Information on EC 1.2.1.38 - N-acetyl-gamma-glutamyl-phosphate reductase

for references in articles please use BRENDA:EC1.2.1.38
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

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EC NUMBER
COMMENTARY hide
1.2.1.38
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RECOMMENDED NAME
GeneOntology No.
N-acetyl-gamma-glutamyl-phosphate reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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-
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Phosphorylation
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-
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redox reaction
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-
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reduction
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arginine biosynthesis II (acetyl cycle)
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L-arginine biosynthesis III (via N-acetyl-L-citrulline)
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L-arginine biosynthesis IV (archaebacteria)
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L-ornithine biosynthesis I
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arginine metabolism
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Arginine biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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Biosynthesis of antibiotics
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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 hide
37251-00-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Wc2
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Manually annotated by BRENDA team
LA16
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Manually annotated by BRENDA team
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
HB27
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Manually annotated by BRENDA team
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-acetyl-5-glutamyl phosphate + NADPH + H+
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
show the reaction diagram
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate
N-acetyl-5-glutamyl phosphate + NADPH
show the reaction diagram
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
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Fe2+
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slight
Mn2+
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slight
N-ethylmaleimide
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Ni2+
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slight
p-hydroxymercuribenzoate
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-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
N-acetyl-L-glumate 5-semialdehyde
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0.17
NADP+
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3
phosphate
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-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9 - 9.5
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activity drops sharply below pH 9.0 and above 9.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
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)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
38000
x * 38000, SDS-PAGE
93000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 38000, SDS-PAGE
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 hide
LITERATURE
5.5 - 9.5
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4°C, 5 h
390280
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
gel filtration, enzyme unstable
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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
by His tag affinity chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.1.38)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)