Any feedback?
Literature summary for 1.4.1.1 extracted from
- A novel type alanine dehydrogenase from Helicobacter aurati molecular characterization and application (2020), Int. J. Biol. Macromol., 161, 636-642 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ald, phylogenetic tree, recombinant expression of His-tagged isozyme HAADH1 in Escherichia coli strain BL21(DE3) | Helicobacter aurati |
| gene CQA66_00465, phylogenetic tree, recombinant expression of His-tagged isozyme HAADH2 in Escherichia coli strain BL21(DE3) | Helicobacter aurati |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.56 | - |
pyruvate | recombinant enzyme, pH 9.0, 55°C | Helicobacter aurati |  |
| 2.23 | - |
L-alanine | recombinant enzyme, pH 8.0, 55°C | Helicobacter aurati | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| L-alanine + H2O + NAD+ | Helicobacter aurati | - |
pyruvate + NH3 + NADH + H+ | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Helicobacter aurati | A0A3D8J648 | - |
- |
| Helicobacter aurati | A0A3D8J924 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged isozyme HAADH1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Helicobacter aurati |
| recombinant His-tagged isozyme HAADH2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Helicobacter aurati |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 26 | - |
purified recombinant enzyme, pH 9.0, 55°C | Helicobacter aurati |
| 268 | - |
purified recombinant enzyme, pH 9.0, 55°C | Helicobacter aurati |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2-oxobutyrate + NH3 + NADH + H+ | - |
Helicobacter aurati | L-2-aminobutyrate + H2O + NAD+ | - |
r | |
| 2-oxoglutarate + NH3 + NADH + H+ | - |
Helicobacter aurati | L-glutamate + H2O + NAD+ | - |
r | |
| 3-fluoropyruvate + NH3 + NADH + H+ | recombinant enzyme in whole-cell catalysis at 25°C | Helicobacter aurati | 3-fluoro-L-alanine + H2O + NAD+ | - |
r | |
| glyoxylate + NH3 + NADH + H+ | - |
Helicobacter aurati | glycine + H2O + NAD+ | - |
r | |
| L-alanine + H2O + NAD+ | - |
Helicobacter aurati | pyruvate + NH3 + NADH + H+ | - |
r | |
| 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 | ? | - |
- |
|
| 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 | ? | - |
- |
|
| oxaloacetate + NH3 + NADH + H+ | - |
Helicobacter aurati | L-aspartate + H2O + NAD+ | - |
r | |
| pyruvate + NH3 + NADH + H+ | - |
Helicobacter aurati | L-alanine + H2O + NAD+ | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADH | - |
Helicobacter aurati |
| ALD | - |
Helicobacter aurati |
| CQA66_00465 | - |
Helicobacter aurati |
| HAADH1 | - |
Helicobacter aurati |
| HAADH2 | - |
Helicobacter aurati |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
recombinant enzyme | Helicobacter aurati |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
deamination reaction, recombinant enzyme | Helicobacter aurati |
| 9 | - |
amination reaction, recombinant enzyme | Helicobacter aurati |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 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 |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
most stable pH for isozyme HADDH1 is pH 8.0 | Helicobacter aurati |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the enzyme shows no activity with NADP+ and NADPH as cofactors | Helicobacter aurati | |
| NAD+ | - |
Helicobacter aurati | |
| NADH | - |
Helicobacter aurati | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | sequence comparisons and phylogenetic analysis | Helicobacter aurati |
| evolution | sequence comparisons and phylogenetic analysis indicate that enzyme HAADH1 is a distinct type of alanine dehydrogenase | Helicobacter aurati |
kcat/KM [mM/s]
| kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 8.1 | - |
L-alanine | recombinant enzyme, pH 8.0, 55°C | Helicobacter aurati | |
| 364 | - |
pyruvate | recombinant enzyme, pH 9.0, 55°C | Helicobacter aurati | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
