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Literature summary extracted from
- Structural and functional insights into (S)-ureidoglycolate dehydrogenase, a metabolic branch point enzyme in nitrogen utilization (2012), PLoS ONE, 7, e52066.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.1.1.350 | expressed in Escherichia coli BL21(DE3) cells | Escherichia coli |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.1.1.350 | 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
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.1.1.350 | D141A | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Escherichia coli |
| 1.1.1.350 | D141E | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Escherichia coli |
| 1.1.1.350 | D141N | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Escherichia coli |
| 1.1.1.350 | H16A | inactive | Escherichia coli |
| 1.1.1.350 | H44A | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Escherichia coli |
| 1.1.1.350 | M251A | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Escherichia coli |
| 1.1.1.350 | 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 |
| 1.1.1.350 | R48A | inactive | Escherichia coli |
| 1.1.1.350 | S140A | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Escherichia coli |
| 1.1.1.350 | S43A | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Escherichia coli |
| 1.1.1.350 | Y52F | the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.350 | 0.37 | - |
NAD+ | mutant enzyme D141E, pH and temperature not specified in the publication | Escherichia coli |  |
| 1.1.1.350 | 0.52 | - |
NAD+ | mutant enzyme D141A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.56 | - |
NAD+ | wild type enzyme, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.65 | - |
NAD+ | mutant enzyme H44A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.81 | - |
NAD+ | mutant enzyme D141N, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.93 | - |
NAD+ | mutant enzyme M251A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.06 | - |
(S)-ureidoglycolate | wild type enzyme, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.26 | - |
NAD+ | mutant enzyme Y52F, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.39 | - |
NAD+ | mutant enzyme S140A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.49 | - |
NAD+ | mutant enzyme R259A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 2.28 | - |
NAD+ | mutant enzyme S43A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 5.27 | - |
(S)-ureidoglycolate | mutant enzyme D141A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 5.84 | - |
(S)-ureidoglycolate | mutant enzyme D141N, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 10.75 | - |
(S)-ureidoglycolate | mutant enzyme S43A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 11.47 | - |
(S)-ureidoglycolate | mutant enzyme R259A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 12.38 | - |
(S)-ureidoglycolate | mutant enzyme S140A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 13.15 | - |
(S)-ureidoglycolate | mutant enzyme M251A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 14.13 | - |
(S)-ureidoglycolate | mutant enzyme D141E, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 16.82 | - |
(S)-ureidoglycolate | mutant enzyme Y52F, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 16.94 | - |
(S)-ureidoglycolate | mutant enzyme H44A, pH and temperature not specified in the publication | Escherichia coli | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.350 | (S)-ureidoglycolate + NAD+ | Escherichia coli | - |
oxalurate + NADH + H+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.1.1.350 | Escherichia coli | P77555 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.1.1.350 | immobilized metal affinity chromatography | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.1.1.350 | (S)-ureidoglycolate + NAD+ | - |
Escherichia coli | oxalurate + NADH + H+ | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.1.1.350 | homodimer | - |
Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.1.1.350 | (S)-ureidoglycolate dehydrogenase | - |
Escherichia coli |
| 1.1.1.350 | AllD | - |
Escherichia coli |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.350 | 0.02 | - |
NAD+ | mutant enzyme S140A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.87 | - |
NAD+ | mutant enzyme D141E, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.03 | - |
NAD+ | mutant enzyme H44A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.06 | - |
NAD+ | mutant enzyme D141A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.29 | - |
(S)-ureidoglycolate | mutant enzyme S140A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.37 | - |
(S)-ureidoglycolate | mutant enzyme S43A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.47 | - |
NAD+ | mutant enzyme D141N, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.62 | - |
(S)-ureidoglycolate | mutant enzyme D141A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.67 | - |
(S)-ureidoglycolate | mutant enzyme D141E, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.76 | - |
(S)-ureidoglycolate | mutant enzyme H44A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.9 | - |
NAD+ | mutant enzyme Y52F, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.92 | - |
(S)-ureidoglycolate | mutant enzyme Y52F, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.97 | - |
(S)-ureidoglycolate | mutant enzyme D141N, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 2.51 | - |
NAD+ | mutant enzyme S43A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 9.29 | - |
NAD+ | mutant enzyme R259A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 11.98 | - |
(S)-ureidoglycolate | mutant enzyme R259A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 30.65 | - |
NAD+ | mutant enzyme M251A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 45.98 | - |
(S)-ureidoglycolate | mutant enzyme M251A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 57.06 | - |
(S)-ureidoglycolate | wild type enzyme, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 62.39 | - |
NAD+ | wild type enzyme, pH and temperature not specified in the publication | Escherichia coli | |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.1.1.350 | NAD+ | the enzyme selectively utilizes NAD+ as a cofactor | Escherichia coli | |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.1.1.350 | 0.01 | - |
NAD+ | mutant enzyme S140A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.1 | - |
(S)-ureidoglycolate | mutant enzyme H44A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.1 | - |
(S)-ureidoglycolate | mutant enzyme S140A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.11 | - |
(S)-ureidoglycolate | mutant enzyme Y52F, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.12 | - |
(S)-ureidoglycolate | mutant enzyme D141E, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.13 | - |
(S)-ureidoglycolate | mutant enzyme S43A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.31 | - |
(S)-ureidoglycolate | mutant enzyme D141A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 0.34 | - |
(S)-ureidoglycolate | mutant enzyme D141N, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.04 | - |
(S)-ureidoglycolate | mutant enzyme R259A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.1 | - |
NAD+ | mutant enzyme S43A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.51 | - |
NAD+ | mutant enzyme Y52F, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.6 | - |
NAD+ | mutant enzyme H44A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 1.81 | - |
NAD+ | mutant enzyme D141N, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 2.04 | - |
NAD+ | mutant enzyme D141A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 2.35 | - |
NAD+ | mutant enzyme D141E, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 3.49 | - |
(S)-ureidoglycolate | mutant enzyme M251A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 6.23 | - |
NAD+ | mutant enzyme R259A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 32.9 | - |
NAD+ | mutant enzyme M251A, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 54.3 | - |
(S)-ureidoglycolate | wild type enzyme, pH and temperature not specified in the publication | Escherichia coli | |
| 1.1.1.350 | 110 | - |
NAD+ | wild type enzyme, pH and temperature not specified in the publication | Escherichia coli | |
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