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Literature summary extracted from

  • Weiner, B.; Poelarends, G.J.; Janssen, D.B.; Feringa, B.L.
    Biocatalytic enantioselective synthesis of N-substituted aspartic acids by aspartate ammonia lyase (2008), Chemistry, 14, 10094-10100.
    View publication on PubMed

Application

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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.1.1 cloned and overexpressed in Escherichia coli TOP10 Bacillus sp. YM55-1

KM Value [mM]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.3.1.1 Bacillus sp. YM55-1
-
thermophilic
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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 ?
-
?

Subunits

EC Number Subunits Comment Organism
4.3.1.1 homotetramer 4 subunits of 478 amino acids Bacillus sp. YM55-1

Synonyms

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

Turnover Number [1/s]

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