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Literature summary for 2.7.2.4 extracted from

  • Viswanath, B.; Rajagopal, S.; Basha, P.; Rao, D.; Begum, P.; Rajakumari, D.; Razak, M.
    Enhancing the activity of aspartate kinase for an overproduction of L-lysine by Corynebacterium glutamicum (2016), Am. J. Biochem. Mol. Biol., 6, 33-44.
No PubMed abstract available
Search for more literature for 2.7.2.4

Application

Application Comment Organism
synthesis the enzyme is a potential target for improved production of L-lysine. Recombinants of Corynebacterium glutamicum with feedback resistant aspartate kinase would be a potential option to increase the L-lysine production by biotechnological process for industrial application Corynebacterium glutamicum

Cloned(Commentary)

Cloned (Comment) Organism
gene lysC, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 Corynebacterium glutamicum

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis is used to construct a mutant of the region coding for regulatory beta-subunit in the aspartate kinase by replacing the codon TCC-GTC to deregulate it from feedback inhibition, which results in improved L-lysine production. The mutant enzymes are resistant against S-(2-aminoethyl)-L-cysteine and feedback inhibition, phenotype, overview Corynebacterium glutamicum

Inhibitors

Inhibitors Comment Organism Structure
L-lysine feedback inhibition Corynebacterium glutamicum
L-methionine feedback inhibition Corynebacterium glutamicum
L-threonine feedback inhibition Corynebacterium glutamicum

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Corynebacterium glutamicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate Corynebacterium glutamicum
-
 ADP + 4-phospho-L-aspartate
-
 ?
ATP + L-aspartate Corynebacterium glutamicum ATCC 13032
-
 ADP + 4-phospho-L-aspartate
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium glutamicum P26512 gene lysC
-
Corynebacterium glutamicum ATCC 13032 P26512 gene lysC
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 by nickel affinity chromatography Corynebacterium glutamicum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate
-
 Corynebacterium glutamicum ADP + 4-phospho-L-aspartate
-
 ?
ATP + L-aspartate
-
 Corynebacterium glutamicum ATCC 13032 ADP + 4-phospho-L-aspartate
-
 ?

Synonyms

Synonyms Comment Organism
Ask
-
 Corynebacterium glutamicum
lysC
-
 Corynebacterium glutamicum

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Corynebacterium glutamicum

General Information

General Information Comment Organism
metabolism lysine biosynthesis in Corynebacterium glutamicum starts from aspartate and aspartate kinase is the principal enzyme involved in the lysine biosynthesis metabolic pathway, regulatory key role of aspartate kinase Corynebacterium glutamicum