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Literature summary extracted from
- Highly stable meso-diaminopimelate dehydrogenase from an Ureibacillus thermosphaericus strain A1 isolated from a Japanese compost: purification, characterization and sequencing (2011), AMB Express, 1, 43.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.4.1.16 | DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain Rosetta (DE3) | Ureibacillus thermosphaericus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.1.16 | 4-chloromercuribenzoate | complete inhibition at 0.1 mM | Ureibacillus thermosphaericus |  |
| 1.4.1.16 | Cu2+ | strong inhibition at 1 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | HgCl2 | complete inhibition at 0.1 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | L-cysteine | strong inhibition at 5 mM | Ureibacillus thermosphaericus | |
| 1.4.1.16 | additional information | no inhibition by Zn2+, Co2+ and Ni2+ at 1 mM, and by 1 mM of D-lysine, L-lysine, EDTA, 2,2'-dipyridyl, NaN3, or iodoacetic acid | Ureibacillus thermosphaericus | |
| 1.4.1.16 | Thioglycollate | strong inhibition at 5 mM | Ureibacillus thermosphaericus | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.16 | 40000 | - |
2 * 40000 SDS-PAGE | Ureibacillus thermosphaericus |
| 1.4.1.16 | 80000 | - |
gel filtration | 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+ | - |
? | |
| 1.4.1.16 | meso-2,6-diaminoheptanedioate + H2O + NADP+ | Ureibacillus thermosphaericus A1 | - |
L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+ | - |
? | |
| 1.4.1.16 | additional information | Ureibacillus thermosphaericus | meso-diaminopimelate dehydrogenase catalyzes the NAD(P)-dependent oxidative deamination of meso-diaminopimelate stereoselectively acting on the D-configuration of meso-diaminopimelate. The enzyme is highly selective for meso-diaminopimelate as the electron donor, and NADP+ but not NAD+ can serve as the electron acceptor | ? | - |
? | |
| 1.4.1.16 | additional information | Ureibacillus thermosphaericus A1 | meso-diaminopimelate dehydrogenase catalyzes the NAD(P)-dependent oxidative deamination of meso-diaminopimelate stereoselectively acting on the D-configuration of meso-diaminopimelate. The enzyme is highly selective for meso-diaminopimelate as the electron donor, and NADP+ but not NAD+ can serve as the electron acceptor | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.4.1.16 | Ureibacillus thermosphaericus | - |
a thermophilic bacterium isolated from compost in Japan | - |
| 1.4.1.16 | Ureibacillus thermosphaericus A1 | - |
a thermophilic bacterium isolated from compost in Japan | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.4.1.16 | recombinant enzyme from Escherichia coli strain Rosetta (DE3) by heat treatment and affinity chromatography, native enzyme 47fold to homogeneity by ammonium sulfate fractionation, and hydrophobic interaction and anion exchange chromatography, followed by preparative slab PAGE | Ureibacillus thermosphaericus |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.16 | 8.28 | - |
purified enzyme, pH 7.2, 50°C | 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+ | - |
? | |
| 1.4.1.16 | meso-2,6-diaminoheptanedioate + H2O + NADP+ | - |
Ureibacillus thermosphaericus A1 | L-2-amino-6-oxoheptanedioate + NH3 + NADPH + H+ | - |
? | |
| 1.4.1.16 | additional information | meso-diaminopimelate dehydrogenase catalyzes the NAD(P)-dependent oxidative deamination of meso-diaminopimelate stereoselectively acting on the D-configuration of meso-diaminopimelate. The enzyme is highly selective for meso-diaminopimelate as the electron donor, and NADP+ but not NAD+ can serve as the electron acceptor | Ureibacillus thermosphaericus | ? | - |
? | |
| 1.4.1.16 | additional information | no activity with DL-2-aminopimelate, D-glutamate, L-glutamate, D-aspartate, L-aspartate, D-alanine, L-alanine, D-valine, L-valine, D-lysine, L-lysine, D-phenylalanine, L-phenylalanine, D-leucine, L-leucine, D-threonine, L-threonine, D-serine, L-serine, D-tryptophan, L-tryptophan, D-cysteine, L-cysteine, D-histidine, L-histidine, D-methionine, D-arginine, D-proline, D-asparagine, D-glutamine, D-isoleucine, and D-ornithine, and with NAD+ | Ureibacillus thermosphaericus | ? | - |
? | |
| 1.4.1.16 | additional information | meso-diaminopimelate dehydrogenase catalyzes the NAD(P)-dependent oxidative deamination of meso-diaminopimelate stereoselectively acting on the D-configuration of meso-diaminopimelate. The enzyme is highly selective for meso-diaminopimelate as the electron donor, and NADP+ but not NAD+ can serve as the electron acceptor | Ureibacillus thermosphaericus A1 | ? | - |
? | |
| 1.4.1.16 | additional information | no activity with DL-2-aminopimelate, D-glutamate, L-glutamate, D-aspartate, L-aspartate, D-alanine, L-alanine, D-valine, L-valine, D-lysine, L-lysine, D-phenylalanine, L-phenylalanine, D-leucine, L-leucine, D-threonine, L-threonine, D-serine, L-serine, D-tryptophan, L-tryptophan, D-cysteine, L-cysteine, D-histidine, L-histidine, D-methionine, D-arginine, D-proline, D-asparagine, D-glutamine, D-isoleucine, and D-ornithine, and with NAD+ | Ureibacillus thermosphaericus A1 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.4.1.16 | homodimer | 2 * 40000 SDS-PAGE | Ureibacillus thermosphaericus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.4.1.16 | meso-DAPDH | - |
Ureibacillus thermosphaericus |
| 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 | 65 | - |
- |
Ureibacillus thermosphaericus |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.16 | 60 | - |
purified enzyme, 30 min, pH 7.2, fully stable | Ureibacillus thermosphaericus |
| 1.4.1.16 | 65 | - |
purified enzyme, 30 min, pH 7.2, loss of 50% activity | Ureibacillus thermosphaericus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.16 | 10.5 | - |
- |
Ureibacillus thermosphaericus |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.4.1.16 | 5 | 11 | purified enzyme, 30 min, 50°C, fully stable | Ureibacillus thermosphaericus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.4.1.16 | NADP+ | - |
Ureibacillus thermosphaericus | |
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