8.1, 30C
Escherichia coli
5.87
-
(S)-ureidoglycolate
mutant D141N, pH 8.1, 30C
Escherichia coli
10.75
-
(S)-ureidoglycolate
mutant S43A, pH 8.1, 30C
Escherichia coli
11.47
-
(S)-ureidoglycolate
mutant R259A, pH 8.1, 30C
Escherichia coli
12.38
-
(S)-ureidoglycolate
mutant S140A, pH 8.1, 30C
Escherichia coli
13.15
-
(S)-ureidoglycolate
mutant M251A, pH 8.1, 30C
Escherichia coli
14.13
-
(S)-ureidoglycolate
mutant D141E, pH 8.1, 30C
Escherichia coli
16.82
-
(S)-ureidoglycolate
mutant Y52F, pH 8.1, 30C
Escherichia coli
16.94
-
(S)-ureidoglycolate
mutant H44A, pH 8.1, 30C
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-ureidoglycolate + NAD+
-
726324
Escherichia coli
oxalureate + NADH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
gel filtration
Escherichia coli
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Escherichia coli
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.02
-
NAD+
mutant S140A, pH 8.1, 30C
Escherichia coli
0.87
-
NAD+
mutant D141E, pH 8.1, 30C
Escherichia coli
1.03
-
NAD+
mutant H44A, pH 8.1, 30C
Escherichia coli
1.06
-
NAD+
mutant D141A, pH 8.1, 30C
Escherichia coli
1.29
-
(S)-ureidoglycolate
mutant S140A, pH 8.1, 30C
Escherichia coli
1.37
-
(S)-ureidoglycolate
mutant S43A, pH 8.1, 30C
Escherichia coli
1.47
-
NAD+
mutant D141N, pH 8.1, 30C
Escherichia coli
1.62
-
(S)-ureidoglycolate
mutant D141A, pH 8.1, 30C
Escherichia coli
1.67
-
(S)-ureidoglycolate
mutant D141E, pH 8.1, 30C
Escherichia coli
1.76
-
(S)-ureidoglycolate
mutant H44A, pH 8.1, 30C
Escherichia coli
1.9
-
NAD+
mutant Y52F, pH 8.1, 30C
Escherichia coli
1.92
-
(S)-ureidoglycolate
mutant Y52F, pH 8.1, 30C
Escherichia coli
1.97
-
(S)-ureidoglycolate
mutant D141N, pH 8.1, 30C
Escherichia coli
2.51
-
NAD+
mutant S43A, pH 8.1, 30C
Escherichia coli
9.29
-
NAD+
mutant R259A, pH 8.1, 30C
Escherichia coli
11.98
-
(S)-ureidoglycolate
mutant R259A, pH 8.1, 30C
Escherichia coli
30.65
-
NAD+
mutant M251A, pH 8.1, 30C
Escherichia coli
45.98
-
(S)-ureidoglycolate
mutant M251A, pH 8.1, 30C
Escherichia coli
57
-
(S)-ureidoglycolate
wild-type, pH 8.1, 30C
Escherichia coli
62
-
NAD+
wild-type, pH 8.1, 30C
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
assay at
Escherichia coli
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.01
-
NAD+
mutant S140A, pH 8.1, 30C
Escherichia coli
0.1
-
(S)-ureidoglycolate
mutant H44A, pH 8.1, 30C; mutant S140A, pH 8.1, 30C
Escherichia coli
0.11
-
(S)-ureidoglycolate
mutant Y52F, pH 8.1, 30C
Escherichia coli
0.12
-
(S)-ureidoglycolate
mutant D141E, pH 8.1, 30C
Escherichia coli
0.13
-
(S)-ureidoglycolate
mutant S43A, pH 8.1, 30C
Escherichia coli
0.31
-
(S)-ureidoglycolate
mutant D141A, pH 8.1, 30C
Escherichia coli
0.34
-
(S)-ureidoglycolate
mutant D141N, pH 8.1, 30C
Escherichia coli
1.04
-
(S)-ureidoglycolate
mutant R259A, pH 8.1, 30C
Escherichia coli
1.1
-
NAD+
mutant S43A, pH 8.1, 30C
Escherichia coli
1.51
-
NAD+
mutant Y52F, pH 8.1, 30C
Escherichia coli
1.6
-
NAD+
mutant H44A, pH 8.1, 30C
Escherichia coli
1.81
-
NAD+
mutant D141N, pH 8.1, 30C
Escherichia coli
2.04
-
NAD+
mutant D141A, pH 8.1, 30C
Escherichia coli
2.35
-
NAD+
mutant D141E, pH 8.1, 30C
Escherichia coli
3.49
-
(S)-ureidoglycolate
mutant M251A, pH 8.1, 30C
Escherichia coli
6.23
-
NAD+
mutant R259A, pH 8.1, 30C
Escherichia coli
32.9
-
NAD+
mutant M251A, pH 8.1, 30C
Escherichia coli
54
-
(S)-ureidoglycolate
wild-type, pH 8.1, 30C
Escherichia coli
110
-
NAD+
wild-type, pH 8.1, 30C
Escherichia coli
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.01
-
NAD+
mutant S140A, pH 8.1, 30C
Escherichia coli
0.1
-
(S)-ureidoglycolate
mutant H44A, pH 8.1, 30C; mutant S140A, pH 8.1, 30C
Escherichia coli
0.11
-
(S)-ureidoglycolate
mutant Y52F, pH 8.1, 30C
Escherichia coli
0.12
-
(S)-ureidoglycolate
mutant D141E, pH 8.1, 30C
Escherichia coli
0.13
-
(S)-ureidoglycolate
mutant S43A, pH 8.1, 30C
Escherichia coli
0.31
-
(S)-ureidoglycolate
mutant D141A, pH 8.1, 30C
Escherichia coli
0.34
-
(S)-ureidoglycolate
mutant D141N, pH 8.1, 30C
Escherichia coli
1.04
-
(S)-ureidoglycolate
mutant R259A, pH 8.1, 30C
Escherichia coli
1.1
-
NAD+
mutant S43A, pH 8.1, 30C
Escherichia coli
1.51
-
NAD+
mutant Y52F, pH 8.1, 30C
Escherichia coli
1.6
-
NAD+
mutant H44A, pH 8.1, 30C
Escherichia coli
1.81
-
NAD+
mutant D141N, pH 8.1, 30C
Escherichia coli
2.04
-
NAD+
mutant D141A, pH 8.1, 30C
Escherichia coli
2.35
-
NAD+
mutant D141E, pH 8.1, 30C
Escherichia coli
3.49
-
(S)-ureidoglycolate
mutant M251A, pH 8.1, 30C
Escherichia coli
6.23
-
NAD+
mutant R259A, pH 8.1, 30C
Escherichia coli
32.9
-
NAD+
mutant M251A, pH 8.1, 30C
Escherichia coli
54
-
(S)-ureidoglycolate
wild-type, pH 8.1, 30C
Escherichia coli
110
-
NAD+
wild-type, pH 8.1, 30C
Escherichia coli
Other publictions for EC 1.1.1.154
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
726324
Rothe
Novel insights into E. colis h ...
Escherichia coli
PLoS ONE
8
e56906
2013
-
-
1
1
11
-
-
20
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
1
-
-
20
1
-
-
1
-
-
-
-
-
1
1
1
11
-
-
-
-
20
-
-
-
-
-
-
-
-
-
-
-
-
1
1
1
-
-
20
1
-
-
-
-
-
-
-
19
19
286034
Van der Drift
S-ureidoglycolate dehydrogenas ...
Arthrobacter allantoicus
Arch. Biochem. Biophys.
145
465-469
1971
-
-
-
-
-
1
4
3
-
-
-
1
-
1
-
-
1
-
-
1
1
-
1
-
-
-
1
-
1
-
1
2
-
-
-
-
-
-
2
-
-
1
-
4
-
3
-
-
-
1
-
-
-
1
-
1
1
-
1
-
-
-
1
-
1
-
1
-
-
-
-
-
-
-