Information on EC 1.2.1.41 - glutamate-5-semialdehyde dehydrogenase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
1.2.1.41
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RECOMMENDED NAME
GeneOntology No.
glutamate-5-semialdehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
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-
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reduction
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Arginine and proline metabolism
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arginine metabolism
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Biosynthesis of antibiotics
-
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Biosynthesis of secondary metabolites
-
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Carbapenem biosynthesis
-
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L-citrulline biosynthesis
-
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L-Ndelta-acetylornithine biosynthesis
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L-ornithine biosynthesis II
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L-proline biosynthesis I
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L-proline biosynthesis III
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Metabolic pathways
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proline metabolism
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)
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CAS REGISTRY NUMBER
COMMENTARY hide
54596-29-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain TGH9011
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-
Manually annotated by BRENDA team
strain TGH9011
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-
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
strain 55-I
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-
Manually annotated by BRENDA team
K12
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-
Manually annotated by BRENDA team
strain DSMZ 2266T
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
tomato, var. Ailsa Craig
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-
Manually annotated by BRENDA team
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Swissprot
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
-
-
?
glutamate gamma-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
show the reaction diagram
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-
-
-
?
L-5-glutamyl phosphate + NADPH
?
show the reaction diagram
L-glutamate 5-semialdehyde + phosphate + NAD+
L-glutamyl 5-phosphate + NADH + H+
show the reaction diagram
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-
-
-
?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
show the reaction diagram
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH + H+
show the reaction diagram
-
-
-
?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
additional information
?
-
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
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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
L-5-glutamyl phosphate + NADPH
?
show the reaction diagram
L-glutamate 5-semialdehyde + phosphate + NAD+
L-glutamyl 5-phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
additional information
?
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Q941T1
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
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less active than NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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highest enzyme activity at 15-20 mM
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-(Phosphonoacetylamido)-L-alanine
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competitive with respect to DL-pyrroline-5-carboxylic acid, non-competitive with respect to NADP+ and phosphate
Ba2+
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50% inhibition at 1 mM
Co2+
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50% inhibition at 2.5 mM
Cu2+
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75% inhibition at 0.1 mM
Disulfiram
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0.01 mM
iodoacetamide
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40% inhibition at 1 mM
iodoacetate
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15% inhibition at 1 mM
L-proline
NADPH
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competitive with respect to all three substrates
Ni2+
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100% inhibition at 0.1 mM
p-chloromercuribenzoate
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100% inhibition at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
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100 mM
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5
DL-pyrroline-5-carboxylic acid
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2.2
glutamic gamma-semialdehyde
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0.05 - 0.19
NADP+
0.35 - 11.3
phosphate
1.8
pyrroline-5-carboxylic acid
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-
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
22.5
3-(Phosphonoacetylamido)-L-alanine
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0.002
NADPH
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0072
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crude extract
0.55
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at 55-65C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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activity assay
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
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pH 6.0 and pH 8.5: about 20% of activity maximum
6.3 - 7.8
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about 30% of activity maximum at pH 7.3, about 20% of activity maximum at pH 7.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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activity assay, room temperature
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41500
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SDS-PAGE
41980
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calculated from DNA sequence
43500
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calculated from DNA sequence
46000
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SDS-PAGE
47000
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SDS-PAGE, monomeric form
60000
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Western blot analysis with antibody against Escherichia coli enzyme
189000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme expresssed in Escherichia coli, at 2 A resolution
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 9
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stable for at least 10 min
390308
7
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long periods
390308
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
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unstable above
50
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rapidly inactivated above, pH 7.0, 30 min, stable below
80
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loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
30-40% loss of activity by freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 6 months
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-70C, 10% glycerol
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-70C, one week
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0-2C, 2 months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
homogeneity
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a fusion of the proA and proB gene of Bacillus subtilis, coding for gamma-glutamyl kinase and gamma-glutamyl phosphate reductase, are cloned for expression of an an artifical bifunctional enzyme in Escherichia coli JM83
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artificial bifunctional enzyme, fusion of the genes proA and proB, resulting in enhanced intracellular concentrations of proline
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into the pCR2.1 TOPO TA vector for sequencing
into the pCR2.1 TOPO TA vector for sequencing; into the pCR2.1 TOPO TA vector for sequencing
into the pGEM-T easy vector for sequencing
into the pGEM-TEasy plasmid for sequencing
into the pGEM-TEasy plasmid for sequencing; into the pGEM-TEasy plasmid for sequencing
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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in humans a natural S352L mutation gives rise to type II hyperprolinemia, mental retardation
additional information
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