EC Number | Application | Comment | Organism |
---|---|---|---|
4.3.1.1 | biotechnology | putative and attractive enzyme for the enantioselective synthesis of N-substituted aspartic acids | Bacillus sp. YM55-1 |
EC Number | Cloned (Comment) | Organism |
---|---|---|
4.3.1.1 | cloned and overexpressed in Escherichia coli TOP10 | Bacillus sp. YM55-1 |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.3.1.1 | additional information | - |
additional information | enzyme processes L-aspartic acid, but not D-aspartic acid | Bacillus sp. YM55-1 | |
4.3.1.1 | 1.54 | - |
hydrazine | reverse reaction, 750 mM hydrazine, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 1.61 | - |
NH3 | reverse reaction, 200 mM NH3, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 2.78 | - |
hydroxylamine | reverse reaction, 400 mM hydroxylamine at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 15 | - |
L-aspartate | his-tagged protein, pH 8.5, 25°C, in 50 mM NaHPO4 buffer | Bacillus sp. YM55-1 | |
4.3.1.1 | 85 | - |
NH3 | reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 151 | - |
hydroxylamine | reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 308 | - |
hydrazine | reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
4.3.1.1 | Mg2+ | enzyme is allosterically activated by its substrate and Mg2+ ions, which are required for activity at alkaline pH | Bacillus sp. YM55-1 |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.3.1.1 | L-aspartate | Bacillus sp. YM55-1 | key role in nitrogen metabolism by catalyzing the reversible elimination of NH3 from l-aspartate | fumarate + NH3 | - |
r | |
4.3.1.1 | additional information | Bacillus sp. YM55-1 | AspA is one of the most specific enzymes known, no other substrates can replace L-aspartic acid in the deamination reaction | ? | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
4.3.1.1 | Bacillus sp. YM55-1 | - |
thermophilic | - |
EC Number | Purification (Comment) | Organism |
---|---|---|
4.3.1.1 | recombinant enzyme containing a C-terminal His6 tag is purified by one-step affinity purification | Bacillus sp. YM55-1 |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
4.3.1.1 | additional information | - |
His6-tag at enzyme does not affect AspB activity | Bacillus sp. YM55-1 |
4.3.1.1 | additional information | - |
no activity with D-aspartic acid, L-cysteine, L-histidine, L-phenylalanine, L-glutamine, L-tyrosine, L-serine, L-alanine, L-valine, L-leucine, L-threonine, L-lysine, alpha-methyl-DL-aspartic acid, beta-methyl-DL-aspartic acid, L-glutamate, beta-alanine, beta-DL-aminobutyric acid, beta-asparagine, beta-phenylalanine and beta-leucine as substrates (25 mm substrate in 100 mm Na2HPO4 buffer, pH 9.0 at 37°C) | Bacillus sp. YM55-1 |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
4.3.1.1 | hydrazine + fumarate | reverse reaction, 100% conversion after 1 day at pH 7 | Bacillus sp. YM55-1 | 2-hydrazinosuccinic acid | - |
r | |
4.3.1.1 | hydroxylamine + fumarate | reverse reaction, 100% conversion after 20 min at pH 7 | Bacillus sp. YM55-1 | N-hydroxyaspartic acid | - |
r | |
4.3.1.1 | L-aspartate | key role in nitrogen metabolism by catalyzing the reversible elimination of NH3 from l-aspartate | Bacillus sp. YM55-1 | fumarate + NH3 | - |
r | |
4.3.1.1 | methoxylamine + fumarate | reverse reaction, 100% conversion after 6 days at pH 8 and after 12 days at pH 7 | Bacillus sp. YM55-1 | N-methoxyaspartic acid | - |
r | |
4.3.1.1 | methylamine + fumarate | reverse reaction, 100% conversion after 7 day at pH 8 | Bacillus sp. YM55-1 | N-methylaspartic acid | - |
r | |
4.3.1.1 | additional information | AspA is one of the most specific enzymes known, no other substrates can replace L-aspartic acid in the deamination reaction | Bacillus sp. YM55-1 | ? | - |
? | |
4.3.1.1 | additional information | AspB efficiently processes small substituted amines, but displays very low (methoxylamine and methamine) or no (ethylamine, glycine, and formamide) activity with larger amine nucleophiles | Bacillus sp. YM55-1 | ? | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
4.3.1.1 | homotetramer | 4 subunits of 478 amino acids | Bacillus sp. YM55-1 |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
4.3.1.1 | aspartase | - |
Bacillus sp. YM55-1 |
4.3.1.1 | aspartate ammonia lyase | - |
Bacillus sp. YM55-1 |
4.3.1.1 | aspB | - |
Bacillus sp. YM55-1 |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
4.3.1.1 | 31 | - |
hydroxylamine | reverse reaction, 400 mM hydroxylamine at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 40 | - |
L-aspartate | his-tagged protein, pH 8.5, 25°C, in 50 mM NaHPO4 buffer | Bacillus sp. YM55-1 | |
4.3.1.1 | 59 | - |
NH3 | reverse reaction, 200 mM NH3, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 89 | - |
NH3 | reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 90 | - |
fumarate | reverse reaction | Bacillus sp. YM55-1 | |
4.3.1.1 | 92 | - |
hydrazine | reverse reaction, 750 mM hydrazine, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 94 | - |
hydrazine | reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 | |
4.3.1.1 | 99 | - |
hydroxylamine | reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate | Bacillus sp. YM55-1 |