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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
nagsd, n-acetyl-gamma-glutamyl-phosphate reductase, n-acetyl-gamma-glutamyl phosphate reductase, n-acetylglutamate 5-semialdehyde dehydrogenase, n-acetylglutamate 5-phosphate reductase, agpreductase,
more
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lysY
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gene name, formerly named argC
N-acetyl-gamma-glutamyl phosphate reductase
N-acetyl-gamma-glutamyl-phosphate reductase
N-acetyl-glutamate semialdehyde dehydrogenase
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N-acetyl-L-glutamate gamma-semialdehyde:NADP oxidoreductase (phosphorylating)
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N-acetylglutamate 5-phosphate reductase
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N-acetylglutamate 5-semialdehyde dehydrogenase
N-acetylglutamic gamma-semialdehyde dehydrogenase
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NAGSA dehydrogenase
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reductase, acetyl-gamma-glutamyl phosphate
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AGPR
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argC
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N-acetyl-gamma-glutamyl phosphate reductase
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N-acetyl-gamma-glutamyl phosphate reductase
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N-acetyl-gamma-glutamyl-phosphate reductase
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N-acetyl-gamma-glutamyl-phosphate reductase
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N-acetylglutamate 5-semialdehyde dehydrogenase
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N-acetylglutamate 5-semialdehyde dehydrogenase
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
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N-acetyl-L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)
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N-acetyl-5-glutamyl phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
substrate produced by AGK
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N-acetyl-5-glutamyl phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
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N-acetyl-5-glutamyl phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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in the dehydrogenase reaction, arsenate can substitute for phosphate
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r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
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N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
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N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
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r
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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enzyme of arginine biosynthesis
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?, r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
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N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
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N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
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N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
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r
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NADP+
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NADPH
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5,5'-dithiobis(2-nitrobenzoate)
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p-hydroxymercuribenzoate
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carbamoyl-phosphate synthase (ammonia) deficiency
Understanding N-acetyl-L-glutamate Synthase Deficiency: Mutational Spectrum, Impact of Clinical Mutations on Enzyme Functionality, and Structural Considerations.
Tuberculosis
Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase from Mycobacterium tuberculosis in complex with NADP(+).
Urea Cycle Disorders, Inborn
N-Acetylglutamate Synthase Deficiency Due to a Recurrent Sequence Variant in the N-acetylglutamate Synthase Enhancer Region.
Urea Cycle Disorders, Inborn
Non-coding sequence variants define a novel regulatory element in the first intron of the N-acetylglutamate synthase gene.
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0.6
N-acetyl-L-glumate 5-semialdehyde
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additional information
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9 - 9.5
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activity drops sharply below pH 9.0 and above 9.5
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Wc2
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brenda
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UniProt
brenda
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UniProt
brenda
LA16
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brenda
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brenda
LBG H1323
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brenda
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brenda
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brenda
HB27
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brenda
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brenda
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UniProt
brenda
K-12
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brenda
W2D ATCC 25542
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brenda
Wc2
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brenda
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brenda
LA16
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brenda
wild type 74A
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brenda
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brenda
LBG H1323
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brenda
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brenda
HB27
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brenda
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low activity
brenda
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low activity
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brenda
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brenda
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soluble matrix enzyme
brenda
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brenda
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high activity
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brenda
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high activity
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brenda
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physiological function
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enzyme overproduction promotes growth delay and inefficient nodules in Medicago sativa
physiological function
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enzyme overproduction promotes growth delay and inefficient nodules in Medicago sativa
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38000
x * 38000, SDS-PAGE
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dimer
crystallography
dimer
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crystallography
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dimer
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2 * 38000-46000, SDS-PAGE
dimer
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2 * 38000-46000, SDS-PAGE
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tetramer
crystallography
tetramer
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crystallography
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AGPR apoenzyme and AGPR in complex with NADP+ crystallized by the sitting-drop method. Crystals of the apoenzyme belong to space group P212121 with four protein subunits in the asymmetric unit (a crystallographic tetramer) and to space group C2 having two protein subunits in the asymmetric unit (a crystallographic C2-dimer). Each AGPR subunit consists of alpha/beta and alpha + beta domains. NADP+ is bound in the cleft between them. Conformational change in AGPR upon NADP+ binding, a loop (Leu88 to His92) moves more than 5 A to confine sterically the cofactor's adenine moiety in a hydrophobic pocket. Residues His217 and His219 can form hydrogen bonds with the docked substrate. An ion pair can form between the substrate phosphate group and the guanidinium group of Arg114, which optimally places and orients the substrate for subsequent nucleophilic attack by Cys158 on the substrate gamma-carboxyl group
hanging-drop vapour-diffusion method using PEG 4000 as a precipitating agent, colourless prosms, with unit-cell parameters a = b = 90.0 A, c = 139.5 A. The crystals belong to the hexagonal space group P6(2)22 or P6(4)22
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5.5 - 9.5
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4°C, 5 h
390280
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gel filtration, enzyme unstable
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-15°C, several weeks, pH 7.0, 0.1 M phosphate, 1.0 mM 2-mercaptoethanol, 0.1 mM EDTA
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by His tag affinity chromatography
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expressed in Medicago sativa
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expression in Escherichia coli
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ligated into pET15b vector. Overexpressed as N-terminal His6 tag in Escherichia coli BL21 (DE3) cells carrying pLysS
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additional information
rapid, highly sensitive, and reproducible coupled enzyme assays for AGS, AGK, and GAT using recombinant Escherichia coli AGK and AGPR as coupling enzymes
additional information
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rapid, highly sensitive, and reproducible coupled enzyme assays for AGS, AGK, and GAT using recombinant Escherichia coli AGK and AGPR as coupling enzymes
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Wandinger-Ness, A.U.; Ness, S.A.; Weiss, R.L.
Simultaneous purification of three mitochondrial enzymes. Acetylglutamate kinase, acetylglutamyl-phosphate reductase and carbamoyl-phosphate synthetase from Neurospora crassa
J. Biol. Chem.
261
4820-4827
1986
Neurospora crassa
brenda
Baich, A.; Vogel, H.J.
N-acetyl-gamma-glutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: Repressible enzymes of arginine synthesis in Escherichia coli
Biochem. Biophys. Res. Commun.
7
491-496
1962
Escherichia coli, Escherichia coli Wc2
brenda
Glansdorff, N.; Sand, G.
Coordination of enzyme synthesis in the arginine pathway of Escherichia coli K-12
Biochim. Biophys. Acta
108
308-311
1965
Escherichia coli
brenda
Vogel, H.J.; McLellan, W.L.
N-Acetylglutamic gamma-semialdehyde dehydrogenase (Escherichia coli)
Methods Enzymol.
17A
255-260
1970
Escherichia coli
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brenda
Cybis, J.; Davis, R.H.
Organization and control in the arginine biosynthetic pathway of Neurospora
J. Bacteriol.
123
196-202
1975
Neurospora crassa
brenda
Wipf, B.; Leisinger, T.
Compartmentation of arginine biosynthesis in Saccharomyces cerivisiae
FEMS Microbiol. Lett.
2
239-242
1977
Saccharomyces cerevisiae, Saccharomyces cerevisiae LBG H1323
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brenda
Haas, D.; Holloway, B.W.
The genetic organization of arginine biosynthesis in Pseudomonas aeruginosa
Mol. Gen. Genet.
154
7-22
1977
Pseudomonas aeruginosa
brenda
Jauniaux, J.C.; Urrestarazu, L.A.; Wiame, J.M.
Arginine metabolism in Saccharomyces cerevisiae: subcellular localization of the enzymes
J. Bacteriol.
133
1096-1107
1978
Saccharomyces cerevisiae
brenda
Minet, M.; Jauniaux, J.C.; Thuriaux, P.; Grenson, M.; Wiame, J.M.
Organization and expression of a two-gene cluster in the arginine biosynthesis of Saccharomyces cerevisiae
Mol. Gen. Genet.
168
299-308
1979
Saccharomyces cerevisiae
brenda
Jacobs, P.; Jauniaux, J.C.
A cis-dominant regulatory mutation linked to the argB-argC gene cluster in Saccharomyces cerevisiae
J. Mol. Biol.
139
691-704
1980
Saccharomyces cerevisiae
brenda
Wandinger-Ness, A.U.; Wolf, E.C.; Weiss, R.L.; Davis, R.H.
Acetylglutamate kinase-acetylglutamyl-phosphate reductase complex of Neurospora crassa. Evidence for two polypeptides
J. Biol. Chem.
260
5974-5978
1985
Neurospora crassa, Neurospora crassa LA16
brenda
Baetens, M.; Legrain, C.; Boyen, A.; Glansdorff, N.
Genes and enzymes of the acetyl cycle of arginine biosynthesis in the extreme thermophilic bacterium Thermus thermophilus HB27