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Literature summary extracted from
- Creation of a thermostable NADP+-dependent D-amino acid dehydrogenase from Ureibacillus thermosphaericus strain A1 meso-diaminopimelate dehydrogenase by site-directed mutagenesis (2012), Biotechnol. Lett., 34, 1693-1699.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.1.16 | gene ddh, expression of wild-type enzyme and mutant Q154L/D158G/T173I/R199M/H249N in Escherichia coli strain Rosetta (DE3) | Ureibacillus thermosphaericus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.4.1.16 | Q154L/D158G/T173I/R199M/H249N | construction of a thermostable, NADP+-dependent D-amino acid dehydrogenase (DAADH) from the meso-diaminopimelate dehydrogenase of strain A1 by introducing five point mutations into amino acid residues located in the active site. In the presence of NADP+, the mutant enzyme catalyzes the oxidative deamination of several D-amino acids, including D-cyclohexylalanine, D-isoleucine, and D-2-aminooctanoate, but not of meso-diaminopimelate. The corresponding 2-oxo acids are aminated in the presence of NADPH and ammonia in the reverse reaction, mutant substrate specificity, overview. The mutant enzyme is also more thermostable than its parental meso-diaminopimelate dehydrogenase | Ureibacillus thermosphaericus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.1.16 | 2-mercaptoethanol | complete inhibition at 5 mM | Ureibacillus thermosphaericus |  |
| 1.4.1.16 | 4-chloromercuribenzoate | complete inhibition at 0.1 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | HgCl2 | complete inhibition at 0.1 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | additional information | no inhibition by EDTA, NaN3, Na2S and iodoacetate at 1 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | N-ethylmaleimide | strong inhibition at 1 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | Ni2+ | strong inhibition at 1 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | thioglycolate | complete inhibition at 5 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | Zn2+ | strong inhibition at 1 mM | Ureibacillus thermosphaericus | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.4.1.16 | additional information | - |
additional information | Michaelis-Menten kinetics | Ureibacillus thermosphaericus |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.1.16 | MnSO4 | slight activation, mutant enzyme | Ureibacillus thermosphaericus | |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.1.16 | meso-2,6-diaminoheptanedioate + H2O + NADP+ | Ureibacillus thermosphaericus | - |
L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+ | - |
r | |
| 1.4.1.16 | meso-2,6-diaminoheptanedioate + H2O + NADP+ | Ureibacillus thermosphaericus A1 | - |
L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+ | - |
r | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.1.16 | Ureibacillus thermosphaericus | G1UII1 | gene ddh | - |
| 1.4.1.16 | Ureibacillus thermosphaericus A1 | G1UII1 | gene ddh | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.4.1.16 | recombinant wild-type enzyme and mutant Q154L/D158G/T173I/R199M/H249N from Escherichia coli strain Rosetta (DE3) by heat treatment and chelating affinity chromatograhy | Ureibacillus thermosphaericus |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.4.1.16 | meso-2,6-diaminoheptanedioate + H2O + NADP+ | - |
Ureibacillus thermosphaericus | L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+ | - |
r | |
| 1.4.1.16 | meso-2,6-diaminoheptanedioate + H2O + NADP+ | - |
Ureibacillus thermosphaericus A1 | L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+ | - |
r | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.1.16 | meso-diaminopimelate dehydrogenase | - |
Ureibacillus thermosphaericus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.16 | 50 | - |
assay at | Ureibacillus thermosphaericus |
| 1.4.1.16 | 60 | - |
mutant enzyme | Ureibacillus thermosphaericus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.16 | 65 | - |
purified mutant enzyme, 30 min, pH 7.2, fully stable, half-liife is 80 min | Ureibacillus thermosphaericus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.16 | 10.5 | - |
reductive amination | Ureibacillus thermosphaericus |
| 1.4.1.16 | 11.5 | - |
oxidative deamination | Ureibacillus thermosphaericus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.1.16 | NADP+ | - |
Ureibacillus thermosphaericus | |
| 1.4.1.16 | NADPH | - |
Ureibacillus thermosphaericus | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.4.1.16 | malfunction | substrate specificity of mut-DAADH Q154L/D158G/T173I/R199M/H249N , overview | Ureibacillus thermosphaericus |
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