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Literature summary extracted from

  • Zhao, Q.; Luo, Y.; Dou, W.; Zhang, X.; Zhang, X.; Zhang, W.; Xu, M.; Geng, Y.; Rao, Z.; Xu, Z.
    Controlling the transcription levels of argGH redistributed L-arginine metabolic flux in N-acetylglutamate kinase and ArgR-deregulated Corynebacterium crenatum (2016), J. Ind. Microbiol. Biotechnol., 43, 55-66.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.8 Mg2+ required Corynebacterium crenatum

Natural Substrates/ Products (Substrates)

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

Organism

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
-

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.8 37
-
 assay at Corynebacterium crenatum

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.8 8
-
 assay at Corynebacterium crenatum

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.2.8 ATP
-
 Corynebacterium crenatum

General Information

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