EC Number | Cloned (Comment) | Organism |
---|---|---|
1.4.1.1 | gene ald, phylogenetic tree, recombinant expression of His-tagged isozyme HAADH1 in Escherichia coli strain BL21(DE3) | Helicobacter aurati |
1.4.1.1 | gene CQA66_00465, phylogenetic tree, recombinant expression of His-tagged isozyme HAADH2 in Escherichia coli strain BL21(DE3) | Helicobacter aurati |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.1.1 | 0.56 | - |
pyruvate | recombinant enzyme, pH 9.0, 55°C | Helicobacter aurati | |
1.4.1.1 | 2.23 | - |
L-alanine | recombinant enzyme, pH 8.0, 55°C | Helicobacter aurati |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.1.1 | L-alanine + H2O + NAD+ | Helicobacter aurati | - |
pyruvate + NH3 + NADH + H+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.4.1.1 | Helicobacter aurati | A0A3D8J648 | - |
- |
1.4.1.1 | Helicobacter aurati | A0A3D8J924 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.4.1.1 | recombinant His-tagged isozyme HAADH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Helicobacter aurati |
1.4.1.1 | recombinant His-tagged isozyme HAADH2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Helicobacter aurati |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
1.4.1.1 | 26 | - |
purified recombinant enzyme, pH 9.0, 55°C | Helicobacter aurati |
1.4.1.1 | 268 | - |
purified recombinant enzyme, pH 9.0, 55°C | Helicobacter aurati |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.4.1.1 | 2-oxobutyrate + NH3 + NADH + H+ | - |
Helicobacter aurati | L-2-aminobutyrate + H2O + NAD+ | - |
r | |
1.4.1.1 | 2-oxoglutarate + NH3 + NADH + H+ | - |
Helicobacter aurati | L-glutamate + H2O + NAD+ | - |
r | |
1.4.1.1 | 3-fluoropyruvate + NH3 + NADH + H+ | recombinant enzyme in whole-cell catalysis at 25°C | Helicobacter aurati | 3-fluoro-L-alanine + H2O + NAD+ | - |
r | |
1.4.1.1 | glyoxylate + NH3 + NADH + H+ | - |
Helicobacter aurati | glycine + H2O + NAD+ | - |
r | |
1.4.1.1 | L-alanine + H2O + NAD+ | - |
Helicobacter aurati | pyruvate + NH3 + NADH + H+ | - |
r | |
1.4.1.1 | additional information | isozyme HAADH2 has no oxidation activity for 20 amino acids, 3-fluoroalanine, D/L-lactic acid, D/L -DOPA and L-2-aminobutyric acid. It also has no reduction activity for all tested 2-oxo acids | Helicobacter aurati | ? | - |
- |
|
1.4.1.1 | additional information | L-alanine and pyruvate are the preferred substrates of the enzyme for the deamination and amination reaction, respectively. Oxaloacetate, 2-oxobutyrate, 3-fluoropyruvate, 2-oxoglutarate, and glyoxylate show 93.30%, 8.93%, 5.62%, 2.57%, 2.51% activity compared to pyruvate, respectively | Helicobacter aurati | ? | - |
- |
|
1.4.1.1 | oxaloacetate + NH3 + NADH + H+ | - |
Helicobacter aurati | L-aspartate + H2O + NAD+ | - |
r | |
1.4.1.1 | pyruvate + NH3 + NADH + H+ | - |
Helicobacter aurati | L-alanine + H2O + NAD+ | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.4.1.1 | ADH | - |
Helicobacter aurati |
1.4.1.1 | ALD | - |
Helicobacter aurati |
1.4.1.1 | CQA66_00465 | - |
Helicobacter aurati |
1.4.1.1 | HAADH1 | - |
Helicobacter aurati |
1.4.1.1 | HAADH2 | - |
Helicobacter aurati |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.4.1.1 | 55 | - |
recombinant enzyme | Helicobacter aurati |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.4.1.1 | 8 | - |
deamination reaction, recombinant enzyme | Helicobacter aurati |
1.4.1.1 | 9 | - |
amination reaction, recombinant enzyme | Helicobacter aurati |
EC Number | pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|---|
1.4.1.1 | additional information | - |
the enzyme reaches maximum activity in the oxidation reaction at pH 9.0, but almost completely loses its activity at pH 10.0 | Helicobacter aurati |
EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|---|
1.4.1.1 | 8 | - |
most stable pH for isozyme HADDH1 is pH 8.0 | Helicobacter aurati |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.4.1.1 | additional information | the enzyme shows no activity with NADP+ and NADPH as cofactors | Helicobacter aurati | |
1.4.1.1 | NAD+ | - |
Helicobacter aurati | |
1.4.1.1 | NADH | - |
Helicobacter aurati |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.4.1.1 | evolution | sequence comparisons and phylogenetic analysis | Helicobacter aurati |
1.4.1.1 | evolution | sequence comparisons and phylogenetic analysis indicate that enzyme HAADH1 is a distinct type of alanine dehydrogenase | Helicobacter aurati |
EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.4.1.1 | 8.1 | - |
L-alanine | recombinant enzyme, pH 8.0, 55°C | Helicobacter aurati | |
1.4.1.1 | 364 | - |
pyruvate | recombinant enzyme, pH 9.0, 55°C | Helicobacter aurati |