2.3.1.35: glutamate N-acetyltransferase
This is an abbreviated version!
For detailed information about glutamate N-acetyltransferase, go to the full flat file.
Word Map on EC 2.3.1.35
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2.3.1.35
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n-acetylglutamate
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n-acetylornithine
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gonorrhoeae
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clavuligerus
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transacetylation
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clavulanic
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acetylornithinase
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2.3.1.1
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chorioretinal
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mango
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gene-enzyme
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drug development
- 2.3.1.35
- n-acetylglutamate
- n-acetylornithine
- gonorrhoeae
- clavuligerus
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transacetylation
-
clavulanic
- acetylornithinase
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2.3.1.1
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chorioretinal
- mango
-
gene-enzyme
- drug development
Reaction
Synonyms
acetylglutamate synthetase, acetylglutamate-acetylornithine transacetylase, acetylglutamic synthetase, acetylglutamic-acetylornithine transacetylase, acetylornithinase, acetylornithine glutamate acetyltransferase, acetyltransferase, glutamate, alpha-N-acetyl-L-ornithine:L-glutamate N-acetyltransferase, argJ, CcOATase, CLGAT, glutamate acetyltransferase, glutamate N-acetyltransferase, L-ornithine acetyltransferase, Mtb OAT, N-acetyl-L-glutamate synthetase, OAT, OAT2, OATase, ornithine acetyl transferase, ornithine acetyltransferase, ornithine transacetylase
ECTree
2.3.1.35 glutamate N-acetyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.3.1.35 - glutamate N-acetyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E354A
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change of residue to the corresponding Escherichia coli residue. Mutation abolishes arginine activation
F121C
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change of residue to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine activation
G360P
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change of residue to the corresponding Escherichia coli residue. Mutation abolishes arginine activation
G362S
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change of residue to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine activation
D150G
autoprocessing to alpha-,beta-subunits: 50% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 50% (wild-type 100%)
DELTA1389
autoprocessing to alpha-,beta-subunits: 100% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 40% (wild-type 100%)
E260A
autoprocessing to alpha-,beta-subunits: not determined (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 40% (wild-type 100%)
K170A
autoprocessing to alpha-,beta-subunits: 0% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 5% (wild-type 100%)
T148A
autoprocessing to alpha-,beta-subunits: 0% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 2% (wild-type: 100%)
T149A
autoprocessing to alpha-,beta-subunits: 80% (compared to wild-type 100%), acetyl transferase activity (production of ornithine from N-alpha-acetyl-L-ornithine/L-Glu): 10% (wild-type: 100%)
E280A
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change of resiude to the corresponding Escherichia coli residue. Mutation abolishes arginine inhibition and decreases synthase activity
F35C
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change of resiude to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation leads to partial inhibition of both synthase and kinase activities by arginine and decrease in synthase activity
G286P
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change of resiude to the corresponding Escherichia coli residue. Mutation abolishes arginine inhibition and decreases synthase activity
G288S
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change of resiude to the corresponding residue in an arginine-resistant Escherichia coli mutant. Mutation abolishes arginine inhibition and decreases synthase activity
additional information
additional information
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-L-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, harboring a mutated argJ-encoded enzyme, to mimic the linear pathway of L-ornithine biosynthesis. Site-directed mutagenesis of argJ and argA is carried out by overlapping PCR using the Corynebacterium crenatum argJ and Escherichia coli strain BL21(DE3) argA gene amplicons as templates. To construct recombinant expression vectors containing pDXW10-argAHY, multi-mutated argAHY is generated using overlapping PCR. The successful introduction of desired mutations is confirmed by DNA sequencing, and the desired sequences ligated into pDXW10 are then transformed into Escherichia coli strain BL21(DE3) for expression. The recombinant plasmids are transformed into Corynebacterium crenatum using the electroporation method
additional information
-
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-L-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, harboring a mutated argJ-encoded enzyme, to mimic the linear pathway of L-ornithine biosynthesis. Site-directed mutagenesis of argJ and argA is carried out by overlapping PCR using the Corynebacterium crenatum argJ and Escherichia coli strain BL21(DE3) argA gene amplicons as templates. To construct recombinant expression vectors containing pDXW10-argAHY, multi-mutated argAHY is generated using overlapping PCR. The successful introduction of desired mutations is confirmed by DNA sequencing, and the desired sequences ligated into pDXW10 are then transformed into Escherichia coli strain BL21(DE3) for expression. The recombinant plasmids are transformed into Corynebacterium crenatum using the electroporation method
additional information
-
the genes argA from Escherichia coli and argE from Serratia marcescens, encoding the enzymes N-acetyl glutamate synthase and N-acetyl-L-ornithine deacetylase, respectively, are introduced into Corynebacterium crenatum, harboring a mutated argJ-encoded enzyme, to mimic the linear pathway of L-ornithine biosynthesis. Site-directed mutagenesis of argJ and argA is carried out by overlapping PCR using the Corynebacterium crenatum argJ and Escherichia coli strain BL21(DE3) argA gene amplicons as templates. To construct recombinant expression vectors containing pDXW10-argAHY, multi-mutated argAHY is generated using overlapping PCR. The successful introduction of desired mutations is confirmed by DNA sequencing, and the desired sequences ligated into pDXW10 are then transformed into Escherichia coli strain BL21(DE3) for expression. The recombinant plasmids are transformed into Corynebacterium crenatum using the electroporation method
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additional information
inactivation of regulatory repressor argR gene and overexpression of argJ gene, argJ overexpression leads to decreased ornithine acetyltransferase activity due to product inhibition by L-ornithine
additional information
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inactivation of regulatory repressor argR gene and overexpression of argJ gene, argJ overexpression leads to decreased ornithine acetyltransferase activity due to product inhibition by L-ornithine
additional information
L-citrulline overproduction in Corynebacterium glutamicum engineered strain correlates with expression levels of ArgJ, which plays a vital role in the L-citrulline biosynthesis
additional information
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L-citrulline overproduction in Corynebacterium glutamicum engineered strain correlates with expression levels of ArgJ, which plays a vital role in the L-citrulline biosynthesis
additional information
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
additional information
-
inactivation of regulatory repressor argR gene and overexpression of argJ gene, argJ overexpression leads to decreased ornithine acetyltransferase activity due to product inhibition by L-ornithine
-
additional information
-
L-citrulline overproduction in Corynebacterium glutamicum engineered strain correlates with expression levels of ArgJ, which plays a vital role in the L-citrulline biosynthesis
-
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
-
additional information
-
to enhance L-ornithine production, the argJ gene from Corynebacterium glutamicum strain ATCC 13032 is overexpressed. In flask cultures, the resulting strain, Corynebacterium glutamicum strain 1006DELTAargR-argJ, produces 31.6 g/l L-ornithine, which is 54.15% more than that produced by wild-type strain 1006. The OAT activity of mutant strain 1006DELTAargR-argJ is significantly greater than that of wild-type strain 1006
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