Information on EC 1.2.1.88 - L-glutamate gamma-semialdehyde dehydrogenase

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

EC NUMBER
COMMENTARY hide
1.2.1.88
-
RECOMMENDED NAME
GeneOntology No.
L-glutamate gamma-semialdehyde dehydrogenase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
ethylene biosynthesis II (microbes)
-
-
L-arginine degradation I (arginase pathway)
-
-
L-proline degradation
-
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proline metabolism
-
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Alanine, aspartate and glutamate metabolism
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Arginine and proline metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate gamma-semialdehyde:NAD+ oxidoreductase
This enzyme catalyses the irreversible oxidation of glutamate-gamma-semialdehyde to glutamate as part of the proline degradation pathway. (S)-1-pyrroline-5-carboxylate, the product of the first enzyme of the pathway (EC 1.5.5.2, proline dehydrogenase) is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde. In many bacterial species, both activities are carried out by a single bifunctional enzyme [3,4].The enzyme can also oxidize other 1-pyrrolines, e.g. 3-hydroxy-1-pyrroline-5-carboxylate is converted into 4-hydroxyglutamate and (R)-1-pyrroline-5-carboxylate is converted into D-glutamate. NADP+ can also act as acceptor, but with lower activity [5].
CAS REGISTRY NUMBER
COMMENTARY hide
9054-82-4
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
strain DSM 406
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
strains IFO 12983, ATCC 8005 and ATCC 21365
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-
Manually annotated by BRENDA team
strains ATCC 39492 and DSM 465
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-
Manually annotated by BRENDA team
camel tick; two isoforms A and B
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-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
glutamate auxotroph
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-
Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain A3(2)
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-
Manually annotated by BRENDA team
strain A3(2)
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-pyrroline-5-carboxylate + NAD(P)+ + H2O
L-glutamate + NAD(P)H
show the reaction diagram
-
-
-
-
?
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
show the reaction diagram
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH + H+
show the reaction diagram
1-pyrroline-5-carboxylate + NADH + H+
L-proline + NAD+
show the reaction diagram
-
-
-
?
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH
show the reaction diagram
-
-
-
-
?
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
show the reaction diagram
-
NAD+ is preferred over NADP+
-
-
ir
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
show the reaction diagram
-
as active as 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
4-methoxybenzaldehyde + NAD+ + H2O
4-methoxybenzoate + NADH + H+
show the reaction diagram
-
as active as 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
4-nitrobenzaldehyde + NAD+ + H2O
4-nitrobenzoate + NADH + H+
show the reaction diagram
-
as active as 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
acetaldehyde + NAD+ + H2O
acetate + NADH + H+
show the reaction diagram
-
41% activity compared to 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
benzaldehyde + NAD+ + H2O
benzoate + NADH + H+
show the reaction diagram
-
2fold higher activity than with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
-
-
?
D-glucose + NAD+ + H2O
D-gluconate + NADH
show the reaction diagram
-
80% of the activity with 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
DELTA1-pyrroline-3-hydroxy-5-carboxylate + NAD+ + H2O
4-hydroxyglutamate + NADH
show the reaction diagram
formaldehyde + NAD+ + H2O
formate + NADH
show the reaction diagram
-
50% of activity with 1-pyrroline-5-carboxylate, isoform A, only slight activity with isoform B
-
-
?
glyceralaldehyde-3-phosphate + NAD+ + H2O
glycerate-3-phosphate + NADH
show the reaction diagram
-
slight activity with isoforms A and B
-
-
?
glyoxylic acid + NAD+ + H2O
oxalic acid + NADH
show the reaction diagram
-
41% activity of that with 1-pyrroline-5-carboxylate with isoform A, no activity with isoform B
-
-
?
indole-3-acetaldehyde + NAD+ + H2O
indole-3-acetate + NADH + H+
show the reaction diagram
-
66% activity of that with 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
-
-
?
indole-3-phosphate + NAD+ + H2O
?
show the reaction diagram
-
slight activity with isoforms A and B
-
-
?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
show the reaction diagram
L-glutamate 5-semialdehyde + NADP+ + H2O
L-glutamate + NADPH + H+
show the reaction diagram
succinate semialdehyde + NAD+ + H2O
succinate + NADH + H+
show the reaction diagram
-
-
-
?
additional information
?
-
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
1-pyrroline-5-carboxylate + NAD+ + H2O
L-glutamate + NADH
show the reaction diagram
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
show the reaction diagram
P09546
the bifunctional enzyme catalyzes the oxidation of proline in two steps. (S)-1-Pyrroline-5-carboxylate, the product of the first reaction is in spontaneous equilibrium with its tautomer L-glutamate gamma-semialdehyde: (1) L-proline + acceptor = (S)-1-pyrroline-5-carboxylate + reduced acceptor, (2) L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH + H+
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
flavin cofactor, 1.2fold stimulated by exogenous FAD
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-aminopentanoate
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4,5-Dehydro-L-pipecolic acid
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baikiain, competitive
4-aminobutyrate
5-Aminopentanoate
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6-aminohexanoate
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-
arsenate
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-
arsenite
Borate
-
-
Cd2+
-
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chloride
CN-
-
-
Co2+
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both isoforms, concentration above 3 mM
DELTA1-pyrroline-2-carboxylate
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fluoride
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glyoxylate
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Hg2+
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both isoforms
imidazole
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iodoacetamide
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both isoforms
L-5-oxoproline
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-
L-Ala
L-arginine
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uncompetitive
L-Asp
L-Glu
L-glutamate
-
L-glutarate
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L-His
L-hydroxyproline
L-Ile
L-Leu
L-Ser
L-Trp
L-Val
Mn2+
-
-
N-ethylmaleimide
NADH
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product inhibition
NH2OH
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Ni2+
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both isoforms
ornithine
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inhibits only the short enzyme form
p-hydroxymercuribenzoate
piperidin-2-one
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proline
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both isoforms
succinate
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sulfate
additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-acetylglutamate
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-
additional information
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no effect of proline on activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.037 - 2
1-pyrroline-5-carboxylate
0.5
3-Methoxybenzaldehyde
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isoform A
0.25
4-methoxybenzaldehyde
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isoform A
1
acetaldehyde
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isoform A
0.5
benzaldehyde
-
isoform A
0.133
D-glucose
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isoform A
0.76
formaldehyde
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isoform A
1
glyoxylic acid
-
isoform A
0.2
indol-3-acetaldehyde
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isoform A
97
L-glutamate 5-semialdehyde
pH 7.2, 28°C
0.18 - 0.75
L-pyrroline-5-carboxylate
0.02 - 103
NAD+
0.0095 - 3
NADP+
0.27
p-nitrobenzaldehyde
-
isoform A
0.35
pyrroline-5-carboxylate
-
-
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.5 - 25
1-pyrroline-5-carboxylate
7
L-glutamate 5-semialdehyde
pH 7.2, 28°C
1.6 - 12
NAD+
0.42 - 3
NADP+
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14
1-pyrroline-5-carboxylate
pH 7.5, 20°C
0.072
L-glutamate 5-semialdehyde
pH 7.2, 28°C
0.0723 - 235
NAD+
0.342
NADP+
pH 7.2, 28°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 3.75
gamma-aminobutyrate
3.4 - 7
glutamate
0.27
glyoxylate
pH 7.0, 20°C
3.75 - 4.75
hydroxyproline
12
L-glutamate
pH 7.0, 20°C
30
L-glutarate
pH 7.0, 20°C
0.6 - 0.77
NADH
2.5 - 3
proline
58
succinate
pH 7.0, 20°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000022
Cd2+
Oryza sativa
-
pH 7.5, 35°C
0.004
Cu2+
Oryza sativa
-
pH 7.5, 35°C
0.0024
Mn2+
Oryza sativa
-
pH 7.5, 35°C
0.0015
Zn2+
Oryza sativa
-
pH 7.5, 35°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.006
-
enzyme from cerebellum
0.07
-
isoform II
0.074
-
isoform I
0.124
-
wild-type
0.13
25°C, pH 7.5, pH 7.5, L-glutamate gamma-semialdehyde dehydrogenase activity proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
0.151
-
embryo, 24 days after oviposition
0.19
-
mitochondrial fraction, with cofactor NADP+
0.223
-
larvae
0.3
-
mitochondrial fraction, with cofactor NAD+
0.55
-
-
7.1
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strain ATCC 8005
8
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strain IFO 12983
9.75
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7 - 7.7
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-
7 - 10
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broad
7.3 - 8.3
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-
7.6
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-
7.8
-
assay at
8
-
independent of buffer
8.5 - 8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
-
cofactor NAD+
5.5 - 8
-
cofactor NADP+
6 - 9.5
-
-
6.5 - 7.7
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both isoforms
7.4 - 9.4
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
cofactor NAD+
37
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assay at
45
-
cofactor NADP+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 37.5
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-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.6
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest activity
Manually annotated by BRENDA team
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not in mycelium or gill
Manually annotated by BRENDA team
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northern blot analysis
Manually annotated by BRENDA team
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northern blot analysis
Manually annotated by BRENDA team
-
northern blot analysis
Manually annotated by BRENDA team
-
short isoform
Manually annotated by BRENDA team
additional information
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
52000
-
1 * 52000, isoform B, SDS-PAGE
60500
Q0DHN6
-
62000
-
? * 62000, DNA sequence determination
66000
-
66000, SDS-PAGE
68000
-
4 * 68000, SDS-PAGE
77700
Q0DHN6
-
100000
-
gel filtration
115000
-
sucrose-glycerol density gradient sedimentation
119000
132000
-
1 * 132000, membrane bound in vivo, disc gel electrophoresis; 2 * 132000, detergent solubilized, disc gel electrophoresis
137000
2 * 137000, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, SDS-PAGE
142000
-
gel filtration
240000
-
gel filtration
259000
-
gel filtration
265000 - 305000
-
native PAGE and gel filtration
293000
gel filtration, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, sucrose density centrifugation
364600
SAXS distance distribution function calculation
649300
dynamic light scattering
714900
gel filtration
additional information
-
putA gene product, different forms by native PAGE with 2 activities: proline oxidase and 1-pyrroline-5-carboxylate dehydrogenase activity
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
? * 62000, DNA sequence determination
hexamer
monomer
multimer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
space group P21 with eight molecules in the asymmetric unit
the substrate-free form displays multiple active site conformations. Protein forms a trimer-of-dimers hexamer in solution
-
complexed with glutarate, succinate, malonate, glyoxylate, and acetate
apoenzyme and in complex with NAD+, to 1.95 and 2.17 A resolution, respectively
mutants R100A crystallizes in the same lattice as wild-type, mutant R100A/K104A/R111A crystaLLIZES IN space group P1
unligandend form and in complex with NAD+, NADPH, and with product glutamate
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
15 min, 40% loss of activity in presence of NAD+, 2% loss of activity in presence of NADP+
40
-
15 min, 75% loss of activity in presence of NAD+, 10% loss of activity in presence of NADP+
45
-
half-life 44 min
47.5
-
5 min, 50% loss of activity
50
-
half-life 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glutathione stabilizes
-
NADP+ stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, 50% loss of activity, 2 months
-
0°C, 0.2 M potsassium phosphate or 0.2 M KCl, pH 7.4, 45 days, 70-80% activity remains
-
0°C, 25 mM Hepes-KOH, pH 7.4, 0.5 mM dithiothreitol, 1 mM MgCl2, 1% polyvinyl polypyrrolidone, loss of 90% activity after 15 days
-
0°C, 70 mM Tris-HCl buffer, pH 8.2, 30% v/v glycerol, several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amino acid composition determination
-
copurification with proline oxidase
-
partial
partial, isoforms I and II
-
subcellular fractionation, isolation of mitochondria
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
into the pGEM-T easy vector for sequencing; into the pGEM-T easy vector for sequencing
Q0DHN6
prn gene cluster characterization with help of mutations and physical mapping
-
pruA gene, nucleotide sequence and deduced amino acid sequence thereof
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
6fold upregulation during the infective stages of the parasite
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E314A
-
inactive. The conserved Glu447 residue has significantly shifted in the mutant, causing NAD+ to be displaced
S352A
-
catalytic site including the oxoanion hole and residue Cys348 remain unchanged in the mutant, and the coenzyme maintains its binding position
S352L
-
inactive. The conserved Glu447 residue has significantly shifted in the mutant, causing NAD+ to be displaced
W193A
mutation disrupts hexamer formation, mutant forms a dimer
K104A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
R100A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer
R100A/K104A/R111A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, contrary to wild-type, the mutant forms a dimer
R111A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
R153A
mutation in alpha3 helix which participates in the dimer-dimer interaces. Catalytic efficiency similar to wild-type, mutant forms a hexamer
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
possible target for upleveled nitrogen usage in commercial mushroom breeding
medicine
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