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 |
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 |
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 |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.2.4 | Mg2+ | required | Corynebacterium glutamicum |
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 | - |
? |
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 | - |
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 | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.1.1.3 | hom | - |
Corynebacterium glutamicum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.2.4 | 30 | - |
assay at | Corynebacterium glutamicum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.2.4 | 7.5 | - |
assay at | Corynebacterium glutamicum |
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 |
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 |