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Literature summary 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

Application

EC Number Application Comment Organism
2.7.2.4 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.4 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

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.4 Mg2+ required Corynebacterium glutamicum

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 Corynebacterium glutamicum
-
 ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate Corynebacterium glutamicum ATCC 13032
-
 ADP + 4-phospho-L-aspartate
-
 ?

Organism

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

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 Ask
-
 Corynebacterium glutamicum
2.7.2.4 lysC
-
 Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.2.4 ATP
-
 Corynebacterium glutamicum

General Information

EC Number General Information Comment Organism
2.7.2.4 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