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Literature summary extracted from

  • Wang, J.; Gao, D.; Yu, X.; Li, W.; Qi, Q.
    Evolution of a chimeric aspartate kinase for L-lysine production using a synthetic RNA device (2015), Appl. Microbiol. Biotechnol., 99, 8527-8536.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.4 functional recombinant expression of His-tagged chimeric mutant BT3 in Escherichia coli strain BL21(DE3) Thermus thermophilus
2.7.2.4 functional recombinant expression of His-tagged chimeric mutant BT3 in Escherichia coli strain BL21(DE3) Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.4 G10D/G324W construction of an engineered chimeric mutant enzyme containing the N-terminal catalytic region from Bacillus subtilis AKII and the C-terminal region from Thermus thermophilus AKII, through random mutagenesis and then screened using a high throughput synthetic RNA device which comprises of an L-lysine-sensing riboswitch and a selection module. Of three evolved aspartate kinases, the best mutant BT3 shows 160% increased in vitro activity compared to the wild-type enzyme from Bacillus subtilis. The mutant enzymes is feedback-resistant to L-lysine Thermus thermophilus
2.7.2.4 G10D/G324W construction of an engineered chimeric mutant enzyme containing the N-terminal catalytic region from Bacillus subtilis AKII and the C-terminal region from Thermus thermophilus AKII, through random mutagenesis and then screened using a high throughput synthetic RNA device which comprises of an L-lysine-sensing riboswitch and a selection module. Of three evolved aspartate kinases, the best mutant BT3 shows 160% increased in vitro activity compared to the wild-type enzyme from Bacillus subtilis. The mutant enzymes is feedback-resistant to L-lysine Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.4 Mg2+ required Thermus thermophilus
2.7.2.4 Mg2+ required Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.2.4 ATP + L-aspartate Thermus thermophilus
-
 ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate Bacillus subtilis
-
 ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate Bacillus subtilis 168
-
 ADP + 4-phospho-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Bacillus subtilis P08495 gene lysC
-
2.7.2.4 Bacillus subtilis 168 P08495 gene lysC
-
2.7.2.4 Thermus thermophilus P61489 gene ask
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate
-
 Thermus thermophilus ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate
-
 Bacillus subtilis ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate
-
 Bacillus subtilis 168 ADP + 4-phospho-L-aspartate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 AKII
-
 Bacillus subtilis
2.7.2.4 aspartokinase UniProt Thermus thermophilus
2.7.2.4 aspartokinase 2 UniProt Bacillus subtilis

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.2.4 ATP
-
 Thermus thermophilus
2.7.2.4 ATP
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
2.7.2.4 evolution the enzyme belongs to class II aspartate kinases Thermus thermophilus
2.7.2.4 evolution the enzyme belongs to class II aspartate kinases Bacillus subtilis