EC Number | Cloned (Comment) | Organism |
---|---|---|
2.7.2.8 | gene argB, cloning in Escherichia coli strain JM109 and recombinant expression of wild-type and mutant enzymes in Corynebacterium crenatum strain SYPA5-5 | Corynebacterium crenatum |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.7.2.8 | A26V | site-directed mutagenesis, the mutation deregulates the feedback inhibition of the enzyme | Corynebacterium crenatum |
2.7.2.8 | E19R | site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation | Corynebacterium crenatum |
2.7.2.8 | G287D | site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation | Corynebacterium crenatum |
2.7.2.8 | H268N | site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinate synthase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine | Corynebacterium crenatum |
2.7.2.8 | H268N | site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation | Corynebacterium crenatum |
2.7.2.8 | H26E | site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation | Corynebacterium crenatum |
2.7.2.8 | M31V | site-directed mutagenesis, the mutation deregulates the feedback inhibition of the enzyme | Corynebacterium crenatum |
2.7.2.8 | additional information | construction of feedback inhibition deregulated Corynebacterium crenatum mutant strains, phenotypes, overview | Corynebacterium crenatum |
2.7.2.8 | R209A | site-directed mutagenesis, the mutant strain shows accumulation of large amounts of pathway intermediates L-citrulline and L-ornithine and decreased production of L-arginine. Transcription levels of argGH decrease accompanied with the reduction of argininosuccinase activity, which leads to the metabolic obstacle from L-citrulline to L-arginine | Corynebacterium crenatum |
2.7.2.8 | R209A | site-directed mutagenesis, the mutation increases the 50% inhibitoryL--arginine concentration significantly in vitro, which deregulates the feedback inhibition of CcNAGK by L-arginine in SYPA5-5 during the fermentation | Corynebacterium crenatum |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.7.2.8 | L-arginine | feedback inhibition. SYPA5-5 N-acetylglutamate kinase feedback inhibition by L-arginine can be deregulated by introducing point mutations, H268N or R209A | Corynebacterium crenatum |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.7.2.8 | Mg2+ | required | Corynebacterium crenatum |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.2.8 | ATP + N-acetyl-L-glutamate | Corynebacterium crenatum | - |
ADP + N-acetyl-L-glutamyl 5-phosphate | - |
r | |
2.7.2.8 | ATP + N-acetyl-L-glutamate | Corynebacterium crenatum SYPA5-5 | - |
ADP + N-acetyl-L-glutamyl 5-phosphate | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.7.2.8 | Corynebacterium crenatum | Q6R6P5 | gene argB | - |
2.7.2.8 | Corynebacterium crenatum SYPA5-5 | Q6R6P5 | gene argB | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.7.2.8 | ATP + N-acetyl-L-glutamate | - |
Corynebacterium crenatum | ADP + N-acetyl-L-glutamyl 5-phosphate | - |
r | |
2.7.2.8 | ATP + N-acetyl-L-glutamate | - |
Corynebacterium crenatum SYPA5-5 | ADP + N-acetyl-L-glutamyl 5-phosphate | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.7.2.8 | CcNAGK | - |
Corynebacterium crenatum |
2.7.2.8 | N-acetylglutamate kinase | - |
Corynebacterium crenatum |
2.7.2.8 | SYPA5-5 N-acetylglutamate kinase | - |
Corynebacterium crenatum |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.7.2.8 | 37 | - |
assay at | Corynebacterium crenatum |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.7.2.8 | 8 | - |
assay at | Corynebacterium crenatum |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.7.2.8 | ATP | - |
Corynebacterium crenatum |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.7.2.8 | metabolism | N-acetylglutamate synthase/kinase catalyzes a rate limiting step in L-arginine biosynthesis. The activity of the enzyme is allosterically regulated by L-arginine, The pathway and regulatory modes involved in l-arginine biosynthesis in Corynebacterium crenatum SYPA5-5, overview | Corynebacterium crenatum |