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Information on EC 1.2.1.38 - N-acetyl-gamma-glutamyl-phosphate reductase
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1.2.1.38 N-acetyl-gamma-glutamyl-phosphate reductaseSpecify your search results
Word Map
- 1.2.1.38
- urea
- crassa
-
vapour-diffusion
- neurospora
-
nadph-dependent
-
sitting-drop
-
hyperammonemia
-
polyprotein
-
disease-causing
- sativa
- nicotinamide
- ornithine
- carbamylphosphate
- rice
-
hexagonal
- tuberculosis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
n-acetyl-gamma-glutamyl-phosphate reductase, nagsd, n-acetylglutamate 5-semialdehyde dehydrogenase, n-acetylglutamate 5-phosphate reductase, agpreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AGPR
N-acetyl-gamma-glutamyl-phosphate reductase
N-acetylglutamate 5-semialdehyde dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
N-acetyl-L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)
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CAS REGISTRY NUMBER
COMMENTARY
37251-00-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
-
r
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
-
-
-
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
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
?, r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
enzyme of arginine biosynthesis
-
?, r
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (31964 entries)
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Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, several weeks, pH 7.0, 0.1 M phosphate, 1.0 mM 2-mercaptoethanol, 0.1 mM EDTA
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligated into pET15b vector. Overexpressed as N-terminal His6 tag in Escherichia coli BL21 (DE3) cells carrying pLysS
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
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
Microbiology
144
479-492
1998
Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
brenda
Parra-Gessert, L.; Koo, K.; Fajardo, J.; Weiss, R.L.
Processing and function of a polyprotein of two mitochondrial proteins in Neurospora crassa
J. Biol. Chem.
273
7972-7980
1998
Neurospora crassa
brenda
Abadjieva, A.; Pauwels, K.; Hilven, P.; Crabeel, M.
A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis. Acetylglutamate synthase activity requires complex formation with acetylglutamate kinase
J. Biol. Chem.
276
42869-42880
2001
Saccharomyces cerevisiae
brenda
Goto, M.; Agari, Y.; Omi, R.; Miyahara, I.; Hirotsu, K.
Expression, purification and preliminary X-ray characterization of N-acetyl-gamma-glutamyl-phosphate reductase from Thermus thermophilus HB8
Acta Crystallogr. Sect. D
59
356-358
2003
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Takahara, K.; Akashi, K.; Yokota, A.
Continuous spectrophotometric assays for three regulatory enzymes of the arginine biosynthetic pathway
Anal. Biochem.
368
138-147
2007
Escherichia coli (P11446), Escherichia coli
brenda
Cherney, L.T.; Cherney, M.M.; Garen, C.R.; Niu, C.; Moradian, F.; James, M.N.
Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase from Mycobacterium tuberculosis in complex with NADP(+)
J. Mol. Biol.
367
1357-1369
2007
Mycobacterium tuberculosis (P9WPZ9), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WPZ9)
brenda
Nishida, H.; Nishiyama, M.; Kobashi, N.; Kosuge, T.; Hoshino, T.; Yamane, H.
A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway a key to the evolution of amino acid biosynthesis
Genome Res.
9
1175-1183
1999
Thermus thermophilus
brenda
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