Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.350 extracted from

  • Kim, M.I.; Shin, I.; Cho, S.; Lee, J.; Rhee, S.
    Structural and functional insights into (S)-ureidoglycolate dehydrogenase, a metabolic branch point enzyme in nitrogen utilization (2012), PLoS ONE, 7, e52066.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21(DE3) cells Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
apo form, in a binary complex with NADH cofactor, and in a ternary complex with NADH and glyoxylate, hanging drop vapor diffusion method, using 0.1 M MES (pH 6.0) and 4.0 M NaCl, at 22°C Escherichia coli

Protein Variants

Protein Variants Comment Organism
D141A the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
D141E the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
D141N the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
H16A inactive Escherichia coli
H44A the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
M251A the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
R259A in the mutant enzyme R259A, the kcat value is approximately 21% that of the wild type enzyme, with about an 11fold increase in Km Escherichia coli
R48A inactive Escherichia coli
S140A the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
S43A the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Escherichia coli
Y52F the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.37
-
NAD+ mutant enzyme D141E, pH and temperature not specified in the publication Escherichia coli
0.52
-
NAD+ mutant enzyme D141A, pH and temperature not specified in the publication Escherichia coli
0.56
-
NAD+ wild type enzyme, pH and temperature not specified in the publication Escherichia coli
0.65
-
NAD+ mutant enzyme H44A, pH and temperature not specified in the publication Escherichia coli
0.81
-
NAD+ mutant enzyme D141N, pH and temperature not specified in the publication Escherichia coli
0.93
-
NAD+ mutant enzyme M251A, pH and temperature not specified in the publication Escherichia coli
1.06
-
(S)-ureidoglycolate wild type enzyme, pH and temperature not specified in the publication Escherichia coli
1.26
-
NAD+ mutant enzyme Y52F, pH and temperature not specified in the publication Escherichia coli
1.39
-
NAD+ mutant enzyme S140A, pH and temperature not specified in the publication Escherichia coli
1.49
-
NAD+ mutant enzyme R259A, pH and temperature not specified in the publication Escherichia coli
2.28
-
NAD+ mutant enzyme S43A, pH and temperature not specified in the publication Escherichia coli
5.27
-
(S)-ureidoglycolate mutant enzyme D141A, pH and temperature not specified in the publication Escherichia coli
5.84
-
(S)-ureidoglycolate mutant enzyme D141N, pH and temperature not specified in the publication Escherichia coli
10.75
-
(S)-ureidoglycolate mutant enzyme S43A, pH and temperature not specified in the publication Escherichia coli
11.47
-
(S)-ureidoglycolate mutant enzyme R259A, pH and temperature not specified in the publication Escherichia coli
12.38
-
(S)-ureidoglycolate mutant enzyme S140A, pH and temperature not specified in the publication Escherichia coli
13.15
-
(S)-ureidoglycolate mutant enzyme M251A, pH and temperature not specified in the publication Escherichia coli
14.13
-
(S)-ureidoglycolate mutant enzyme D141E, pH and temperature not specified in the publication Escherichia coli
16.82
-
(S)-ureidoglycolate mutant enzyme Y52F, pH and temperature not specified in the publication Escherichia coli
16.94
-
(S)-ureidoglycolate mutant enzyme H44A, pH and temperature not specified in the publication Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-ureidoglycolate + NAD+ Escherichia coli
-
oxalurate + NADH + H+
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P77555
-
-

Purification (Commentary)

Purification (Comment) Organism
immobilized metal affinity chromatography Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-ureidoglycolate + NAD+
-
Escherichia coli oxalurate + NADH + H+
-
?

Subunits

Subunits Comment Organism
homodimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
(S)-ureidoglycolate dehydrogenase
-
Escherichia coli
AllD
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.02
-
NAD+ mutant enzyme S140A, pH and temperature not specified in the publication Escherichia coli
0.87
-
NAD+ mutant enzyme D141E, pH and temperature not specified in the publication Escherichia coli
1.03
-
NAD+ mutant enzyme H44A, pH and temperature not specified in the publication Escherichia coli
1.06
-
NAD+ mutant enzyme D141A, pH and temperature not specified in the publication Escherichia coli
1.29
-
(S)-ureidoglycolate mutant enzyme S140A, pH and temperature not specified in the publication Escherichia coli
1.37
-
(S)-ureidoglycolate mutant enzyme S43A, pH and temperature not specified in the publication Escherichia coli
1.47
-
NAD+ mutant enzyme D141N, pH and temperature not specified in the publication Escherichia coli
1.62
-
(S)-ureidoglycolate mutant enzyme D141A, pH and temperature not specified in the publication Escherichia coli
1.67
-
(S)-ureidoglycolate mutant enzyme D141E, pH and temperature not specified in the publication Escherichia coli
1.76
-
(S)-ureidoglycolate mutant enzyme H44A, pH and temperature not specified in the publication Escherichia coli
1.9
-
NAD+ mutant enzyme Y52F, pH and temperature not specified in the publication Escherichia coli
1.92
-
(S)-ureidoglycolate mutant enzyme Y52F, pH and temperature not specified in the publication Escherichia coli
1.97
-
(S)-ureidoglycolate mutant enzyme D141N, pH and temperature not specified in the publication Escherichia coli
2.51
-
NAD+ mutant enzyme S43A, pH and temperature not specified in the publication Escherichia coli
9.29
-
NAD+ mutant enzyme R259A, pH and temperature not specified in the publication Escherichia coli
11.98
-
(S)-ureidoglycolate mutant enzyme R259A, pH and temperature not specified in the publication Escherichia coli
30.65
-
NAD+ mutant enzyme M251A, pH and temperature not specified in the publication Escherichia coli
45.98
-
(S)-ureidoglycolate mutant enzyme M251A, pH and temperature not specified in the publication Escherichia coli
57.06
-
(S)-ureidoglycolate wild type enzyme, pH and temperature not specified in the publication Escherichia coli
62.39
-
NAD+ wild type enzyme, pH and temperature not specified in the publication Escherichia coli

Cofactor

Cofactor Comment Organism Structure
NAD+ the enzyme selectively utilizes NAD+ as a cofactor Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.01
-
NAD+ mutant enzyme S140A, pH and temperature not specified in the publication Escherichia coli
0.1
-
(S)-ureidoglycolate mutant enzyme H44A, pH and temperature not specified in the publication Escherichia coli
0.1
-
(S)-ureidoglycolate mutant enzyme S140A, pH and temperature not specified in the publication Escherichia coli
0.11
-
(S)-ureidoglycolate mutant enzyme Y52F, pH and temperature not specified in the publication Escherichia coli
0.12
-
(S)-ureidoglycolate mutant enzyme D141E, pH and temperature not specified in the publication Escherichia coli
0.13
-
(S)-ureidoglycolate mutant enzyme S43A, pH and temperature not specified in the publication Escherichia coli
0.31
-
(S)-ureidoglycolate mutant enzyme D141A, pH and temperature not specified in the publication Escherichia coli
0.34
-
(S)-ureidoglycolate mutant enzyme D141N, pH and temperature not specified in the publication Escherichia coli
1.04
-
(S)-ureidoglycolate mutant enzyme R259A, pH and temperature not specified in the publication Escherichia coli
1.1
-
NAD+ mutant enzyme S43A, pH and temperature not specified in the publication Escherichia coli
1.51
-
NAD+ mutant enzyme Y52F, pH and temperature not specified in the publication Escherichia coli
1.6
-
NAD+ mutant enzyme H44A, pH and temperature not specified in the publication Escherichia coli
1.81
-
NAD+ mutant enzyme D141N, pH and temperature not specified in the publication Escherichia coli
2.04
-
NAD+ mutant enzyme D141A, pH and temperature not specified in the publication Escherichia coli
2.35
-
NAD+ mutant enzyme D141E, pH and temperature not specified in the publication Escherichia coli
3.49
-
(S)-ureidoglycolate mutant enzyme M251A, pH and temperature not specified in the publication Escherichia coli
6.23
-
NAD+ mutant enzyme R259A, pH and temperature not specified in the publication Escherichia coli
32.9
-
NAD+ mutant enzyme M251A, pH and temperature not specified in the publication Escherichia coli
54.3
-
(S)-ureidoglycolate wild type enzyme, pH and temperature not specified in the publication Escherichia coli
110
-
NAD+ wild type enzyme, pH and temperature not specified in the publication Escherichia coli