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
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RECOMMENDED NAME
GeneOntology No.
L-glutamate gamma-semialdehyde dehydrogenase
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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
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-
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1-pyrroline-5-carboxylate dehydrogenase
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Alanine, aspartate and glutamate metabolism
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Arginine and proline metabolism
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ethylene biosynthesis II (microbes)
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L-arginine degradation I (arginase pathway)
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L-proline degradation
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Metabolic pathways
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proline metabolism
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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
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-
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Manually annotated by BRENDA team
strain DSM 406
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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UniProt
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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-
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Manually annotated by BRENDA team
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-
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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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-
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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one of three key regulatory enzyme of intestinal citrulline synthesis
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
-
-
-
-
ir
1-pyrroline-5-carboxylate + NADP+ + H2O
L-glutamate + NADPH + H+
show the reaction diagram
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NAD+ is preferred over NADP+
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-
ir
3-methoxybenzaldehyde + NAD+ + H2O
3-methoxybenzoate + NADH
show the reaction diagram
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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
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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
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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
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slight activity with isoforms A and B
-
-
?
glyoxylic acid + NAD+ + H2O
oxalic acid + NADH
show the reaction diagram
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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
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66% activity of that with 1-pyrroline-5-carboxylate with isoform A, only slight activity with isoform B
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-
?
indole-3-phosphate + NAD+ + H2O
?
show the reaction diagram
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slight activity with isoforms A and B
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-
?
L-glutamate 5-semialdehyde + NAD+ + H2O
L-glutamate + NADH + H+
show the reaction diagram
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+
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?
additional information
?
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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
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+
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-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
flavin cofactor, 1.2fold stimulated by exogenous FAD
NADP+
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
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chloride
CN-
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Co2+
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both isoforms, concentration above 3 mM
Cu2+
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DELTA1-pyrroline-2-carboxylate
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fluoride
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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-Asp
L-Glu
L-His
L-hydroxyproline
L-Ile
L-Leu
L-Ser
L-Trp
L-Val
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
sulfate
Zn2+
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both isoforms
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 - 1.22
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
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isoform A
0.133
D-glucose
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isoform A
0.76
formaldehyde
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isoform A
1
glyoxylic acid
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isoform A
0.2
indol-3-acetaldehyde
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isoform A
0.18 - 0.75
L-pyrroline-5-carboxylate
0.02 - 2.3
NAD+
0.0095 - 1
NADP+
0.27
p-nitrobenzaldehyde
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isoform A
0.35
pyrroline-5-carboxylate
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-
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.6 - 25
1-pyrroline-5-carboxylate
1.6
NAD+
Thermus thermophilus
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pH 7.4, 50C
0.42
NADP+
Thermus thermophilus
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pH 7.4, 50C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 3.75
gamma-aminobutyrate
3.4 - 7
glutamate
3.75 - 4.75
hydroxyproline
0.6 - 0.77
NADH
2.5 - 3
proline
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.006
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enzyme from cerebellum
0.07
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isoform II
0.074
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isoform I
0.124
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wild-type
0.13
25C, pH 7.5, pH 7.5, L-glutamate gamma-semialdehyde dehydrogenase activity proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase
0.151
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embryo, 24 days after oviposition
0.19
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mitochondrial fraction, with cofactor NADP+
0.223
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larvae
0.3
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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
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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
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assay at
8
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independent of buffer
8.5 - 8.6
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
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cofactor NAD+
5.5 - 8
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cofactor NADP+
6 - 9.5
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-
6.5 - 7.7
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both isoforms
7.4 - 9.4
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
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cofactor NAD+
37
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assay at
45
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cofactor NADP+
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15 - 37.5
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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highest activity
Manually annotated by BRENDA team
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not in mycelium or gill
Manually annotated by BRENDA team
northern blot analysis
Manually annotated by BRENDA team
northern blot analysis
Manually annotated by BRENDA team
northern blot analysis
Manually annotated by BRENDA team
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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
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
265000 - 305000
-
native PAGE and gel filtration
293000
gel filtration, bifunctional enzyme: proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase, sucrose density centrifugation
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
-
consisting of three dimers, crystallization data
monomer
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
unligandend form and in complex with NAD+, NADPH, and with product glutamate
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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
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half-life 44 min
50
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half-life 30 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glutathione stabilizes
-
NADP+ stabilizes
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, 50% loss of activity, 2 months
-
0C, 0.2 M potsassium phosphate or 0.2 M KCl, pH 7.4, 45 days, 70-80% activity remains
-
0C, 25 mM Hepes-KOH, pH 7.4, 0.5 mM dithiothreitol, 1 mM MgCl2, 1% polyvinyl polypyrrolidone, loss of 90% activity after 15 days
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0C, 70 mM Tris-HCl buffer, pH 8.2, 30% v/v glycerol, several weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
amino acid composition determination
-
copurification with proline oxidase
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partial
partial, isoforms I and II
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subcellular fractionation, isolation of mitochondria
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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possible target for upleveled nitrogen usage in commercial mushroom breeding
medicine
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