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Literature summary for 4.3.1.1 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
Search for more literature for 4.3.1.1

Application

Application Comment Organism
biotechnology putative and attractive enzyme for the enantioselective synthesis of N-substituted aspartic acids Bacillus sp. YM55-1

Cloned(Commentary)

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

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information enzyme processes L-aspartic acid, but not D-aspartic acid Bacillus sp. YM55-1
1.54
-
 hydrazine reverse reaction, 750 mM hydrazine, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
1.61
-
 NH3 reverse reaction, 200 mM NH3, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
2.78
-
 hydroxylamine reverse reaction, 400 mM hydroxylamine at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
15
-
 L-aspartate his-tagged protein, pH 8.5, 25°C, in 50 mM NaHPO4 buffer Bacillus sp. YM55-1
85
-
 NH3 reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
151
-
 hydroxylamine reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
308
-
 hydrazine reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1

Metals/Ions

Metals/Ions Comment Organism Structure
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)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-aspartate Bacillus sp. YM55-1 key role in nitrogen metabolism by catalyzing the reversible elimination of NH3 from l-aspartate fumarate + NH3
-
 r
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

Organism UniProt Comment Textmining
Bacillus sp. YM55-1
-
 thermophilic
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme containing a C-terminal His6 tag is purified by one-step affinity purification Bacillus sp. YM55-1

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 His6-tag at enzyme does not affect AspB activity Bacillus sp. YM55-1
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hydrazine + fumarate reverse reaction, 100% conversion after 1 day at pH 7 Bacillus sp. YM55-1 2-hydrazinosuccinic acid
-
 r
hydroxylamine + fumarate reverse reaction, 100% conversion after 20 min at pH 7 Bacillus sp. YM55-1 N-hydroxyaspartic acid
-
 r
L-aspartate key role in nitrogen metabolism by catalyzing the reversible elimination of NH3 from l-aspartate Bacillus sp. YM55-1 fumarate + NH3
-
 r
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
methylamine + fumarate reverse reaction, 100% conversion after 7 day at pH 8 Bacillus sp. YM55-1 N-methylaspartic acid
-
 r
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 ?
-
 ?
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

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

Synonyms

Synonyms Comment Organism
aspartase
-
 Bacillus sp. YM55-1
aspartate ammonia lyase
-
 Bacillus sp. YM55-1
aspB
-
 Bacillus sp. YM55-1

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
31
-
 hydroxylamine reverse reaction, 400 mM hydroxylamine at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
40
-
 L-aspartate his-tagged protein, pH 8.5, 25°C, in 50 mM NaHPO4 buffer Bacillus sp. YM55-1
59
-
 NH3 reverse reaction, 200 mM NH3, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
89
-
 NH3 reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
90
-
 fumarate reverse reaction Bacillus sp. YM55-1
92
-
 hydrazine reverse reaction, 750 mM hydrazine, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
94
-
 hydrazine reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1
99
-
 hydroxylamine reverse reaction, 20 mM fumarate, at pH 8, 22°C in 50 mM phosphate Bacillus sp. YM55-1