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Information on EC 1.4.1.2 - glutamate dehydrogenase and Organism(s) Bacillus subtilis and UniProt Accession P39633

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Bacillus subtilis
UNIPROT: P39633 not found.
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
glutamate dehydrogenase, gdh, glud1, hgdh1, glutamic dehydrogenase, nad-gdh, l-glutamate dehydrogenase, nad-dependent glutamate dehydrogenase, nadh-gdh, glutamic acid dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glutamate dehydrogenase
-
dehydrogenase, glutamate
-
-
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase (NAD)
-
-
-
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glutamate oxidoreductase
-
-
-
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glutamic acid dehydrogenase
-
-
-
-
glutamic dehydrogenase
-
-
-
-
L-glutamate dehydrogenase
-
-
-
-
NAD+-dependent GluDH
-
-
NAD-dependent glutamate dehydrogenase
-
-
-
-
NAD-dependent glutamic dehydrogenase
-
-
-
-
NAD-GDH
-
-
-
-
NAD-glutamate dehydrogenase
-
-
-
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NAD-linked glutamate dehydrogenase
-
-
-
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NAD-linked glutamic dehydrogenase
-
-
-
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NAD-specific glutamate dehydrogenase
-
-
-
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NAD-specific glutamic dehydrogenase
-
-
-
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NAD:glutamate oxidoreductase
-
-
-
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NADH-dependent glutamate dehydrogenase
-
-
-
-
NADH-linked glutamate dehydrogenase
-
-
-
-
Surface-associated protein PGAG1
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
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oxidation
-
-
-
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reduction
-
-
-
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reductive amination
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-
-
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NAD+ oxidoreductase (deaminating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9001-46-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxobutyrate + NADH + NH3
2-aminobutyrate + NAD+ + H2O
show the reaction diagram
faint specificity
-
-
?
2-oxoglutarate + NADH + NH3
L-glutamate + NAD+ + H2O
show the reaction diagram
-
-
-
r
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
?
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
show the reaction diagram
faint specificity
-
-
?
pyruvate + NADPH + NH3
L-alanine + NADP+ + H2O
show the reaction diagram
faint specificity
-
-
?
2-oxo-3-methylvalerate + NADPH + NH3
L-isoleucine + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
?
2-oxo-iso-caproate + NADPH + NH3
L-norleucine + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
?
2-oxo-iso-valerate + NADPH + NH3
L-leucine + NADP+ + H2O
show the reaction diagram
-
low specificity of wild-type
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
wild-type enzyme highly specific for 2-oxoglutarate
-
-
r
beta-phenylpyruvate + NADPH + NH3
L-phenylalanine + NADP+ + H2O
show the reaction diagram
-
low specificity of wild-type
-
-
?
L-glutamate + H2O + NAD+
2-oxoglutarate + NH3 + NADH + H+
show the reaction diagram
-
RocG is exclusively devoted to L-glutamate degradation rather than to its synthesis
-
-
?
oxaloacetate + NADPH + NH3
L-aspartate + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
?
p-hydroxyphenylpyruvate + NADPH + NH3
L-tyrosine + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
?
pyruvate + NADPH + NH3
L-alanine + NADP+ + H2O
show the reaction diagram
-
very low specificity of wild-type
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
does not prevent heat inactivation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.65 - 1.22
2-oxoglutarate
0.34
L-glutamate
wild-type
0.08
NAD+
wild-type
0.07 - 0.41
NADH
52.3 - 56.8
NH4+
0.65 - 100
2-oxoglutarate
0.07 - 0.095
NADH
2.27 - 4.16
oxaloacetate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
342 - 435
2-oxoglutarate
18.1
L-glutamate
wild-type
0.012 - 344
2-oxoglutarate
3.45 - 5.68
oxaloacetate
additional information
oxaloacetate
-
mutant M101S
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.012
-
2-oxoglutarate, mutant M101K
0.014
-
2-oxoglutarate, mutant K80R
0.019
-
2-oxoglutarate, mutant G82R and M101S
0.026
-
2-oxoglutarate, mutant G82K
0.21
-
on L-aspartate, mutant M101S
0.39
-
on L-aspartate, mutant G82K
440
-
2-oxoglutarate, wild-type
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
optimal for 2-oxoglutarate amination
7.7
optimal for L-glutamate deamination
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain ISW1214
Uniprot
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
270000
gel filtration
46000
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis
46553
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis
46587
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis
45000
-
SDS-PAGE
46000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
6 * 46000, SDS-PAGE, 6 * 46587, MALDI-MS, 6 * 46553, sequence analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E27F
improved thermostability as compared to wild-type
E27K
slightly improved thermostability as compared to wild-type
E27V
slightly improved thermostability as compared to wild-type
G255A
no significant thermostability
Q144C
improved thermostability as compared to wild-type
Q144D
slightly improved thermostability as compared to wild-type
Q144K
no improved thermostability as compared to wild-type
Q144R
highly improved thermostability as compared to wild-type
W100R
no significant thermostability
G82K
-
dramatically switches to increased specificity for oxaloacetate, 280fold higher than those for 2-oxoglutarate
G82R
-
specific activity not drastically altered compared to the wild-type
K80R
-
specific activity not drastically altered compared to the wild-type
M101K
-
specific activity not drastically altered compared to the wild-type
M101S
-
dramatically switches to increased specificity for oxaloacetate, 495fold higher than those for 2-oxoglutarate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
50% of its activity remains after incubation of the wild-type enzyme for 20 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogeneity, about 39fold
Ni2+ HiTrap chelating column chromatography
-
to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli MV1184
expressed in Escherichia coli BL21(DE3)/pLysS cells
-
expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
-
produktion of L-ornithine in Corynebacterium glutamicum SNK118, by deletion of genes argF, argR, and ncgl2228 to block the degradation of L-ornithine, and overexpression of NADP-dependent glyceraldehyde 3-phosphate dehydrogenases gene from Clostridium saccharobutylicum and glutamate dehydrogenase RocG. In fed-batch fermentation, L-ornithine of 88.26 g/l with productivity of 1.23 g/l/h (over 72 h) and yield of 0.414 g/g glucose are achieved by the final strain in a 10-l bioreactor
additional information
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Khan, I.H.; Kim, H.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
Altering the substrate specificity of glutamate dehydrogenase from Bacillus subtilis by site-directed mutagenesis
Biosci. Biotechnol. Biochem.
69
1802-1805
2005
Bacillus subtilis
Manually annotated by BRENDA team
Khan, M.I.; Ito, K.; Kim, H.; Ashida, H.; Ishikawa, T.; Shibata, H.; Sawa, Y.
Molecular properties and enhancement of thermostability by random mutagenesis of glutamate dehydrogenase from Bacillus subtilis
Biosci. Biotechnol. Biochem.
69
1861-1870
2005
Bacillus subtilis (P39633), Bacillus subtilis, Bacillus subtilis 168 (P39633)
Manually annotated by BRENDA team
Commichau, F.M.; Herzberg, C.; Tripal, P.; Valerius, O.; Stuelke, J.
A regulatory protein-protein interaction governs glutamate biosynthesis in Bacillus subtilis: the glutamate dehydrogenase RocG moonlights in controlling the transcription factor GltC
Mol. Microbiol.
65
642-654
2007
Bacillus subtilis
Manually annotated by BRENDA team
Dong, J.; Kan, B.; Liu, H.; Zhan, M.; Wang, S.; Xu, G.; Han, R.; Ni, Y.
CRISPR-Cpf1-assisted engineering of Corynebacterium glutamicum SNK118 for enhanced L-ornithine production by NADP-dependent glyceraldehyde-3-phosphate dehydrogenase and NADH-dependent glutamate dehydrogenase
Appl. Biochem. Biotechnol.
191
955-967
2020
Bacillus subtilis, Bacillus subtilis HB-1
Manually annotated by BRENDA team