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Literature summary 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.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.3 gene hom1, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), recombinant overexpression of constructs comprising the enzyme with homoserine kinase, aspartate kinase, acetohydroxy acid synthase, or threonine dehydratase, overview Corynebacterium glutamicum
2.7.2.4 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

EC Number Protein Variants Comment Organism
1.1.1.3 G378S construction of a homoserine dehydrogenase mutant HDG378S, encoded by hom1, in Corynebacterium glutamicum strain IWJ001, one of the best L-isoleucine producing strains. Strain HDG378S is partially resistant to L-threonine with the half maximal inhibitory concentration between 12 and 14 mM. Overexpression of lysC1, hom1 and thrB1 increased L-threonine and L-lysine production in Corynebacterium glutamicum ATCC13869 by 96folds and 21.2folds, respectively, overview Corynebacterium glutamicum
1.1.1.3 additional information releasing the enzymes of the L-threonine biosynthesis pathway from feedback control and coordinating their expression plays a pivotal role in engineering Corynebacterium glutamicum into L-isoleucine producers, construction of transgenic Corynebacterium glutamicum with deregulated L-threonine biosynthesis pathway enzymes for enhanced L-isoleucine biosynthesis Corynebacterium glutamicum
2.7.2.4 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

EC Number Inhibitors Comment Organism Structure
1.1.1.3 L-threonine the enzyme activity is subjected to feedback regulation by L-threonine Corynebacterium glutamicum
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.
1.1.1.3 L-homoserine + NADP+ Corynebacterium glutamicum
-
 L-aspartate 4-semialdehyde + NADPH + H+
-
 r
1.1.1.3 L-homoserine + NADP+ Corynebacterium glutamicum IWJ001
-
 L-aspartate 4-semialdehyde + NADPH + H+
-
 r
2.7.2.4 ATP + L-aspartate Corynebacterium glutamicum
-
 ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate Corynebacterium glutamicum ATCC 13869
-
 ADP + 4-phospho-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.3 Corynebacterium glutamicum P08499
-
-
1.1.1.3 Corynebacterium glutamicum IWJ001 P08499
-
-
2.7.2.4 Corynebacterium glutamicum
-
 gene lysC
-
2.7.2.4 Corynebacterium glutamicum ATCC 13869
-
 gene lysC
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.3 L-homoserine + NADP+
-
 Corynebacterium glutamicum L-aspartate 4-semialdehyde + NADPH + H+
-
 r
1.1.1.3 L-homoserine + NADP+
-
 Corynebacterium glutamicum IWJ001 L-aspartate 4-semialdehyde + NADPH + H+
-
 r
2.7.2.4 ATP + L-aspartate
-
 Corynebacterium glutamicum ADP + 4-phospho-L-aspartate
-
 ?
2.7.2.4 ATP + L-aspartate
-
 Corynebacterium glutamicum ATCC 13869 ADP + 4-phospho-L-aspartate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.3 hom
-
 Corynebacterium glutamicum

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.4 30
-
 assay at Corynebacterium glutamicum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.4 7.5
-
 assay at Corynebacterium glutamicum

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.3 NADP+
-
 Corynebacterium glutamicum
1.1.1.3 NADPH
-
 Corynebacterium glutamicum
2.7.2.4 ATP
-
 Corynebacterium glutamicum

General Information

EC Number General Information Comment Organism
1.1.1.3 metabolism homoserine dehydrogenase is a key enzyme in the L-threonine pathway Corynebacterium glutamicum
2.7.2.4 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