Literature summary for 2.7.2.4 extracted from

Dong, X.; Zhao, Y.; Zhao, J.; Wang, X.
Characterization of aspartate kinase and homoserine dehydrogenase from Corynebacterium glutamicum IWJ001 and systematic investigation of L-isoleucine biosynthesis (2016), J. Ind. Microbiol. Biotechnol., 43, 873-885.

Cloned(Commentary)

Cloned (Comment)	Organism
expressing mutant gene lysC1 alone in Corynebacterium glutamicum wild-type strain ATCC13869 leads to exclusive L-lysine accumulation, co-expressing hom1 and thrB1 with lysC1 shifts partial carbon flux from L-lysine to L-threonine with minor L-isoleucine and no L-homoserine accumulation, further co-expressing ilvA1 completely deplets L-threonine and strongly shifts carbon flux from L-lysine to L-isoleucine	Corynebacterium glutamicum

Cloned (Comment)

Organism

expressing mutant gene lysC1 alone in Corynebacterium glutamicum wild-type strain ATCC13869 leads to exclusive L-lysine accumulation, co-expressing hom1 and thrB1 with lysC1 shifts partial carbon flux from L-lysine to L-threonine with minor L-isoleucine and no L-homoserine accumulation, further co-expressing ilvA1 completely deplets L-threonine and strongly shifts carbon flux from L-lysine to L-isoleucine

Corynebacterium glutamicum

Protein Variants

Protein Variants	Comment	Organism
A279T	isolated from Corynebacterium glutamicum strain IWJ001, aspartate kinase mutant AKA279T is encoded by gene lysC1. The mutant enzymes is completely resistant to feed-back inhibition by L-threonine and L-lysine	Corynebacterium glutamicum

Inhibitors

Inhibitors	Comment	Organism
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 13869	-	ADP + 4-phospho-L-aspartate	-	?

Organism

Organism	UniProt	Comment	Textmining
Corynebacterium glutamicum	-	gene lysC	-
Corynebacterium glutamicum ATCC 13869	-	gene lysC	-

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 13869	ADP + 4-phospho-L-aspartate	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Corynebacterium glutamicum

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Corynebacterium glutamicum

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Corynebacterium glutamicum

General Information

General Information	Comment	Organism
metabolism	the enzyme catalyzes the first step of the biosynthesis of several amino acids, with L-isoleucine being the endproductof the pathway, overview. The enzyme is regulated by feedback inhibition, overview	Corynebacterium glutamicum