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
1.2.1.41
-
RECOMMENDED NAME
GeneOntology No.
glutamate-5-semialdehyde dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamate 5-semialdehyde + phosphate + NADP+ = L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidation
Q941T1
-
oxidation
B1P5P4
-
oxidation
B1P5P5, B1P5P6
;
oxidation
B1P5P3
-
oxidation
B1P5P7, B1P5P8
;
redox reaction
-
-
-
-
reduction
-
-
-
-
reduction
B1P5P4
-
reduction
B1P5P5, B1P5P6
;
reduction
B1P5P3
-
reduction
B1P5P7, B1P5P8
;
PATHWAY
KEGG Link
MetaCyc Link
Arginine and proline metabolism
-
citrulline biosynthesis
-
Metabolic pathways
-
ornithine de novo biosynthesis
-
proline biosynthesis I
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Aldh18a1
-
-
Aldh18a1
Q9Z110
isozyme
beta-glutamylphosphate reductase
-
-
-
-
dehydrogenase, glutamate semialdehyde
-
-
-
-
gamma glutamyl semialdehyde dehydrogenase
-
-
gamma-glutamyl phosphate reductase
-
-
-
-
gamma-glutamyl phosphate reductase
-
-
gamma-glutamyl phosphate reductase
B1P5P4
-
gamma-glutamyl phosphate reductase
B1P5P5, B1P5P6
-
gamma-glutamyl phosphate reductase
B1P5P3
-
gamma-glutamyl phosphate reductase
-
-
gamma-glutamyl phosphate reductase
B1P5P7, B1P5P8
-
gamma-GPR
-
-
gamma-GPR
B1P5P4
-
gamma-GPR
B1P5P5, B1P5P6
-
gamma-GPR
B1P5P3
-
gamma-GPR
B1P5P7, B1P5P8
-
glutamate 5-semialdehyde dehydrogenase
Q941T1
-
glutamate semialdehyde dehydrogenase
-
-
-
-
Glutamate-5-semialdehyde dehydrogenase
-
-
-
-
Glutamate-5-semialdehyde dehydrogenase
-
-
Glutamate-5-semialdehyde dehydrogenase
-
-
glutamate-gamma-semialdehyde dehydrogenase
-
-
-
-
glutamic gamma-semialdehyde dehydrogenase
-
-
-
-
glutamic-gamma-semialdehyde dehydrogenase
B1P5P4
-
glutamic-gamma-semialdehyde dehydrogenase
B1P5P5, B1P5P6
-
glutamic-gamma-semialdehyde dehydrogenase
B1P5P3
-
glutamic-gamma-semialdehyde dehydrogenase
B1P5P7, B1P5P8
-
Glutamyl-gamma-semialdehyde dehydrogenase
-
-
-
-
GPR
-
-
-
-
GSA dehydrogenase
-
-
-
-
OsALDH18-1
Q941T1
-
P5CS
B1P5P4
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
P5CS
B1P5P5, B1P5P6
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
P5CS
B1P5P3
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
P5CS
B1P5P7, B1P5P8
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline 5-carboxylate dehydrogenase
-
-
pyrroline-5-carboxylate synthase
B1P5P4
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthase
B1P5P5, B1P5P6
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthase
B1P5P3
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthase
B1P5P7, B1P5P8
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthetase
B1P5P4
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthetase
B1P5P5, B1P5P6
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthetase
B1P5P3
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
pyrroline-5-carboxylate synthetase
B1P5P7, B1P5P8
bifunctional enzyme, encompasses the gamma-glutamyl kinase and the glutamic-gamma-semialdehyde dehydrogenase activities
reductase, gamma-glutamyl phosphate
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
54596-29-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain TGH9011
-
-
Manually annotated by BRENDA team
Campylobacter jejuni TGH9011
strain TGH9011
-
-
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
strain 55-I
-
-
Manually annotated by BRENDA team
various strains
-
-
Manually annotated by BRENDA team
Escherichia coli 55-I
strain 55-I
-
-
Manually annotated by BRENDA team
Escherichia coli K12
K12
-
-
Manually annotated by BRENDA team
strain DSMZ 2266T
UniProt
Manually annotated by BRENDA team
fragment
SwissProt
Manually annotated by BRENDA team
tomato, var. Ailsa Craig
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
Q9Z110
-
-
-
?
glutamate gamma-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
show the reaction diagram
-
-
-
-
?
L-5-glutamyl phosphate + NADPH
?
show the reaction diagram
-
second enzyme in pathway of proline biosynthesis
-
-
-
L-5-glutamyl phosphate + NADPH
?
show the reaction diagram
-
gamma-glutamyl kinase (the first enzyme of proline biosynthetic pathway) and gamma-glutamyl phosphate reductase (second enzyme) form a complex which stabilizes the labile intermediate i.e. gamma-glutamyl phosphate
-
-
-
L-5-glutamyl phosphate + NADPH
?
show the reaction diagram
Escherichia coli K12
-
second enzyme in pathway of proline biosynthesis
-
-
-
L-glutamate 5-semialdehyde + phosphate + NAD+
L-glutamyl 5-phosphate + NADH + H+
show the reaction diagram
-
-
-
-
?
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
show the reaction diagram
-
-
-
-
-
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
show the reaction diagram
-
-
-
-
r
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
show the reaction diagram
-
L-glutamate 5-semialdehyde spontaneously cyclizes to delta-1-pyrroline-5-carboxylic acid
-
-
-
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
show the reaction diagram
-
arsenate can replace phosphate
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
show the reaction diagram
-
divalent anions can substitute for phosphate, L-glutamate 5-semialdehyde is in equilibrium with delta'-pyrroline-5-carboxylate
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
show the reaction diagram
Escherichia coli 55-I
-
arsenate can replace phosphate
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH
show the reaction diagram
Escherichia coli K12
-
-
-
-
-
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
B1P5P4
-
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
B1P5P5, B1P5P6
-
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
B1P5P3
-
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
B1P5P7, B1P5P8
-
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-5-glutamyl phosphate + NADPH + H+
show the reaction diagram
A7Y114, -
-
-
-
?
additional information
?
-
Q941T1
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-5-glutamyl phosphate + NADPH
?
show the reaction diagram
-
second enzyme in pathway of proline biosynthesis
-
-
-
L-5-glutamyl phosphate + NADPH
?
show the reaction diagram
-
gamma-glutamyl kinase (the first enzyme of proline biosynthetic pathway) and gamma-glutamyl phosphate reductase (second enzyme) form a complex which stabilizes the labile intermediate i.e. gamma-glutamyl phosphate
-
-
-
L-5-glutamyl phosphate + NADPH
?
show the reaction diagram
Escherichia coli K12
-
second enzyme in pathway of proline biosynthesis
-
-
-
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
-
-
-
-
?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
B1P5P4
-
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
B1P5P5, B1P5P6
-
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
B1P5P3
-
-
-
r
L-glutamate 5-semialdehyde + phosphate + NADP+
L-glutamyl 5-phosphate + NADPH + H+
show the reaction diagram
B1P5P7, B1P5P8
-
-
-
r
additional information
?
-
Q941T1
ALDH superfamily represents a group of enzymes that catalyze the oxidation of endogenous and exogenous aldehydes to the corresponding carboxylic acids
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD+
-
required
NAD+
Q9Z110
-
NAD+
-
the work based on a computer simulation using a PDB data set of Thermus thermophilus GGSALDH, pdb2BJA, in this structure the enzyme is co-crystallized with NADH
NAD+
Q941T1
-
NADH
-
less active than NADPH
NADP+
Q941T1
-
NADP+
B1P5P5, B1P5P6
;
NADP+
B1P5P7, B1P5P8
;
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
highest enzyme activity at 15-20 mM
additional information
A7Y114, -
expression of the proA gene is salinity-dependent and reaches a maximum at 2.5 M NaCl
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3-(Phosphonoacetylamido)-L-alanine
-
competitive with respect to DL-pyrroline-5-carboxylic acid, non-competitive with respect to NADP+ and phosphate
Ba2+
-
50% inhibition at 1 mM
Co2+
-
50% inhibition at 2.5 mM
Cu2+
-
75% inhibition at 0.1 mM
Disulfiram
-
0.01 mM
iodoacetamide
-
40% inhibition at 1 mM
iodoacetate
-
15% inhibition at 1 mM
L-proline
-
25% inhibition at 50 mM
L-proline
-
50% inhibition at 0.07 mM
NADPH
-
competitive with respect to all three substrates
Ni2+
-
100% inhibition at 0.1 mM
p-chloromercuribenzoate
-
100% inhibition at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
phosphate
-
100 mM
additional information
A7Y114, -
cellular mRNA levels are increased up to 90fold in the presence of glutamate. A minimal concentration of 0.2 M glutamate already stimulates proA gene expression
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.5
-
DL-pyrroline-5-carboxylic acid
-
-
0.05
-
NADP+
-
-
0.18
-
NADP+
-
-
0.19
-
NADP+
-
-
0.35
-
phosphate
-
-
11
-
phosphate
-
-
11.3
-
phosphate
-
-
1.8
-
pyrroline-5-carboxylic acid
-
-
2.2
-
glutamic gamma-semialdehyde
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km with various phosphate substitutes
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
22.5
-
3-(Phosphonoacetylamido)-L-alanine
-
-
0.002
-
NADPH
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0072
-
-
crude extract
0.55
-
-
at 55-65C
13.84
-
-
-
additional information
-
-
relative specific activities of different strains
additional information
-
-
specific activity as a function of cultivation temperature
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.2
-
-
activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8.5
-
pH 6.0 and pH 8.5: about 20% of activity maximum
6.3
7.8
-
about 30% of activity maximum at pH 7.3, about 20% of activity maximum at pH 7.8
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
activity assay, room temperature
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
41500
-
-
SDS-PAGE
41980
-
-
calculated from DNA sequence
43500
-
-
calculated from DNA sequence
46000
-
-
SDS-PAGE
47000
-
-
SDS-PAGE, monomeric form
60000
-
-
Western blot analysis with antibody against Escherichia coli enzyme
79500
-
Q941T1
-
189000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexamer
-
6 * 41500
hexamer
-
composed by dimers
hexamer
Escherichia coli K12
-
6 * 41500
-
tetramer
-
4 * 47000, SDS-PAGE
tetramer
Q9WYC9
dimer of dimers, crystallization data
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme expresssed in Escherichia coli, at 2 A resolution
Q9WYC9
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9
-
stable for at least 10 min
7
-
-
long periods
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
-
-
unstable above
50
-
-
rapidly inactivated above, pH 7.0, 30 min, stable below
80
-
-
loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
30-40% loss of activity by freezing and thawing
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 6 months
-
-70C, 10% glycerol
-
0-2C, 2 months
-
-70C, one week
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
homogeneity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
into the pGEM-TEasy plasmid for sequencing
B1P5P4
into the pGEM-TEasy plasmid for sequencing; into the pGEM-TEasy plasmid for sequencing
B1P5P5, B1P5P6
artificial bifunctional enzyme, fusion of the genes proA and proB, resulting in enhanced intracellular concentrations of proline
-
into the pGEM-T easy vector for sequencing
Q941T1
into the pCR2.1 TOPO TA vector for sequencing
B1P5P3
into the pCR2.1 TOPO TA vector for sequencing; into the pCR2.1 TOPO TA vector for sequencing
B1P5P7, B1P5P8
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
in humans a natural S352L mutation gives rise to type II hyperprolinemia, mental retardation
additional information
A7Y114, -
the genes proH encoding pyrroline-5-carboxylate reductase, proJ encoding glutamate-5-kinase, and proA encoding glutamate-5-semialdehyde dehydrogenase form a transcriptional unit. This pro operon is involved in salinity-induced proline biosynthesis