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Literature summary for 2.7.2.4 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
Search for more literature for 2.7.2.4

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Thermus thermophilus
ATP
-
 Bacillus subtilis

General Information

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