Information on EC 1.4.1.4 - glutamate dehydrogenase (NADP+)

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

EC NUMBER
COMMENTARY
1.4.1.4
-
RECOMMENDED NAME
GeneOntology No.
glutamate dehydrogenase (NADP+)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-glutamate + H2O + NADP+ = 2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
oxidative deamination
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
reductive amination
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Alanine, aspartate and glutamate metabolism
-
Arginine and proline metabolism
-
glutamate biosynthesis III
-
Metabolic pathways
-
nitrate reduction V (assimilatory)
-
nitrate reduction VI (assimilatory)
-
Nitrogen metabolism
-
TCA cycle VI (obligate autotrophs)
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NADP+ oxidoreductase (deaminating)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dehydrogenase, glutamate (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
GDH
Cenococcum geophilum H5-3
-
-
-
GDH
Lactococcus lactis NCDO1867
-
-
-
GdhA
Klebsiella pneumoniae MK53
-
-
-
GdhA
Penicillium chrysogenum DS12975
-
-
-
GdhA
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of three (GDHA, GDHB and GDHC) forms of NADP-GDH in Pseudomonas aeruginosa strain PPD
GDHB
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of three (GDHA, GDHB and GDHC) forms of NADP-GDH in Pseudomonas aeruginosa strain PPD
GDHC
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of three (GDHA, GDHB and GDHC) forms of NADP-GDH in Pseudomonas aeruginosa strain PPD
GDHI
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of two (GDHI and GDHII) forms of NADP-GDH in Pseudomonas aeruginosa strain PP4
GDHI
Pseudomonas aeruginosa PP4
-
-
-
GDHI'
Acinetobacter lwoffii ISP4
-
-
-
GDHII
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of two (GDHI and GDHII) forms of NADP-GDH in Pseudomonas aeruginosa strain PP4
GDHP
-
activity staining, inhibition and thermal stability studies indicate the carbon source-dependent presence of one GDHP form of NADP-GDH in Acinetobacter lwoffii strain ISP4
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
Klebsiella pneumoniae MK53
-
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
Lactococcus lactis NCDO1867
-
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
-
-
glutamate dehydrogenase
C6EVR5
-
glutamate dehydrogenase 1
Q8ILT0
-
glutamate dehydrogenase 2
Q8ILF7
-
glutamic acid dehydrogenase
-
-
-
-
glutamic dehydrogenase
-
-
-
-
hGDH
-
-
L-glutamate dehydrogenase
-
-
-
-
L-glutamate dehydrogenase
A3MWK6
-
L-glutamate dehydrogenase
A3MWK6
-
-
NAD(P)H-dependent glutamate dehydrogenase
-
-
-
-
NADP(H)-dependent glutamate dehydrogenase
-
-
NADP(H)-GDH
-
-
NADP+ - dependant-glutamate dehydrogenase
A0R3E3
-
NADP+-dependent GDH
-
-
NADP+-dependent GDH
P00370
-
NADP+-dependent GDH
-
-
NADP+-dependent GDH
-
-
-
NADP+-dependent glutamate dehydrogenase
-
-
NADP+-dependent glutamate dehydrogenase
-
-
-
NADP+-Gdh
Kluyveromyces marxianus CBS6556
-
-
-
NADP+-Gdh
A0R3E3
-
NADP-dependent glutamate dehydrogenase
-
-
NADP-dependent glutamate dehydrogenase
Cenococcum geophilum H5-3
-
-
-
NADP-dependent glutamate dehydrogenase
-
-
NADP-dependent glutamate dehydrogenase
-
-
NADP-dependent glutamate dehydrogenase
-
-
NADP-dependent glutamate dehydrogenases
-
2 isoenzymes: a yeast-form isoenzyme and a mycelium-form isoenzyme
NADP-GDH
-
-
-
-
NADP-GDH
Acinetobacter lwoffii ISP4
-
-
-
NADP-GDH
Aspergillus awamori NCIM 1225
-
-
-
NADP-GDH
Aspergillus niger NCIM 565
-
-
-
NADP-GDH
-
-
NADP-GDH
Aspergillus oryzae NCIM 553
-
-
-
NADP-GDH
Aspergillus terreus NCIM 656
-
-
-
NADP-GDH
Cenococcum geophilum H5-3
-
-
-
NADP-GDH
Debaryomyces hansenii Y7426
-
-
-
NADP-GDH
Emericella nidulans NCIM 1211
-
-
-
NADP-GDH
P28724
-
NADP-GDH
Q2WCS9
-
NADP-GDH
Lactobacillus plantarum DPPMA49
Q2WCS9
-
-
NADP-GDH
Pseudomonas aeruginosa PP4
-
-
-
NADP-GDH
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
Aspergillus awamori NCIM 1225
-
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
Aspergillus niger NCIM 565
-
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
Aspergillus oryzae NCIM 553
-
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
Aspergillus terreus NCIM 656
-
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
Debaryomyces hansenii Y7426
-
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
Emericella nidulans NCIM 1211
-
-
-
NADP-glutamate dehydrogenase
Q2WCS9
-
NADP-glutamate dehydrogenase
Lactobacillus plantarum DPPMA49
Q2WCS9
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
-
-
NADP-glutamate dehydrogenase
-
two isoenzymes: Gdh3P and Gdh1p
NADP-linked glutamate dehydrogenase
-
-
NADP-linked glutamate dehydrogenase
Cenococcum geophilum H5-3
-
-
-
NADP-specific glutamate dehydrogenase
-
-
NADP-specific L-glutamate dehydrogenase
-
-
NADPH-dependent glutamate dehydrogenase
-
-
NADPH-dependent glutamate dehydrogenase
Penicillium chrysogenum DS12975
-
-
-
OsGDH4
-
-
Pcal_1606
A3MWK6
gene name
Pcal_1606
A3MWK6
gene name
-
CAS REGISTRY NUMBER
COMMENTARY
9029-11-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
NADPH-GDH isozymes GDHI, GDHII, and GDHI'
-
-
Manually annotated by BRENDA team
strain ISP4, when grown on isophthalate, Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD show activity of NADP-dependent GDH, while cells grown on glucose, 2fold yeast extract-tryptone broth (2YT) or glutamate show activities of both NAD-dependent GDH and NADP-GDH
-
-
Manually annotated by BRENDA team
Acinetobacter lwoffii ISP4
NADPH-GDH isozymes GDHI, GDHII, and GDHI'
-
-
Manually annotated by BRENDA team
strain JCM 9820
-
-
Manually annotated by BRENDA team
Aeropyrum pernix K1 JCM
strain JCM 9820
-
-
Manually annotated by BRENDA team
strain 7324
-
-
Manually annotated by BRENDA team
strain DSM 8774
-
-
Manually annotated by BRENDA team
Archaeoglobus fulgidus 7324
strain 7324
-
-
Manually annotated by BRENDA team
strain NCIM 1225
-
-
Manually annotated by BRENDA team
Aspergillus awamori NCIM 1225
strain NCIM 1225
-
-
Manually annotated by BRENDA team
GDH from Aspergillus terreus is kinetically distinct from GDH of Aspergilli niger
-
-
Manually annotated by BRENDA team
gene gdhA
-
-
Manually annotated by BRENDA team
strain NCIM 565
-
-
Manually annotated by BRENDA team
Aspergillus niger NCIM 565
strain NCIM 565
-
-
Manually annotated by BRENDA team
strain ATCC
-
-
Manually annotated by BRENDA team
Aspergillus ochraceus ATCC
strain ATCC
-
-
Manually annotated by BRENDA team
strain NCIM 553
-
-
Manually annotated by BRENDA team
Aspergillus oryzae NCIM 553
strain NCIM 553
-
-
Manually annotated by BRENDA team
GDH from Aspergillus terreus is kinetically distinct from GDH of Aspergilli niger
-
-
Manually annotated by BRENDA team
strain NCIM 656
-
-
Manually annotated by BRENDA team
Aspergillus terreus NCIM 656
strain NCIM 656
-
-
Manually annotated by BRENDA team
strain KSM-635
-
-
Manually annotated by BRENDA team
strain KSM-635
-
-
Manually annotated by BRENDA team
hosts human adult and human infant
-
-
Manually annotated by BRENDA team
strain breve a and parvolorum a
-
-
Manually annotated by BRENDA team
hosts rat and calf
-
-
Manually annotated by BRENDA team
strain infantis a and liberorum
-
-
Manually annotated by BRENDA team
the hosts are pig and chicken
-
-
Manually annotated by BRENDA team
strain H5-3
-
-
Manually annotated by BRENDA team
Cenococcum geophilum H5-3
strain H5-3
-
-
Manually annotated by BRENDA team
two isoenzymes alpha-subunits at 2 mM ammonia and beta-subunits at 29 mM ammonia
-
-
Manually annotated by BRENDA team
Clostridium difficile
-
-
-
Manually annotated by BRENDA team
strain Y7426
-
-
Manually annotated by BRENDA team
Debaryomyces hansenii Y7426
strain Y7426
-
-
Manually annotated by BRENDA team
strain NCIM 1211
-
-
Manually annotated by BRENDA team
Emericella nidulans NCIM 1211
strain NCIM 1211
-
-
Manually annotated by BRENDA team
strain IFO 12964
-
-
Manually annotated by BRENDA team
Enterococcus faecalis IFO 12964
strain IFO 12964
-
-
Manually annotated by BRENDA team
strain DH5alpha
-
-
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
strain K2
-
-
Manually annotated by BRENDA team
strain MRE 600
-
-
Manually annotated by BRENDA team
Escherichia coli DH5alpha
strain DH5alpha
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
strain K2
-
-
Manually annotated by BRENDA team
Escherichia coli MRE
strain MRE 600
-
-
Manually annotated by BRENDA team
NRC-1, enzyme is encoded by gdhA1
-
-
Manually annotated by BRENDA team
strain NRC 36014
-
-
Manually annotated by BRENDA team
Halobacterium salinarum NRC 36014
strain NRC 36014
-
-
Manually annotated by BRENDA team
monokaryotic strain h1
Uniprot
Manually annotated by BRENDA team
strain F-5-2
-
-
Manually annotated by BRENDA team
strain MK53
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae F-5-2
strain F-5-2
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae MK53
strain MK53
-
-
Manually annotated by BRENDA team
Kluyveromyces marxianus CBS6556
CBS6556
-
-
Manually annotated by BRENDA team
strain S238N
Uniprot
Manually annotated by BRENDA team
Laccaria bicolor S238N
strain S238N
Uniprot
Manually annotated by BRENDA team
strain IFO 3071
-
-
Manually annotated by BRENDA team
Lactobacillus fermentum IFO 3071
strain IFO 3071
-
-
Manually annotated by BRENDA team
Lactobacillus plantarum DPPMA49
-
UniProt
Manually annotated by BRENDA team
strain IFO 12546
-
-
Manually annotated by BRENDA team
strain NCDO1867
-
-
Manually annotated by BRENDA team
Lactococcus lactis IFO 12546
strain IFO 12546
-
-
Manually annotated by BRENDA team
Lactococcus lactis NCDO1867
strain NCDO1867
-
-
Manually annotated by BRENDA team
gene msmeg_5442
UniProt
Manually annotated by BRENDA team
strain CDC46
-
-
Manually annotated by BRENDA team
Mycobacterium smegmatis CDC46
strain CDC46
-
-
Manually annotated by BRENDA team
no activity in Amanita citrina
-
-
-
Manually annotated by BRENDA team
no activity in Amanita muscaria
strain MAN
-
-
Manually annotated by BRENDA team
no activity in Amanita muscaria MAN
strain MAN
-
-
Manually annotated by BRENDA team
no activity in Boletus edulis
strain Hub 0
-
-
Manually annotated by BRENDA team
no activity in Boletus edulis Hub 0
strain Hub 0
-
-
Manually annotated by BRENDA team
no activity in Lactarius quietus
-
-
-
Manually annotated by BRENDA team
no activity in Lactarius subdulcis
strain BRI 2
-
-
Manually annotated by BRENDA team
no activity in Lactarius subdulcis BRI 2
strain BRI 2
-
-
Manually annotated by BRENDA team
no activity in Paxillus involutus
-
-
-
Manually annotated by BRENDA team
no activity in Pisolithus tinctorius
strain 441
-
-
Manually annotated by BRENDA team
no activity in Pisolithus tinctorius 441
strain 441
-
-
Manually annotated by BRENDA team
no activity in Rhizopogon luteolus
strain SERRE
-
-
Manually annotated by BRENDA team
no activity in Rhizopogon luteolus SERRE
strain SERRE
-
-
Manually annotated by BRENDA team
no activity in Scleroderma citrinum
strain Foug A
-
-
Manually annotated by BRENDA team
no activity in Scleroderma citrinum Foug A
strain Foug A
-
-
Manually annotated by BRENDA team
no activity in Suillus bovinus
strain LED 1
-
-
Manually annotated by BRENDA team
no activity in Suillus bovinus LED 1
strain LED 1
-
-
Manually annotated by BRENDA team
no activity in Thelephora terrestris
strain CHA
-
-
Manually annotated by BRENDA team
no activity in Thelephora terrestris CHA
strain CHA
-
-
Manually annotated by BRENDA team
no activity in Tricholoma populinum
strain BLAE
-
-
Manually annotated by BRENDA team
no activity in Tricholoma populinum BLAE
strain BLAE
-
-
Manually annotated by BRENDA team
no activity in Xerocomus chrysenteron
-
-
-
Manually annotated by BRENDA team
four putative GDH genes (OsGDH1-4) are present in the rice genome. The GDH sequences from rice and other species can be classified into two types (I and II). OsGDH1-3 belong to type II genes, whereas OsGDH4 belong to type I like gene
-
-
Manually annotated by BRENDA team
strain DS12975
-
-
Manually annotated by BRENDA team
strain NCAIM 00237
-
-
Manually annotated by BRENDA team
Penicillium chrysogenum DS12975
strain DS12975
-
-
Manually annotated by BRENDA team
Penicillium chrysogenum NCAIM 00237
strain NCAIM 00237
-
-
Manually annotated by BRENDA team
NADPH-GDH isozymes GDHI, GDHII, and GDHI'
-
-
Manually annotated by BRENDA team
strain PP4, when grown on isophthalate, Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD show activity of NADP-dependent GDH, while cells grown on glucose, 2fold yeast extract-tryptone broth (2YT) or glutamate show activities of both NAD-dependent GDH and NADP-GDH; strain PPD, when grown on isophthalate, Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD show activity of NADP-dependent GDH, while cells grown on glucose, 2fold yeast extract-tryptone broth (2YT) or glutamate show activities of both NAD-dependent GDH and NADP-GDH
-
-
Manually annotated by BRENDA team
Pseudomonas aeruginosa PP4
NADPH-GDH isozymes GDHI, GDHII, and GDHI'
-
-
Manually annotated by BRENDA team
strain TAD1
-
-
Manually annotated by BRENDA team
genes pcal_1031 and pcal_1606
UniProt
Manually annotated by BRENDA team
genes pcal_1031 and pcal_1606
UniProt
Manually annotated by BRENDA team
strain DSM 3638
-
-
Manually annotated by BRENDA team
strain DSM 3773
-
-
Manually annotated by BRENDA team
contains two NADPH-dependent glutamate dehydrogenases
-
-
Manually annotated by BRENDA team
strain Y05499, strain Y10345 and strain Y11672
-
-
Manually annotated by BRENDA team
two NADP+-dependent glutamate dehydrogenases encoded by GDH1 and GDH3
-
-
Manually annotated by BRENDA team
two NADP+-dependent glutamate dehydrogenases encoded by GDH1 and GDH3
-
-
Manually annotated by BRENDA team
strains 975h- and 972h+
-
-
Manually annotated by BRENDA team
Sphaerostilbe repens
-
-
-
Manually annotated by BRENDA team
strain IFO 12553
-
-
Manually annotated by BRENDA team
Streptococcus equinus IFO 12553
strain IFO 12553
-
-
Manually annotated by BRENDA team
strain PCC 6803
-
-
Manually annotated by BRENDA team
isolate AN1
-
-
Manually annotated by BRENDA team
Thermophilic bacillus
-
-
-
Manually annotated by BRENDA team
strain ATCC 95640
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
two industrial strains of Penicillium chrysogenum a penicillin (PC-pen)- and a cephalosporin producing (PC-ceph) are used in which the NADPH-dependent GDH is deleted by replacing 0.8 kb of the C-terminus of the gdhA gene with the hygromyin B resistance marker, resulting in PC-pen-DELTAgdhA and PC-ceph-DELTAgdhA. The two strains are isogenic except for the insertion of the Streptomyces clavuligerus expandase gene into the genome of PC-ceph. It is shown that this genetic modification results in a radical change in morphology
malfunction
-
Gdh3-null cells show accelerated chronological aging and hypersusceptibility to thermal and oxidative stress during stationary phase. Upon exposure to oxidative stress, Gdh3-null strains display a rapid loss in viability associated with typical apoptotic hallmarks, i.e. reactive oxygen species accumulation, nuclear fragmentation, DNA breakage, and phosphatidylserine translocation. In addition, Gdh3-null cells, but not Gdh1-null cells, have a higher tendency toward GSH depletion and subsequent reactive oxygen species accumulation than did wild-type cells. GSH depletion is rescued by exogenous GSH or glutamate. The hypersusceptibility of stationary phase Gdh3-null cells to stress-induced apoptosis is suppressed by deletion of GDH2. Gdh1, but not Gdh3, is subjected to stationary phase-specific degradation in which the Lys-426 residue in the Box420Gdh1 region plays an essential role
malfunction
-
Gdh3-null cells show accelerated chronological aging and hypersusceptibility to thermal and oxidative stress during stationary phase. Upon exposure to oxidative stress, Gdh3-null strains display a rapid loss in viability associated with typical apoptotic hallmarks, i.e. reactive oxygen species accumulation, nuclear fragmentation, DNA breakage, and phosphatidylserine translocation. In addition, Gdh3-null cells, but not Gdh1-null cells, have a higher tendency toward GSH depletion and subsequent reactive oxygen species accumulation than did wild-type cells. GSH depletion is rescued by exogenous GSH or glutamate. The hypersusceptibility of stationary phase Gdh3-null cells to stress-induced apoptosis is suppressed by deletion of GDH2. Gdh1, but not Gdh3, is subjected to stationary phase-specific degradation in which the Lys-426 residue in the Box420Gdh1 region plays an essential role
-
metabolism
A0R3E3, -
NADP+-GDH is involved in nitrogen assimilation due to a constitutive aminating activity, specific activity of the aminating NADP+-GDH reaction is independent of nitrogen availability, it does not change significantly in response to prolonged exposure to nitrogen limitation, in contrast to the deaminating activity, which is 2fold increased exposed to ammonium starvation conditions. The deaminating reaction changes in response to varying ammonium concentrations and is regulated in response to nitrogen availability. NADP+-GDH is not regulated on the transcriptional level. The enzyme is invovled in the additional nitrogen assimilatory pathway via glutamate dehydrogenase, GDH, regulation of NADP+-GDH specific activity, overview
physiological function
-
to test the effect of decreased hGDH expression, small interfering hGDH RNAs are expressed intracellularly in BE(2)C human neuroblastoma cells. hGDH mRNA knockdown is confirmed by immunoblotting and RT-PCR. TUNEL and DNA fragmentation assays 48 h after transfection reveal that inhibition of hGDH expression induces cellular apoptosis and activates phospho-ERK1/2 (phospho-extracellular-signal-regulated kinase 1/2)
physiological function
-
carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60C are analysed: isophthalate-, glucose-, 2YT- or mHB-grown cells retain 100% of the activity of NADP-GDH
physiological function
-
carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD; carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60C are analysed: GDHI from isophthalate- and mHB-grown cells retain 70% and 90% of its activity, respectively; carbon source-dependent modulation of different forms of NADP-GDH in bacterial strains Acinetobacter lwoffii strain ISP4, Pseudomonas aeruginosa strain PP4 and Pseudomonas strain PPD. Time-dependent changes in the activity of NADP-GDH at 60C are analysed: In Pseudomonas aeruginosa strain PPD, isophthalate-, glucose-, 2YT- or mHB-grown cells retain 100% of the activity of NADP-GDH, while PPD cells grown on pHB and benzoate show 25% and 40% loss of activity
physiological function
-
involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cells, overview. GDH1, but not GDH3, is responsible for the resistance against stress-induced apoptosis in logarithmic phase cells, Necessity of GDH3 for the resistance to stress-induced apoptosis and chronological aging is due to the stationary phase-specific expression of GDH3 and concurrent degradation of Gdh1 in which the Lys-426 residue plays an essential role
physiological function
-
Gdh1p is the primary GDH enzyme and Gdh3p plays an evident role during aerobic glutamate metabolism
physiological function
-
involvement of GDH3-encoded NADP+-dependent glutamate dehydrogenase in yeast cell resistance to stress-induced apoptosis in stationary phase cells, overview. GDH1, but not GDH3, is responsible for the resistance against stress-induced apoptosis in logarithmic phase cells, Necessity of GDH3 for the resistance to stress-induced apoptosis and chronological aging is due to the stationary phase-specific expression of GDH3 and concurrent degradation of Gdh1 in which the Lys-426 residue plays an essential role
-
metabolism
-
both NADP(H)-GDH (gdhA) and glutamine synthetase play important roles in ammonium assimilation
additional information
P00370
modelling of NADP+ in domain II reveals the potential contribution of positively charged residues from a neighbouring alpha-helical hairpin to phosphate recognition, sequence-structure relationship, overview. A single sequence accommodates both coenzymes in the dual-specificity GDHs of animals
additional information
Q8ILF7, Q8ILT0
the parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes; the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The parasitic enzyme does not contain the antenna domain, responsible for allosteric regulation in the mammalian enzymes
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-aminopentanoate + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
show the reaction diagram
-
activity with 2-oxovalerate amd 2-aminopentanoate is 25% and 17% compared to the activity with 2-oxoglutarate and L-glutamate
-
-
r
2-oxoadipate + NADPH + NH3
L-2-aminoadipate + NADP+ + H2O
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae F-5-2
-
6.3% of the activity with 2-oxoglutarate
-
-
?
2-oxobutyrate + NADPH + NH3
L-2-aminobutyrate + NADP+ + H2O
show the reaction diagram
Klebsiella pneumoniae, Klebsiella pneumoniae F-5-2
-
12% of the activity with 2-oxoglutarate
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
show the reaction diagram
P54388
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
show the reaction diagram
Q96UJ9
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
show the reaction diagram
Q9HFR6
-
-
-
?
2-oxoglutarate + NAD(P)H + NH3
L-glutamate + NAD(P)+ + H2O
show the reaction diagram
Laccaria amethystina, Hebeloma bulbiferum, Cenococcum geophilum H5-3
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-, P28998
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Aspergillus oryzae NCIM 553
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Klebsiella pneumoniae F-5-2
-
-, ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Debaryomyces hansenii Y7426
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Aspergillus awamori NCIM 1225, Emericella nidulans NCIM 1211, Aspergillus niger NCIM 565
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Lactococcus lactis NCDO1867
-
-
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Aspergillus terreus NCIM 656
-
-
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Kluyveromyces marxianus CBS6556
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NH3 + NADH
L-glutamate + H2O + NAD+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADH + H+
L-glutamate + H2O + NAD+
show the reaction diagram
-
weak activity
-
-
?
2-oxoglutarate + NH3 + NADPH
L-glutamate + H2O + NADP+
show the reaction diagram
-
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
Q8ILF7, Q8ILT0
-
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
Q8ILF7, Q8ILT0
referred reaction
-
-
r
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
Sphaerostilbe repens
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
Thermophilic bacillus
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
Bifidobacterium bifidum A
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
Aspergillus niger NCIM 565
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
Lactobacillus fermentum IFO 3071
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
Aspergillus ochraceus ATCC
-
-
-
-
-
2-oxoglutarate + NH4+ + NADPH
L-glutamate + NADP+
show the reaction diagram
Bifidobacterium bifidum B
-
-
-
-
-
2-oxovalerate + NADPH + NH3
L-2-aminovalerate + NADP+ + H2O
show the reaction diagram
-
15% of the activity with 2-oxoglutarate
-
-
?
L-2-oxoglutarate + NADPH + NH3
glutamate + NADP+ + H2O
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
P28724
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
Penicillium chrysogenum DS12975
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH
show the reaction diagram
Lactococcus lactis NCDO1867
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
?
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-, Q2WCS9
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
P00370
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
A3MWK6
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
Q8ILF7, Q8ILT0
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
usage of NH4Cl as substrate for the reverse reaction
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
A0R3E3, -
reaction cycle, specificities of forward and reverse reactions, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
A0R3E3, -
reaction cycle, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
usage of NH4Cl as substrate for the reverse reaction
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
the enzyme shows a strict specificity for L-glutamate and NADP+ on oxidative deamination and for 2-oxoglutarate and NADPH on reductive amination. No activity with the following amino acids in oxidative deamination: D-glutamate, L-norvaline, L-2-aminobutyrate, L-valine, L-alanine, L-aspartate, L-serine, L-cysteine, L-lysine, or L-phenylalanin. No activity with the following amino acids in reductive amination: pyruvate, 2-oxovalerate, 2-oxoisocaproate, 2-oxobutyrate, or 2-oxoisovalerate
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
Lactobacillus plantarum DPPMA49
Q2WCS9
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
A3MWK6
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
Pseudomonas aeruginosa PP4
-
-
-, usage of NH4Cl as substrate for the reverse reaction
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
Acinetobacter lwoffii ISP4
-
-, usage of NH4Cl as substrate for the reverse reaction
-
-
r
L-glutamate + NAD(P)+ + H2O
2-oxoglutarate + NAD(P)H + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Clostridium difficile
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Sphaerostilbe repens
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Thermophilic bacillus
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Sphaerostilbe repens
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
biphasic kinetic behavior for L-glutamate
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium bifidum A
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Escherichia coli DH5alpha
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Streptococcus equinus IFO 12553
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium thermophilum B
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Escherichia coli MRE
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Halobacterium salinarum NRC 36014
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Aeropyrum pernix K1 JCM
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Aeropyrum pernix K1 JCM
-
-
biphasic kinetic behavior for ammonia
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Lactobacillus fermentum IFO 3071
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Lactococcus lactis IFO 12546
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Enterococcus faecalis IFO 12964
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Archaeoglobus fulgidus 7324
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Escherichia coli K12
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium pseudolongum A
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium pseudolongum B
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Penicillium chrysogenum NCAIM 00237
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Aspergillus ochraceus ATCC
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium bifidum B
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Mycobacterium smegmatis CDC46
-
-
-
r
additional information
?
-
-
glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
-
-
-
additional information
?
-
-
glutamate dehydrogenase functions physiologically for the synthesis of L-glutamate from 2-oxoglutarate and ammonia
-
-
-
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
-
additional information
?
-
-
the enzyme is encoded by gdhA. In strains expressing high levels of gdhA mRNA, two promoters, gdhA P1 and gdhA P2, initiate transcription of gdhA. In strains expressing low mRNA levels, gdhA P2 is not active because of weak expression of GdhR, an associated regulatory gene. 2-Oxoglutarate inhibits binding of GdhR to gdhA P2
-
-
-
additional information
?
-
-
the yeast form specific isoenzyme is induced in presence of glucose, the mycelium-form is not induced. Possible involvement of the enzyme in yeast-mycelium transition
-
-
-
additional information
?
-
-
no activity with 2-oxoisovalerate and pyruvate
-
-
-
additional information
?
-
-
no reaction with D-glutamate, L-glutamine or DL-2-hydroxyglutarate as possible substrates in place of L-glutamate, methylamine is unable to replace ammonium in the biosynthetic reaction
-
-
-
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
-
-
-
additional information
?
-
Q8ILF7, Q8ILT0
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
-
additional information
?
-
Q8ILF7, Q8ILT0
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
-
additional information
?
-
A3MWK6
the enzyme also shows low activity with NAD+/NADH, 17% and 7% of the activity with NADP+ and NADPH, respectively. The enzyme also shows low activity with L-norvaline as substrates for oxidative deamination, and with 2-oxovalerate and 2-oxobutyrate for reducive amination, substrate specificity, overview. No activity with L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate, 2-oxocaproate, and pyruvate
-
-
-
additional information
?
-
Klebsiella pneumoniae F-5-2
-
no activity with 2-oxoisovalerate and pyruvate
-
-
-
additional information
?
-
Debaryomyces hansenii Y7426
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
-
additional information
?
-
Aspergillus niger NCIM 565
-
no reaction with D-glutamate, L-glutamine or DL-2-hydroxyglutarate as possible substrates in place of L-glutamate, methylamine is unable to replace ammonium in the biosynthetic reaction
-
-
-
additional information
?
-
A3MWK6
the enzyme also shows low activity with NAD+/NADH, 17% and 7% of the activity with NADP+ and NADPH, respectively. The enzyme also shows low activity with L-norvaline as substrates for oxidative deamination, and with 2-oxovalerate and 2-oxobutyrate for reducive amination, substrate specificity, overview. No activity with L-glutamine, L-alanine, L-aspartate, L-cysteine, L-serine, L-lysine, L-phenylalanine, and L-tryptophan, or with 2-oxoisocaproate, 2-oxocaproate, and pyruvate
-
-
-
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
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Klebsiella pneumoniae F-5-2
-
ammonia-assimilating enzyme
-
-
r
2-oxoglutarate + NADPH + NH3
L-glutamate + NADP+ + H2O
show the reaction diagram
Kluyveromyces marxianus CBS6556
-
the enzyme primary functions to assimilate ammonium when its extracellular concentration is in a narrow range. The enzyme may not be the main enzyme for ammonia assimilation in Kluyveromyces marxianus
-
-
?
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
-
-
-
-
ir
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
Q8ILF7, Q8ILT0
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-, Q2WCS9
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
P00370
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
A3MWK6
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
Q8ILF7, Q8ILT0
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
A0R3E3, -
reaction cycle, specificities of forward and reverse reactions, overview
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
Lactobacillus plantarum DPPMA49
Q2WCS9
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
A3MWK6
-
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
Pseudomonas aeruginosa PP4, Acinetobacter lwoffii ISP4
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Clostridium difficile
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Sphaerostilbe repens
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Thermophilic bacillus
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium bifidum A
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Escherichia coli DH5alpha
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Streptococcus equinus IFO 12553
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium thermophilum B
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Escherichia coli MRE
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Halobacterium salinarum NRC 36014
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Aeropyrum pernix K1 JCM
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Lactobacillus fermentum IFO 3071, Lactococcus lactis IFO 12546
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Enterococcus faecalis IFO 12964
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Archaeoglobus fulgidus 7324
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Escherichia coli K12
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium pseudolongum A, Bifidobacterium pseudolongum B
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Penicillium chrysogenum NCAIM 00237
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Aspergillus ochraceus ATCC
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Bifidobacterium bifidum B
-
-
-
-
r
L-glutamate + NADP+ + H2O
2-oxoglutarate + NADPH + NH3
show the reaction diagram
Mycobacterium smegmatis CDC46
-
-
-
-
r
additional information
?
-
-
glutamate dehydrogenase represents an enzymatic link between major catabolic and biosynthetic pathways via the tricarboxylic acid cycle intermediate 2-oxoglutarate
-
-
-
additional information
?
-
-
glutamate dehydrogenase functions physiologically for the synthesis of L-glutamate from 2-oxoglutarate and ammonia
-
-
-
additional information
?
-
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
-
additional information
?
-
-
the enzyme is encoded by gdhA. In strains expressing high levels of gdhA mRNA, two promoters, gdhA P1 and gdhA P2, initiate transcription of gdhA. In strains expressing low mRNA levels, gdhA P2 is not active because of weak expression of GdhR, an associated regulatory gene. 2-Oxoglutarate inhibits binding of GdhR to gdhA P2
-
-
-
additional information
?
-
-
the yeast form specific isoenzyme is induced in presence of glucose, the mycelium-form is not induced. Possible involvement of the enzyme in yeast-mycelium transition
-
-
-
additional information
?
-
-
in yeast, NADP+-dependent enzymes, EC 1.4.1.4, encoded by GDH1 and GDH3, are reported to synthesize glutamate from 2-oxtoglutarate, while an NAD+-dependent enzyme, EC 1.4.1.2, encoded by GDH2, catalyzes the reverse reaction. Gdh1p is the primary GDH enzyme and Gdh2p and Gdh3p play evident roles during aerobic glutamate metabolism
-
-
-
additional information
?
-
Q8ILF7, Q8ILT0
Like PfGDH1, PfGDH2 is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH1 but with slightly higher Km values for its substrates
-
-
-
additional information
?
-
Q8ILF7, Q8ILT0
PfGDH1, like PfGDH2, is an NADP(H)-dependent enzyme with a specific activity comparable to PfGDH2 but with slightly lower Km values for its substrates
-
-
-
additional information
?
-
Debaryomyces hansenii Y7426
-
enzyme synthesis is increased under hyperosmotic conditions in the halotolerant yeast
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NAD(P)H
P54388
-
NAD(P)H
Q9HFR6
-
NAD+
-
the ratio of turnover-number to KM-value for NADP+ is 72679fold higher than the ratio for NAD+
NAD+
-
low activity
NADH
-
the ratio of turnover-number to KM-value for NADPH is 6fold higher than the ratio for NADH
NADP+
-
the enzyme requires NADP+ as the coenzyme for the oxidation of L-glutamate, which can not be replaced by NAD+
NADP+
Clostridium difficile
-
-
NADP+
Sphaerostilbe repens
-
-
NADP+
Thermophilic bacillus
-
-
NADP+
-
preferred coenzyme. The ratio of turnover-number to KM-value for NADP+ is 72679fold higher than the ratio for NAD+
NADP+
-
stimulates the enzyme at lower 2-oxoglutarate levels
NADP+
A0R3E3, -
specific for
NADP+
P00370
binding structure involving Asp263 and Ser264, residues P7 and P8, molecular modelling of NADP+ onto the free enzyme structure, overview
NADP+
Q8ILF7, Q8ILT0
;
NADPH
-
for the reduction of 2-oxoglutarate, NADPH is the coenzyme and NADH is inert
NADPH
Clostridium difficile
-
-
NADPH
Sphaerostilbe repens
-
-
NADPH
Thermophilic bacillus
-
-
NADPH
-
preferred coenzyme. The ratio of turnover-number to KM-value for NADPH is 6fold higher than the ratio for NADH
NADPH
-
OsGDH4 gene contains an NADPH-specific motif
NADPH
-
preferred coenzyme compared to NADH
NADPH
A0R3E3, -
specific for
NADPH
Q8ILF7, Q8ILT0
;
additional information
-
cofactor specificity not mentioned
-
additional information
A3MWK6
low activity with NAD+/NADH
-
additional information
Q8ILF7, Q8ILT0
no activity with NAD+; no activity with NAD+
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Zn2+
-
forward reaction of GDH from Aspergillus terreus is 80% inhibited by 5 mM ZnCl2
additional information
-
Ca2+ has no effects on the aminating activity of NADP(H)-GDH
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,4-Pyridinedicarboxylate
-
-
2,4-Pyridinedicarboxylate
-
inhibits less efficiently
2,4-Pyridinedicarboxylate
-
weak inhibitor
2-Methyleneglutarate
-
-
2-Methyleneglutarate
-
weak inhibitor
2-oxoglutarate
-
competitive inhibitor of the deamination
2-oxoglutarate
-
shows allosteric properties and a sigmoid response (nH=2.5) towards 2-oxoglutarate saturation
2-oxoglutarate
-
substrate inhibition above 2.0 mM
4-chloromercuribenzoate
-
at 1 mM, 86% inhibition
4-chloromercuribenzoate
-
at 0.01 mM, 35% inhibition
4-chloromercuribenzoate
-
at 1 mM and 10 mM, 30% inhibition and 100% inhibition
ADP
-
at 4 mM slight inhibitory
ADP
-
at 1 mM, 57% inhibition for oxidative deamination and 23% inhibition for reductive amination respectively
ADP
-
at 0.3 mM, 22% inhibition of oxidative deamination
Ag2+
-
at 1 mM, 60% inhibition
AgNO3
-
1 mM, 30C, complete loss of aminating activity
AlCl3
-
at 1 mM, 30% inhibition
AlCl3
-
at 1 mM, 21% inhibition
AlCl3
-
1 mM, 30C, 23% loss of aminating activity
AMP
-
slight inhibitory
AMP
-
slight inhibitory
AMP
-
at 0.3 mM 33% inhibition of oxidative deamination
AMP
-
inhibitory at higher concentrations than 1 mM
ATP
-
at 4 mM slight inhibitory
BaCl2
-
1 mM, 30C, 15% loss of aminating activity
Bithionol
Q8ILF7, Q8ILT0
;
Ca2+
-
at 1 mM 27% inhibition
CaCl2
-
1 mM, 30C, 11% loss of aminating activity
CH2ICOOH
-
1 mM, 30C, 15% loss of aminating activity
dimethyl ester of isophthalic acid
-
dimethyl ester of isophthalate (DMIP), but not isophthalate, inhibits Aspergillus niger growth on agar as well as in liquid culture. This is ascribed to the inability of isophthalate to enter fungal mycelia. Dimethyl ester of isophthalic acid is hydrolysed intracellularly to isophthalate. Subsequent to DMIP addition, intracellular isophthalate can be demonstrated. Addition of NH4+ to DMIP-treated Aspergillus niger mycelia results in intensive vacuolation, retraction of cytoplasm and autolysis
FeSO3(NH4)2SO4
-
1 mM, 30C, 14% loss of aminating activity
fumarate
-
at 5 mM 20% inhibition
fumarate
-
at 20 mM 30% inhibition
glutamate
-
competitive inhibitor of the amination reaction
Glutaric acid
-
at 20 mM, 25% inhibition
glyoxylate
-
at 20 mM, 30% inhibition
guanidine hydrochloride
-
complete loss of activity
guanidine hydrochloride
-
complete loss of activity
GW5074
Q8ILF7, Q8ILT0
;
Hexachlorophene
Q8ILF7, Q8ILT0
15% inhibition at 0.016 mM; 80% inhibition at 0.016 mM
Hg2+
-
at 1 mM, 100% activity loss
Hg2+
-
at 1 mM, 70% inhibition
Hg2+
-
at 0.1 mM, complete activity loss
Hg2+
-
at 1 mM, 10% inhibition
Hg2+
-
at 1 mM, 100% activity loss
HgCl2
-
at 1 mM, 64% inhibition
HgCl2
-
at 1 mM, 45% inhibition
HgCl2
-
at 1 mM, no activity, oxidative deamination
HgCl2
-
at 0.01 mM, 27% inhibition
HgCl2
-
1 mM, 30C, 48% loss of aminating activity
hydroxylamine
-
competitive inhibitor with ammonia and uncompetitive inhibitor with both 2-oxoglutarate and NADPH
iodoacetamide
-
at 4 mM, complete inactivation
Isophthalate
-
-
Isophthalate
-
potent in vitro inhibitor
Isophthalate
-
weak inhibitor
Isophthalate
-
a competitive inhibitor of glutamate dehydrogenase, is involved in C and N metabolism
Isophthalic acid
-
-
KCl
-
more than 50 mM
KCl
-
500 mM, 80-90% inhibition, by high ionic strength
L-glutamate
-
substrate inhibition above 15 mM
L-Glutamic acid
-
at 20 mM 25% inhibition
L-homoserine
-
competitive inhibitor with respect to both ammonia and glutamine
L-tryptophan
-
at 20 mM, 15% inhibition
malate
-
at 5 mM, 20% inhibition
malate
-
at 20 mM, 30% inhibition
Mg2+
-
at 1 mM, 16% activity loss
Mn2+
-
at 1 mM, 19% activity loss
MnCl2
-
at 1 mM, 63% inhibition
N-ethylmaleimide
-
at 0.8 mM, 44% inhibition
NaCl
-
more than 50 mM
NaCl
-
50 mM, 50% inhibition. 100 mM, about 60% inhibition. 500 mM, about 90% inhibition by high ionic strength
NADP+
-
inhibits at higher 2-oxoglutarate levels
NH4+
-
inhibits the oxidative deamination activity as a product, inhibition is non-competitive with respect to L-glutamate
nitrogen assimilation control protein
-
represses the transcription of the gene gdhA
-
oxaloacetate
-
at 20 mM slight inhibitory
oxaloacetate
-
at 20 mM, 60% inhibition
p-Chloromercuriphenyl sulfonate
-
inactivetes, can be reversed by addition of cysteine
p-hydroxymercuribenzoic acid
-
at 0.08 mM, 50% inhibition
p-hydroxymercuribenzoic acid
-
at 10 mM, 90% inhibition after 40 min
Pb(CH3COO)2
-
at 1 mM, 59% inhibition
Pb(CH3COO)2
-
at 1 mM, 64% inhibition
potassium phosphate
-
over 0.1 M at oxidative deamination
pyridoxal 5'-phosphate
-
at 1 mM, 35% inhibition
pyridoxal 5'-phosphate
-
at 1 mM, 45% inhibition
pyridoxal 5'-phosphate
-
at 10 mM, 90% inhibition, complete protection when 16.8 mM 2-oxoglutarate and 1.68 mM NADP+ are added
pyruvate
-
at 10 mM slight inhibitory
sodium dodecylsulfate
-
at 0.7% w/v after 1 h 5% activity
succinate
-
competitive inhibitor with 2 oxoglutarate, uncompetitive with NADPH and non-competitive with ammonia
Urea
-
at 0C 1 h at 2 M 65% inhibition
Urea
-
inactivation with 2 mM urea
Urea
-
fully active at 20C in 8 mM urea
Urea
-
no activity at 6 mM
Urea
-
at 8 M stable for 10 min
Zn2+
-
at 1 mM, 64% activity loss
Zn2+
-
at 1 mM, 40% inhibition
MnCl2
-
at 1 mM, 20% inhibition
additional information
-
not inhibited by D-glutamate, L-glutamine or DL-2-hydroxyglutarate
-
additional information
-
2-oxoglutarate and NH3 show substrate inhibition
-
additional information
-
no effect: EDTA, o-phenanthroline, sodium azide, 8-hydroxyquinoline in the concentration raneg of 1-10 mM
-
additional information
Q8ILF7, Q8ILT0
inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1; inhibitors hexachlorophene, GW5074, and bithionol are more effective on PfGDH2 than on PfGDH1
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3,5-pyrazoledicarboxylate
-
activates at lower 2-oxoglutarate concentration
3,5-pyridinedicarboxylate
-
activates at lower 2-oxoglutarate concentration
acetonitrile
-
activates
ADP
-
at 1 mM, 11% activation
ADP
-
at 0.3 mM 40% activation
AMP
-
slight activation up to 1 mM
ATP
-
at 0.3 mM, 60% activation of reductive amination
ATP
-
at 2 mM, 50% activation
ATP
-
30% stimulation in the presence of 2 mM Mg2+
CaCl2
-
at 5 mM, 135% activation, oxidative deamination
CaCl2
-
at 20 mM, 25% and 108% activation of reductive amination and oxidative deamination respectively
DL-2-hydroxyglutarate
-
activates at lower 2-oxoglutarate concentration
ethanol
-
activates up to 40% v/v
GDP
-
at 1 mM five-fold Michaelis Menten constant of 2-oxoglutarate
GDP
-
30% stimulation in the presence of 2 mM Mg2+
Glutarate
-
activates at lower 2-oxoglutarate concentration
GTP
-
at 0.083 mM 22% activation
GTP
-
30% stimulation in the presence of 2 mM Mg2+
IDP
-
at 1 mM five-fold Michaelis Menten constant of 2-oxoglutarate
Itaconate
-
activates even in the presence of 10 mM 2-oxoglutarate
K2HPO4
-
at 0.15 M three to fourfold stimulation of activity
K2SO4
-
280-300% activity at 150-200 mM
K3PO4
-
less effective than K2SO4 and Na3PO4
KCl
-
170-200% activity at 50-100 mM
KCl
-
at 0.2 M three to fourfold stimulation of activity
KCl
-
optimal activity at 1-1.5 M
KCl
-
at concentrations below 2 mM
KCl
-
at concentrations below 1 mM
KCl
-
up to 50mM
methanol
-
activates
MgCl2
-
at 5 mM, 104% activity, oxidative deamination
Na2SO4
-
less effective than K2SO4 and Na3PO4
Na3PO4
-
280-300% activity at 150-200 mM
NaCl
-
170-200% activity at 50-100 mM
NaCl
-
at 0.2 M three to fourfold stimulation of activity
NaCl
-
optimal activity at 1-1.5 M
NaCl
-
up to 50 mM
oxalylglycine
-
activates at lower 2-oxoglutarate concentration
potassium phosphate
-
up to 0.1 M oxidative deamination
UTP
-
activates up to 70%
Zn2+
-
activates up to 0.1 mM
MnCl2
-
at 5 mM, 250% activity, oxidative deamination
additional information
-
exhibits 2.5-fold-higher GDH activity than cells are grown in milk, instead of glucose
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.16
-
2-oxoglutarate
-
reductive amination at 80C
0.2
-
2-oxoglutarate
-
reductive amination
0.2
-
2-oxoglutarate
Q8ILF7, Q8ILT0
pH 7.0, 25C, recombinant enzyme
0.28
-
2-oxoglutarate
-
reductive amination
0.32
-
2-oxoglutarate
-
reductive amination
0.34
-
2-oxoglutarate
-
reductive amination at 25C
0.36
-
2-oxoglutarate
-
reductive amination
0.365
-
2-oxoglutarate
Q8ILF7, Q8ILT0
pH 7.0, 25C, recombinant enzyme
0.4
-
2-oxoglutarate
-
reductive amination
0.5
-
2-oxoglutarate
-
reductive amination at 60C
0.5
-
2-oxoglutarate
-
reductive amination
0.64
-
2-oxoglutarate
Sphaerostilbe repens
-
reductive amination
0.64
-
2-oxoglutarate
-
reductive amination
0.68
-
2-oxoglutarate
-
in the presence of 100 mM NH4Cl, at 25C and pH 8
0.68
-
2-oxoglutarate
-
wild-type EcGDH, Vmax: 464 micromol/min/mg, pH 8.0, 25C
0.77
-
2-oxoglutarate
-
reductive amination
0.93
-
2-oxoglutarate
-
reductive amination
1
-
2-oxoglutarate
-
reductive amination
1.1
-
2-oxoglutarate
-
in the presence of 200 mM NH4Cl, at 25C and pH 8
1.2
-
2-oxoglutarate
-
reductive amination
1.25
-
2-oxoglutarate
-
reductive amination
1.3
-
2-oxoglutarate
Thermophilic bacillus
-
reductive amination
1.5
-
2-oxoglutarate
-
reductive amiantion
1.54
-
2-oxoglutarate
-
reductive amination
1.7
-
2-oxoglutarate
-
pH 8.3, 50C
1.7
-
2-oxoglutarate
-
reductive amination at 50C
1.7
-
2-oxoglutarate
-
reductive amination at 80C
1.7
-
2-oxoglutarate
A3MWK6
pH 9.5, 50C, recombinant enzyme
2
-
2-oxoglutarate
-
reductive amination at 0.6 M NH4Cl
2
-
2-oxoglutarate
-
reductive amination at 56C
2.2
-
2-oxoglutarate
-
pH 8.0, 25C
2.41
-
2-oxoglutarate
-
reductive amination
2.5
3
2-oxoglutarate
-
in the presence of 400 mM NH4Cl, at 25C and pH 8
3
-
2-oxoglutarate
-
reductive amination at 25C
3
-
2-oxoglutarate
-
reductive amination at 25C
3.13
-
2-oxoglutarate
-
reductive amination at 30C
3.2
-
2-oxoglutarate
-
reductive amination at 33C
3.2
-
2-oxoglutarate
-
pH 7.0, 38.5C, DELTA40N-homohexamer
3.25
-
2-oxoglutarate
-
reductive amination
3.97
-
2-oxoglutarate
-
pH 8.0, 30C, recombinant enzyme
4.78
-
2-oxoglutarate
-
-
4.78
-
2-oxoglutarate
-
28C
5
-
2-oxoglutarate
-
reductive amination
5
-
2-oxoglutarate
-
pH 7.0, 38.5C, alpha-homohexamer
5.6
-
2-oxoglutarate
-
reductive amination
6
-
2-oxoglutarate
-
28C
6
-
2-oxoglutarate
-
pH 7.6, 60C
6.8
-
2-oxoglutarate
-
pH 7.0, 38.5C, beta-homohexamer
9
-
2-oxoglutarate
-
reductive amination at 1 M NH4Cl
285
-
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 781 mM NH4Cl, Vmax: 2260 micromol/min/mg, pH 8.0, 25C
606
-
2-oxoglutarate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 1800 mM NH4Cl, Vmax: 200 micromol/min/mg, pH 8.0, 25C
0.22
-
L-glutamate
-
oxidative deamination at 80C
0.6
-
L-glutamate
-
pH 7.6, 60C
0.61
-
L-glutamate
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
1.05
-
L-glutamate
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
1.1
-
L-glutamate
Thermophilic bacillus
-
oxidative deamination
1.3
-
L-glutamate
-
oxidative deamination
2
-
L-glutamate
-
reductive amination
2.2
-
L-glutamate
-
oxidative deamination
2.3
-
L-glutamate
-
oxidative deamination
2.3
-
L-glutamate
-
oxidative deamination
2.3
-
L-glutamate
-
at 25C and pH 8
2.3
-
L-glutamate
-
wild-type EcGDH, Vmax: 37.9 micromol/min/mg, pH 8.0, 25C
3.2
-
L-glutamate
-
oxidative deamination at 25C
3.3
-
L-glutamate
-
pH 8.3, 50C
3.3
-
L-glutamate
-
oxidative deamination at 50C
3.4
-
L-glutamate
A3MWK6
pH 10.5, 50C, recombinant enzyme
3.7
-
L-glutamate
-
reductive amination
3.9
-
L-glutamate
-
oxidative deamination at 60C
5.18
-
L-glutamate
-
oxidative deamination
5.5
-
L-glutamate
Sphaerostilbe repens
-
oxidative deamination
6.06
-
L-glutamate
-
oxidative deamination at 30C
6.36
-
L-glutamate
-
oxidative deamination, Gdh3p gene
9.12
-
L-glutamate
-
oxidative deamination at 80C
9.79
-
L-glutamate
-
oxidative deamination, Gdh1p gene
10
-
L-glutamate
-
oxidative deamination
14.2
-
L-glutamate
-
oxidative deamination
15.15
-
L-glutamate
-
pH 8.0, 30C, recombinant enzyme
18
-
L-glutamate
-
oxidative deamination, biphasic kinetics
21
-
L-glutamate
-
pH 7.0, 38.5C, beta-homohexamer
24.1
-
L-glutamate
-
28C
25
-
L-glutamate
-
pH 7.0, 38.5C, DELTA40N-homohexamer
27
-
L-glutamate
-
oxidative deamination at 33C
28.6
-
L-glutamate
-
oxidative deamination
29
-
L-glutamate
-
oxidative deamination
32.3
-
L-glutamate
-
oxidative deamination
34
-
L-glutamate
-
pH 7.0, 38.5C, alpha-homohexamer
34.6
-
L-glutamate
-
28C
34.7
-
L-glutamate
-
-
38.2
-
L-glutamate
-
oxidative deamination
44
-
L-glutamate
-
oxidative deamination
67.4
-
L-glutamate
-
oxidative deamination
79
-
L-glutamate
-
oxidative deamination
81
-
L-glutamate
-
oxidative deamination, biphasic kinetics
225
-
L-glutamate
-
oxidative deamination
3.629
-
NAD+
-
pH 9.0, 50C
0.36
-
NADH
-
pH 7.6, 50C
0.368
-
NADH
-
pH 9.0, 50C
0.0064
-
NADP+
-
oxidative deamination
0.0098
-
NADP+
-
recombinant enzyme, oxidative deamination
0.01
-
NADP+
-
oxidative deamination at 25C
0.0102
-
NADP+
-
wild-type enzyme, oxidative deamination
0.0105
-
NADP+
-
oxidative deamination, Gdh3p gene
0.013
-
NADP+
-
oxidative deamination
0.0141
-
NADP+
-
oxidative deamination, Gdh1p gene
0.015
-
NADP+
-
pH 7.0, 38.5C, DELTA40N-homohexamer
0.017
-
NADP+
-
-
0.017
-
NADP+
-
28C
0.018
-
NADP+
-
wild-type EcGDH, Vmax: 45.6 micromol/min/mg, pH 8.0, 25C
0.0184
-
NADP+
P00370
wild-type enzyme, pH 8.0, temperature not specified in the publication
0.019
-
NADP+
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
0.02
-
NADP+
-
pH 7.6, 60C
0.02
-
NADP+
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
0.023
-
NADP+
-
oxidative deamination
0.027
-
NADP+
-
pH 7.0, 38.5C, alpha-homohexamer
0.028
-
NADP+
-
pH 7.0, 38.5C, beta-homohexamer
0.029
-
NADP+
-
oxidative deamination at 80C
0.029
-
NADP+
-
oxidative deamination at 30C
0.03
-
NADP+
-
oxidative deamination
0.031
-
NADP+
-
oxidative deamination
0.0328
-
NADP+
P00370
mutant K289Q, pH 8.0, temperature not specified in the publication
0.035
-
NADP+
A3MWK6
pH 10.5, 50C, recombinant enzyme
0.038
-
NADP+
-
oxidative deamination at 80C
0.039
-
NADP+
-
oxidative deamination
0.039
-
NADP+
-
pH 8.3, 50C
0.039
-
NADP+
-
oxidative deamination at 50C
0.04
-
NADP+
-
oxidative deamination
0.04
-
NADP+
-
oxidative deamination
0.041
-
NADP+
-
pH 8.0, 30C, recombinant enzyme
0.042
-
NADP+
-
oxidative deamination
0.043
-
NADP+
-
oxidative deamination
0.043
-
NADP+
Sphaerostilbe repens
-
oxidative deamination
0.044
-
NADP+
-
oxidative deamination
0.045
-
NADP+
-
oxidative deamination
0.045
-
NADP+
-
28C
0.05
-
NADP+
-
oxidative deamination
0.053
-
NADP+
-
oxidative deamination
0.06
-
NADP+
-
oxidative deamination at 60C
0.061
-
NADP+
-
oxidative deamination
0.0819
-
NADP+
P00370
mutant K292Q, pH 8.0, temperature not specified in the publication
0.088
-
NADP+
-
pH 9.0, 50C
0.11
-
NADP+
-
oxidative deamination
0.117
-
NADP+
-
oxidative deamination at 33C
0.12
-
NADP+
-
oxidative deamination
0.12
-
NADP+
-
oxidative deamination
0.129
-
NADP+
P00370
mutant K286Q, pH 8.0, temperature not specified in the publication
0.163
-
NADP+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25C
0.3
-
NADP+
Thermophilic bacillus
-
oxidative deamination
0.929
-
NADP+
P00370
mutant K286Q/R289Q/R292Q , pH 8.0, temperature not specified in the publication
18.3
-
NADP+
P00370
mutant K286Q/R289Q/R292Q/S264L/S240A, pH 8.0, temperature not specified in the publication
18.4
-
NADP+
-
at 25C and pH 8
19.06
-
NADP+
P00370
mutant K286Q/R289Q/R292Q/S264L, pH 8.0, temperature not specified in the publication
0.003
-
NADPH
-
reductive amination
0.004
-
NADPH
-
reductive amination
0.007
-
NADPH
Q8ILF7, Q8ILT0
pH 7.0, 25C, recombinant enzyme
0.0087
-
NADPH
-
reductive amination
0.0097
-
NADPH
-
reductive amination
0.01
-
NADPH
-
reductive amination
0.011
-
NADPH
-
28C
0.0113
-
NADPH
-
reductive amination, Gdh1p gene
0.012
-
NADPH
-
pH 7.6, 60C
0.012
-
NADPH
Q8ILF7, Q8ILT0
pH 7.0, 25C, recombinant enzyme
0.017
-
NADPH
-
reductive amination
0.017
-
NADPH
A3MWK6
pH 9.5, 50C, recombinant enzyme
0.018
-
NADPH
-
reductive amination at 25C
0.02
-
NADPH
-
reductive amination at 60C
0.02
-
NADPH
-
reductive amination
0.021
-
NADPH
-
pH 8.0, 25C
0.022
-
NADPH
-
pH 8.3, 50C
0.022
-
NADPH
-
reductive amination at 50C
0.024
-
NADPH
-
reductive amination
0.027
-
NADPH
-
reductive amination
0.027
-
NADPH
-
reductive amination
0.028
-
NADPH
-
reductive amination
0.03
-
NADPH
-
reductive amination at 25C
0.0331
-
NADPH
-
reductive amination, Gdh3p gene
0.035
-
NADPH
-
reductive amination
0.04
-
NADPH
-
reductive amination
0.044
-
NADPH
-
reductive amination at 30C
0.049
-
NADPH
-
reductive amination
0.049
-
NADPH
Sphaerostilbe repens
-
reductive amination
0.053
-
NADPH
Thermophilic bacillus
-
reductive amination
0.055
-
NADPH
-
28C
0.06
-
NADPH
-
wild-type EcGDH, Vmax: 503 micromol/min/mg, pH 8.0, 25C
0.064
-
NADPH
-
reductive amination
0.066
-
NADPH
-
reductive amination at 80C
0.07
-
NADPH
-
reductive amination
0.074
-
NADPH
-
reductive amination at 33C
0.075
-
NADPH
-
reductive amination at 70C
0.078
-
NADPH
-
reductive amination
0.083
-
NADPH
-
reductive amination
0.095
-
NADPH
-
reductive amination
0.11
-
NADPH
-
reductive amination
0.125
-
NADPH
-
pH 7.0, 38.5C, DELTA40N-homohexamer
0.14
-
NADPH
-
reductive amination at 80C
0.14
-
NADPH
-
pH 7.0, 38.5C, alpha-homohexamer
0.26
-
NADPH
-
pH 7.0, 38.5C, beta-homohexamer
0.28
-
NADPH
-
pH 9.0, 50C
0.34
-
NADPH
-
pH 8.0, 30C, recombinant enzyme
0.51
-
NADPH
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 2180 micromol/min/mg, pH 8.0, 25C
59.7
-
NADPH
-
at 25C and pH 8
0.00056
-
NH3
-
recombinant enzyme, reductive amination
0.00065
-
NH3
-
wild-type enzyme, reductive amination
1.16
-
NH3
-
pH 8.0, 30C, recombinant enzyme
1.89
-
NH3
-
in the presence of 20 mM 2-oxoglutarate, at 25C and pH 8
2.2
-
NH3
A3MWK6
pH 9.5, 50C, recombinant enzyme
2.47
-
NH3
-
in the presence of 5 mM 2-oxoglutarate, at 25C and pH 8
2.5
3
NH3
-
in the presence of 2.5 mM 2-oxoglutarate, at 25C and pH 8
5
-
NH3
-
reductive amination, Gdh3p gene
5.96
-
NH3
-
reductive amination, Gdh1p gene
16
-
NH3
-
pH 8.0, 25C
83
-
NH3
-
pH 8.3, 50C
0.37
-
NH4+
-
reductive amination
0.63
-
NH4+
-
reductive amination at 80C
0.95
-
NH4+
-
28C
1.05
-
NH4+
-
28C
1.1
-
NH4+
-
reductive amination
1.7
-
NH4+
-
reductive amination
2
-
NH4+
-
reductive amination
2.1
-
NH4+
-
reductive amination at 33C
2.2
-
NH4+
-
reductive amination at 25C
2.2
-
NH4+
-
reductive amination
2.5
3
NH4+
-
wild-type EcGDH, Vmax: 298 micromol/min/mg, pH 8.0, 25C
2.6
-
NH4+
Sphaerostilbe repens
-
reductive amination, biphasic kinetics
3.3
-
NH4+
-
reductive amination alpha-isoenzyme, depending on NADPH-concentration
3.7
-
NH4+
-
reductive amination
4.2
-
NH4+
-
reductive amination at 25C
6.5
-
NH4+
-
reductive amination
6.6
-
NH4+
-
pH 7.0, 38.5C, alpha-homohexamer
6.76
-
NH4+
-
reductive amination
7.5
-
NH4+
-
reductive amination at 56C
7.7
-
NH4+
-
reductive amination
9
-
NH4+
-
reductive amination
9.2
-
NH4+
-
reductive amination
10
-
NH4+
-
reductive amination
10.8
-
NH4+
-
pH 7.0, 38.5C, DELTA40N-homohexamer
15.5
-
NH4+
-
reductive amination at 80C
16.6
-
NH4+
-
reductive amination
20
-
NH4+
-
reductive amination
21
-
NH4+
Thermophilic bacillus
-
reductive amination
21.2
-
NH4+
Sphaerostilbe repens
-
biphasic kinetics; reductive amination
22
-
NH4+
-
reductive amination
30.8
-
NH4+
-
reductive amination
36
-
NH4+
-
reductive amination
66
-
NH4+
-
reductive amination
75
-
NH4+
-
reductive amination beta-isoenzyme
80
-
NH4+
-
pH 7.0, 38.5C, beta-homohexamer
83
-
NH4+
-
reductive amination at 50C
304
-
NH4+
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 1960 micromol/min/mg, pH 8.0, 25C
416
-
NH4+
-
reductive amination
2.5
-
NH4Cl
-
reductive amination
4
-
NH4Cl
-
reductive amination at 60C
4
-
NH4Cl
-
reductive amination
4
-
NH4Cl
-
reductive amination at 60C
4.56
-
NH4Cl
-
reductive amination
5.96
-
NH4Cl
-
reductive amination at 30C
119
-
NH4Cl
-
reductive amination at 70C
1349
-
L-glutamate
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25C
additional information
-
additional information
-
kinetic analysis, overview, the isozyme GDHI' shows negative cooperativity with NH4+ substrate, with a decreased affinity for NH4Cl
-
additional information
-
additional information
-
kinetic analysis, overview, the isozymes show negative cooperativity with NH4+ substrate, with a decreased affinity for NH4Cl
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
25
-
2-oxoglutarate
Q8ILF7, Q8ILT0
pH 7.0, 25C, recombinant enzyme
53.33
-
2-oxoglutarate
Q8ILF7, Q8ILT0
pH 7.0, 25C, recombinant enzyme
95
-
2-oxoglutarate
A3MWK6
pH 9.5, 50C, recombinant enzyme
0.367
-
L-glutamate
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
13
-
L-glutamate
A3MWK6
pH 10.5, 50C, recombinant enzyme
78.33
-
L-glutamate
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
1.5
-
NAD+
-
pH 9.0, 50C
6144
-
NADH
-
pH 9.0, 50C
2.5
-
NADP+
P00370
mutant K286Q/R289Q/R292Q/S264L, pH 8.0, temperature not specified in the publication
6.9
-
NADP+
P00370
mutant K286Q/R289Q/R292Q/S264L/S240A, pH 8.0, temperature not specified in the publication
9.9
-
NADP+
A3MWK6
pH 10.5, 50C, recombinant enzyme
24
-
NADP+
P00370
mutant K286Q/R289Q/R292Q, pH 8.0, temperature not specified in the publication
34.2
-
NADP+
P00370
mutant K286Q, pH 8.0, temperature not specified in the publication
37.3
-
NADP+
P00370
wild-type enzyme, pH 8.0, temperature not specified in the publication
37.6
-
NADP+
P00370
mutant K289Q, pH 8.0, temperature not specified in the publication
47.3
-
NADP+
P00370
mutant K292Q, pH 8.0, temperature not specified in the publication
2136
-
NADP+
-
pH 9.0, 50C
92
-
NADPH
A3MWK6
pH 9.5, 50C, recombinant enzyme
1100
-
NADPH
Sphaerostilbe repens
-
-
28650
-
NADPH
-
pH 9.0, 50C
100
-
NH3
A3MWK6
pH 9.5, 50C, recombinant enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
14.67
-
2-oxoglutarate
Q8ILF7, Q8ILT0
pH 7.0, 25C, recombinant enzyme
2883
56
-
2-oxoglutarate
A3MWK6
pH 9.5, 50C, recombinant enzyme
2883
1250
-
2-oxoglutarate
Q8ILF7, Q8ILT0
pH 7.0, 25C, recombinant enzyme
2883
0.75
-
L-glutamate
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
12211
3.8
-
L-glutamate
A3MWK6
pH 10.5, 50C, recombinant enzyme
12211
6
-
L-glutamate
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
12211
0.00000013
-
NADP+
P00370
mutant K286Q/R289Q/R292Q/S264L, pH 8.0, temperature not specified in the publication
27497
0.00000038
-
NADP+
P00370
mutant K286Q/R289Q/R292Q/S264L/S240A, pH 8.0, temperature not specified in the publication
27497
0.0000258
-
NADP+
P00370
mutant K286Q/R289Q/R292Q, pH 8.0, temperature not specified in the publication
27497
0.000115
-
NADP+
P00370
mutant K289Q, pH 8.0, temperature not specified in the publication
27497
0.000265
-
NADP+
P00370
mutant K286Q, pH 8.0, temperature not specified in the publication
27497
0.000578
-
NADP+
P00370
mutant K292Q, pH 8.0, temperature not specified in the publication
27497
0.00203
-
NADP+
P00370
wild-type enzyme, pH 8.0, temperature not specified in the publication
27497
280
-
NADP+
A3MWK6
pH 10.5, 50C, recombinant enzyme
27497
5400
-
NADPH
A3MWK6
pH 9.5, 50C, recombinant enzyme
27498
45
-
NH3
A3MWK6
pH 9.5, 50C, recombinant enzyme
14472
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
202
-
2,4-Pyridinedicarboxylate
-
-
9.2
-
2-Methyleneglutarate
-
-
0.45
-
2-oxoglutarate
-
competitive
5.6
-
glutamate
-
competitive inhibitor
6.9
-
Isophthalate
-
-
additional information
-
additional information
-
Ki values for isophthalate with isozyme from differently grown strains in forward and reverse reactions, overview
-
additional information
-
additional information
-
Ki values for isophthalate with different isozymes from differently grown strains in forward and reverse reactions, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0252
-
Bithionol
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
0.12
-
Bithionol
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
0.139
-
GW5074
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
0.15
-
GW5074
Q8ILF7, Q8ILT0
pH 8.0, 25C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.29
-
-
host human adult, reductive amination at 30C and pH 6.5
0.31
-
-
host human infant, reductive amination at 30C and pH 6.5
0.33
-
-
wild-type EcGDH using NAD+ as coenzyme
0.34
-
-
host chicken, reductive amination at 30C and pH 6.5
0.37
-
-
crude extract
0.4
-
-
reductive amination at 30C and pH 6.5
0.45
-
-
host calf, reductive amination at 30C and pH 6.5
0.49
-
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NAD+ as coenzyme
0.59
-
-
host rat, reductive amination at 30C and pH 6.5
0.62
-
-
strain parvolorum, reductive amination at 30C and pH 6.5
0.7
-
-
reductive amination at 30C and pH 6.5
0.7
-
-
host pig; reductive amination at 30C and pH 6.5
0.8
-
-
strain liberorum, reductive amination at 30C and pH 6.5
1.1
-
-
strain breve a, reductive amination at 30C and pH 6.5
1.16
-
-
strain infantis a, reductive amination at 30C and pH 6.5
1.68
-
-
oxidative deamination
2.17
-
-
crude extract
2.54
-
-
reductive amination
4
-
Q8ILF7, Q8ILT0
deamination, pH 8.0, 25C, recombinant enzyme
4.9
-
-
unpurified supernatant, at 25C in 0.1 M potassium phosphate containing 100 mM L-glutamate and 0.5 mM NADP+ at pH 8
5.64
-
-, Q2WCS9
strain DPPMA49, pH 8.0, 37C, comparison to activity in diverse other DPPMA strains of Lactobacillus plantarum and to other Lactobacilli, overview
7
-
-
purified enzyme
8.2
-
-
reductive amination at 33C
9
-
Q8ILF7, Q8ILT0
deamination, pH 8.0, 25C, recombinant enzyme
9.2
-
-
reductive amination
10.3
-
-
oxidative deamination at 50C and pH 8.2
10.92
-
-
reductive amination
18.4
-
-
oxidative deamination at 25C
24.3
-
-
oxidative deamination at 50C and pH 8.2
28
-
Q8ILF7, Q8ILT0
amination, pH 8.0, 25C, recombinant enzyme
32.8
-
-
pH 9.0, 50C
32.9
-
-
reductive amination at 30C
36.5
-
-
after 7.4fold purification, at 25C in 0.1 M potassium phosphate containing 100 mM L-glutamate and 0.5 mM NADP+ at pH 8
40
-
-
T138E-mutant
46.2
-
Thermophilic bacillus
-
reductive amination at 55C
51.2
-
-
reductive amination
57.6
-
-
reductive amination
58
-
-
chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH using NADP+ as coenzyme
59.4
-
-
purified enzyme
60
-
-
reductive amination at 40C
61
-
Q8ILF7, Q8ILT0
amination, pH 8.0, 25C, recombinant enzyme
63
-
-
wild-type EcGDH using NADP+ as coenzyme
74.5
-
-
oxidative deamination at pH 7.0 and 70C
78
-
-
reductive amination at 20C
80
-
-
E158Q-mutant
80.2
-
-
reductive amination
85
-
-
oxidative deamination at 80C and pH 8.0
121
-
-
reductive amination at 30C
133
-
-
reductive amination at 37C and pH 6.7
180
-
-
oxidative deamination at 25C
194.3
-
-
oxidative deamination at 75C
204.1
-
-
oxidative deamination at 20C
231
-
-
oxidative deamination at 25C
250
-
-
oxidative deamination
388
-
-
reductive amination
416
-
-
reductive amination at 30C
464
-
-
oxidative deamination at 80C and pH 7.54
930
-
-
reductive amination at 37C
1140
-
-
reductive amination at pH 7.5 and 60C
2500
-
-
wild-type
2940
-
-
reductive amination at 80C and pH 7.54
additional information
-
Q9HFR6
exhibits highest NADP-GDH specific activity among fungi under survey
additional information
-
-
late-exponential-phase cells are used for this study since they show a higher activity of GDH compared with early exponential-phase cells
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-, Q2WCS9
strain DPPMA49 shows highest enzyme activity under condition 13C, pH 5.5, NaCl 5.62%
6.7
-
-
reductive amination
6.7
-
-
reductive amination
6.9
-
Sphaerostilbe repens
-
reductive amination
7
-
-
reductive amination and oxidative deamination
7
-
-
oxidative deamination
7
-
-
oxidative deamination
7
-
-
enzyme from mycelium and yeast
7
-
Q8ILF7, Q8ILT0
amination, assay at; amination, assay at
7.2
-
-
reductive amination
7.2
-
Thermophilic bacillus
-
reductive amination
7.4
7.6
-
oxidative deamination
7.4
-
-
reductive amination at 50C
7.5
8
-
reductive amination
7.5
-
-
reductive amination
7.5
-
-
reductive amination
7.5
-
-
reductive amination
7.5
-
-
reductive amination
7.5
-
-
reductive amination
7.5
-
-
reductive amination in potassium phosphate buffer
7.5
-
-
reductive amination
7.6
-
-
reductive amination
7.6
-
-
assay at
7.7
-
-
reductive amination
7.8
-
-
reductive amination
7.8
-
-
assay at
7.9
-
-
reductive amination
8
8.5
-
reverse reaction, assay at
8
-
-
oxidative deamination at 80C
8
-
-
oxidative deamination at 60C
8
-
-
oxidative deamination at 20C
8
-
-
oxidative deamination at 60C
8
-
-
reductive amination
8
-
-
reductive amination in Tris hydrochloride buffer
8
-
-
oxidative deamination
8
-
-
reductive amination
8
-
-
reductive amination
8
-
-
reductive amination
8
-
-
reductive amination
8
-
-
reductive amination
8
-
-
aminating activity
8
-
-
for reductive amination
8
-
-
assay at
8
-
-
reductive amination
8
-
-
assay at
8
-
-
assay at
8
-
P00370
assay at
8
-
Q8ILF7, Q8ILT0
deamination, assay at; deamination, assay at
8
-
-
assay at
8.1
8.4
-
amination of 2-oxoglutarate. Determined at 50C in 125 mM glycylglycine/NaOH buffer
8.1
8.4
-
reductive amination at 50C
8.2
-
-
oxidative deamination at 50C
8.3
8.7
-
deamination of L-glutamate. Determined at 50C in 125 mM glycylglycine/NaOH buffer
8.3
8.7
-
oxidative deamination at 50C
8.3
-
-
reductive amination and oxidative deamination
8.4
-
-
reductive amination at 60C
8.4
-
-
reductive amination
8.4
-
Sphaerostilbe repens
-
oxidative deamination
8.4
-
Thermophilic bacillus
-
oxidative deamination
8.5
-
-
reductive amination
8.5
-
-
oxidative deamination
8.5
-
-
reductive amination
8.5
-
-
reductive amination reaction
8.6
-
-
oxidative deamination
8.6
-
-
oxidative deamination
8.8
9.8
-
oxidative deamination
9
10
-
deaminating activity
9
-
-
oxidative deamination
9
-
-
reductive amination at 20C
9
-
-
oxidative deamination
9
-
-
oxidative deamination
9
-
-
oxidative deamination
9
-
-
oxidative deamination
9
-
-
oxidative deamination
9
-
-
for oxidative deamination
9
-
A3MWK6
reductive deamination
9.3
-
-
oxidative deamination
9.3
-
-
oxidative deamination
9.5
-
-
oxidative deamination
9.5
-
-
forward reaction, assay at
9.5
-
A3MWK6
oxidative deamination
9.6
10
-
reductive amination
9.75
-
-
oxidative deamination reaction
10
-
-
oxidative deamination
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
10
-
fully active after 60 min
4
9
-
above pH 9 or below 4.0 no activity
5
10
-
fully active
8.5
10
-
pH 8.5: about 60% of maximal activity, pH 10.0: about 40% of maximal activity
additional information
-
-, Q2WCS9
optimal enzyme production conditions and activity profile, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
13
-
-, Q2WCS9
strain DPPMA49 shows highest enzyme activity under condition 13C, pH 5.5, NaCl 5.62%
25
-
-
assay at
25
-
Q8ILF7, Q8ILT0
amination, assay at; assay at
28
-
-
enzyme from mycelium
28
-
-
assay at
28
-
-
assay at
30
-
-
assay at
32
-
-
enzyme from yeast
34
-
-
reductive amination
50
-
-
assay at 50C because of instability of NADP+ under assay conditions
50
-
A3MWK6
assay at
55
-
-
T158E-mutant
56
-
-
reductive amination
58
-
-
S128R-mutant
60
-
-
S128R/T158E/S160E-mutant
60
-
-
E158Q-mutant
60
-
-
reductive amination
60
-
-
reductive amination and oxidative deamination
60
-
-
reductive amination
60
-
-
reductive amination and oxidative deamination
60
-
-
alpha-hexamer and beta-hexamer
60
-
-
assay at
63
-
-
N117R-mutant and S128R/T158E/N117R/S160E-mutant
65
-
-
wild-type and S128R/T158E-mutant
65
-
-
DELTA40N-homohexamer
68
-
-
S128R/T158E/N117R-mutant
75
-
-
reductive amination
80
-
-
reductive amination
80
-
-
oxidation of glutamate
85
-
-
T138E-mutant
85
-
-
assay at
95
-
-
oxidative deamination
95
-
-
reductive amination
95
-
-
oxidative deamination
95
-
-
reductive amination
100
-
-
oxidative deamination
100
-
-
maximum activity in L-glutamate deamination
100
-
-
oxidative deamination
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
35
-
15C: about 55% of maximal activity, 35C: about 25% of maximal activity
50
100
-
the activity of the enzyme increases with an increase in temperature from 50 to 100C. The highest activity is observed at 100C and is about 15 times than that at 50C
50
70
-
50C: about 65% of maximal activity, 70C: about 85% of maximal activity
50
70
-
50C: alpha-homohexamer shows about 65% of maximal activity, beta-homohexamer shows about shows about 70% of maximal activity, DELTA40N-homohexamer shows about 55% of maximal activity. 70C: alpha-homohexamer shows about 90% of maximal activity, beta-homohexamer shows about 60% of maximal activity, DELTA40N-homohexamer shows about 80% of maximal activity
additional information
-
-
no temperature dependence
additional information
-
-, Q2WCS9
optimal enzyme production conditions and activity profile, overview
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
isoelectrofocusing
7.48
-
Q8ILF7, Q8ILT0
sequence calculation
9.09
-
Q8ILF7, Q8ILT0
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
isophthalate as a sole source of carbon and energy. Strain ISP4 produces a single form of NADP-GDH, GDHI' when it is grown on either isophthalate or rich medium 2YT
Manually annotated by BRENDA team
-
isophthalate as a sole source of carbon and energy. Strain PP4 shows carbon source-dependent modulation of NADP-GDH. GDHI is produced when cells are grown on isophthalate
Manually annotated by BRENDA team
Acinetobacter lwoffii ISP4
-
isophthalate as a sole source of carbon and energy. Strain ISP4 produces a single form of NADP-GDH, GDHI' when it is grown on either isophthalate or rich medium 2YT
-
Manually annotated by BRENDA team
-
two different enzymes in yeast and in mycelium cells
Manually annotated by BRENDA team
Aspergillus niger NCIM 565, Aspergillus oryzae NCIM 553, Aspergillus terreus NCIM 656, Cenococcum geophilum H5-3, Emericella nidulans NCIM 1211
-
-
-
Manually annotated by BRENDA team
-
BE(2)C neuroblastoma cells
Manually annotated by BRENDA team
-
two different enzymes in yeast and in mycelium cells
Manually annotated by BRENDA team
Pseudomonas aeruginosa PP4
-
isophthalate as a sole source of carbon and energy. Strain PP4 shows carbon source-dependent modulation of NADP-GDH. GDHI is produced when cells are grown on isophthalate
-
Manually annotated by BRENDA team
additional information
-
ubiquitously expressed in various tissues
Manually annotated by BRENDA team
additional information
-, Q2WCS9
strain DPPMA49 shows the highest NADP-GDH activity under temperature, pH and NaCl values found during cheese ripening. Enzyme production conditions and activity profiles, overview
Manually annotated by BRENDA team
additional information
Lactobacillus plantarum DPPMA49
-
strain DPPMA49 shows the highest NADP-GDH activity under temperature, pH and NaCl values found during cheese ripening. Enzyme production conditions and activity profiles, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Q8ILF7, Q8ILT0
GDH2 co-localizes with the acyl carrier protein
Manually annotated by BRENDA team
Lactobacillus plantarum DPPMA49
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
49000
-
C6EVR5, -
predicted from cDNA
50000
-
-
SDS-PAGE
170000
-
-
isozymes GDHI and GDHII, gel filtration
200000
-
-
gel filtration
204000
-
-
gel filtration
208000
-
-
gel filtration
212000
-
-
sedimentation equilibrium and sedimentation velocity and diffusion coefficient
230000
-
-
gel filtration
245000
-
-
gel filtration
245500
-
-
gel filtration
250000
-
-
isozyme GDHI', gel filtration
263000
-
-
gel filtration
263000
-
-
gel filtration
270000
-
-
sucrose-density-gradient centrifugation
270000
-
-
gel filtration, expressed in Escherichia coli
270000
-
-
gel filtration
270000
-
-
gel filtration, expressed in Escherichia coli
270000
-
-
gel filtration
270000
-
A3MWK6
gel filtration, tagged recombinant enzyme
275000
-
-
gel filtration
280000
-
-
gel filtration
280000
-
-
gel filtration
280000
-
Sphaerostilbe repens
-
non-denaturating PAGE
280000
-
-
gel filtration
284000
-
-
gel filtration
285000
-
-
gel filtration
290000
-
-
gel filtration
291000
-
-
sucrose-density-gradient centrifugation
294000
-
-
gel filtration
300000
-
-
gel filtration
300000
-
-
gel filtration
300000
-
-
sedimentation equilibrium
300000
-
-
gel filtration
300000
-
-
gel filtration
300000
-
Q8ILF7, Q8ILT0
recombinant enzyme, gel filtration
310000
-
-
gel filtration
315000
-
-
gel filtration
320000
-
-
gel filtration
330000
-
-
gel filtration
339000
-
-
gel filtration
350000
-
-
gel filtration
350000
-
-
gel filtration
350000
-
-
FPLC on a Superdex G-75 column
360000
-
-
gel filtration
400000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 47000, gel filtration; x * 47169, amino acid analysis
?
-
x * 46170, amino acid analysis
?
-
x * 53000, SDS-PAGE, beta-holoenzyme; x * 55500, SDS-PAGE, alpha-holoenzyme
?
-
x * 40000, SDS-PAGE
?
-
x * 46000, SDS-PAGE
?
-
x * 48000, SDS-PAGE
?
Escherichia coli MRE
-
x * 46000, SDS-PAGE
-
hexamer
-
6 * 46000, SDS-PAGE
hexamer
-
6 * 52000, SDS-PAGE
hexamer
-
6 * 44000, SDS-PAGE
hexamer
-
crystallography
hexamer
-
x * 50000, SDS-PAGE
hexamer
-
6 x 50000, SDS-PAGE
hexamer
-
native PAGE
hexamer
A3MWK6
6 * 47700, tagged recombinant enzyme, SDS-PAGE
hexamer
P00370
EcGDH is a hexamer with 32 symmetry, an assembly. Protomer F (EcGDH-F) is the only molecule in the hexamer that adopts an open conformation that is sufficiently wide for diffusion of both substrate and cofactor, structure comparison to the enzyme from Clostridium symbiosum and other GDHs, overview
hexamer
Q8ILF7, Q8ILT0
6 * 52546, GDH1, sequence calculation; 6 * 54024, GDH2, sequence calculation
hexamer
Aspergillus niger NCIM 565
-
x * 50000, SDS-PAGE
-
hexamer
Klebsiella pneumoniae F-5-2
-
6 * 52000, SDS-PAGE
-
hexamer
-
6 * 47700, tagged recombinant enzyme, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 45000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * ?, crystallization
homohexamer
-
alpha6, 6 * 45000, SDS-PAGE, expressed in Escherichia coli
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE; alpha6, 6 * 49285, amino acid analysis
homohexamer
-
alpha6, 6 * 46000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47300, SDS-PAGE
homohexamer
-
alpha6, 6 * 46500, SDS-PAGE; alpha6, 6 * 50120, MALDI-TOF
homohexamer
-
alpha6, 6 * 46000, SDS-PAGE
homohexamer
-
alpha6, 6 * 48000, CTAB-PAGE; alpha6, 6 * 55000, SDS-PAGE
homohexamer
-
alpha6, 6 * 52000, SDS-PAGE
homohexamer
-
alpha6, 6 * 56000, SDS-PAGE
homohexamer
-
alpha6, 6 * 43000, SDS-PAGE
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE
homohexamer
-
alpha6, 6 * 44500, SDS-PAGE
homohexamer
-
alpha6, 6 * 52000, SDS-PAGE
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
homohexamer
-
alpha6, 6 * 56000, SDS-PAGE
homohexamer
-
alpha6, 6 * 50000, SDS-PAGE
homohexamer
Sphaerostilbe repens
-
alpha6, 6 * 48000, SDS-PAGE
homohexamer
-
alpha6, 6 * 40000, SDS-PAGE
homohexamer
-
alpha6, 6 * 50000, SDS-PAGE
homohexamer
-
4 * 43000, isozyme GDHI', SDS-PAGE
homohexamer
Acinetobacter lwoffii ISP4
-
4 * 43000, isozyme GDHI', SDS-PAGE
-
homohexamer
-
alpha6, 6 * 52000, SDS-PAGE
-
homohexamer
Lactobacillus fermentum IFO 3071
-
alpha6, 6 * 50000, SDS-PAGE
-
homohexamer
Mycobacterium smegmatis CDC46
-
alpha6, 6 * 40000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 48000, SDS-PAGE
-
homohexamer
Penicillium chrysogenum NCAIM 00237
-
alpha6, 6 * 56000, SDS-PAGE
-
homohexamer
-
alpha6, 6 * 47000, SDS-PAGE; alpha6, 6 * 49285, amino acid analysis
-
homotetramer
-
alpha4, 4 * 47000, SDS-PAGE
homotetramer
-
alpha4, 4 * 49000, SDS-PAGE
homotetramer
-
alpha4, 4 * 46000, SDS-PAGE
homotetramer
-
alpha4, 4 * 53500, SDS-PAGE
homotetramer
-
4 * 64000, SDS-PAGE
homotetramer
-
4 * 43000, isozymes GDHI and GDHII, SDS-PAGE
homotetramer
Pseudomonas aeruginosa PP4
-
4 * 43000, isozymes GDHI and GDHII, SDS-PAGE
-
additional information
P00370
modelling of NADP+ in domain II reveals the potential contribution of positively charged residues from a neighbouring alpha-helical hairpin to phosphate recognition, sequence-structure relationship, overview
additional information
Q8ILF7, Q8ILT0
the subunit interactions are mediated by networks of salt bridges and hydrogen bonds, monome-monomer interaction, overview; the three-dimensional structure of hexameric PfGDH2 is solved to 3.1 A resolution, overview. The subunit interactions are mainly assisted by hydrogen bonds and hydrophobic interactions, monome-monomer interaction, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
phosphoprotein
-
phosphorylation increases the activity of the mycelial form of the enzyme. The yeast enzyme remains unaffected. The yeast-form specific native NADP-GDH is in active phosphorylated form. In mycelium the native enzyme is in dephosphorylated inactive form
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
purified GDH in the absence of reactants, hanging drop vapour diffusion method, mixing of 10 mg/ml protein in 20 mM Tris-HCl, pH 7.6, with 15-25% PEG 3350, Tris/HEPES, pH 70-8.0, and 0.2 M NaCl, 18C, 2 days, X-ray diffraction structure determination and analysis at 2.5 A resolution, modelling
P00370
three non-isomorphous crystal forms, all belong to orthorhombic system, homohexamers, one grown from ammonium sulfate, two from L-glutamate, 3.0 A resolution
-
plate-like crystals of monoclinic space group C2 grown by vapour-diffusion using the sitting-drop method, X-ray crystallography to a resolution of 2.7 A
-
purified recombinant detagged GDH2, 0.0025 ml of 16 mg/ml protein in 100 mM Tris, 500 mM NaCl, pH 7.8, mixed with 0.0025 ml of reservoir solution containing 0.2 M magnesium chloride hexahydrate, 0.1 M Tris/HCl pH 8.5, 30% PEG 4000 including 0.01 M spermine tetra HCl droplet concentration and 10 mM glutamate, X-ray diffraction structure determination and analysis at 3.1 A resolution
Q8ILF7, Q8ILT0
dialysis against ammonium sulfate solution
-
cofactor binding domain of glutamate dehydrogenase, sitting-drop vapor diffusion method. X-ray structure of the domain of wild-type enzyme and mutant enzyme R190A/E231A/K193A is solved at 1.43 A
-
quadruple mutant S128R/T158E/N117R/S160E, homohexamer, 2.9 A resolution
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
9.5
A3MWK6
Pcal_1606 retains more than 80% of its activity after incubation for 30 min at pH 4.5-9.5 at 50C
4.7
-
Thermophilic bacillus
-
inactivation
5.5
11.5
-
stable
5.8
9
Thermophilic bacillus
-
highly thermostable
6
9
-
unstable below pH 5.0 or above pH 10.0
additional information
-
-
Gdh3-encoded enzyme undergoes in vitro deamination at a particular asparaginyl residue which is absent in homologous isoenzyme, Gdh1p. Deamination of Asn54 is observed in vitro when Gdh3p is incubated at alkaline pH. The specific deamination of Asn54, could account, in part, for the relative lower stability of the GDH3-encoded protein
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
-
-
inactivated by freezing
20
-
Sphaerostilbe repens
-
stable for 15 h
25
-
-
12% activity loss after 1 h
30
-
-
30 min, stable
37
-
-
72% activity loss after 1 h
37
-
-
60 min, yeast enzyme retains 41% of its activity, mycelial enzyme retains 9% of its activity
37
-
-
20 h, stable
40
55
-
30 min, stable
40
-
-
30 min, about 10% loss of activity
45
-
-
maximal temperature for activity, 60 min stable
50
-
-
irreversible heat inactivation
50
-
-
10 min stable
50
-
-
irreversible heat inactivation
50
-
-
pH 8.0, 10 min, maintains more than 90% activity
50
-
-
stable at
55
-
-
complete activity loss after 1 h
55
-
-
9% activity loss after 5 min
57
-
-
after 1 h stable
60
-
-
irreversible inactivation
61
-
-
50% activity after 5 min
65
-
-
at 4.3 M NaCl stable for several h
66
-
-
50% activity after 5 min
70
-
-
complete inactivation
70
-
-
after 25 min 10% activity
70
-
-
after 10 min in phosphate buffer pH 7.4 100% activity
70
-
Thermophilic bacillus
-
after 300 min 60% activity
72
-
-
complete inactivation
75
-
-
after 2 min 50% activity
80
-
-
50% activity after 4 h
80
-
-
30 min, complete loss of activity
80
-
Q8ILF7, Q8ILT0
purified enzyme, 10 min, stable
85
-
-
no activity loss after 5 h
85
-
-
quadruple mutant 50% activity after 5 min; wild-type 50% activity after 209 min
85
-
-
recombinant enzyme retains 90% activity after 3 h of incubation; wild-type enzyme retains 100% activity after 3 h of incubation
85
-
-
recombinant enzyme fully active after 30 min
90
-
-
fully active after 5 h
90
-
-
50% activity after 1 h
90
-
-
50% activity after 12.5 h in 0.1 M NaH2PO4/Na2HPO4
90
-
-
20 h, stable
90
-
A3MWK6
Pcal_1606 retains full activity after incubation for 10 min at temperatures up to 90C
95
-
-
30 min, the enzyme retains its full activity
95
-
-
fully active after 30 min
98
-
-
50% activity after 2 h
98
-
-
recombinant enzyme retains 50% activity after 1.5 h of incubation; wild-type enzyme retains 50% activity after 6.4 h of incubation
100
-
-
50% activity after 140 min
100
-
-
74% activity after 5 h
100
-
-
30 min, 5% loss of activity
100
-
-
fully active after 30 min
100
-
-
wild-type and T138E 50% activity after 2 h and 3 h respectively
100
-
-
50% activity after 140 min
100
-
-
half-life: 12 h
102
-
-
50% activity after 55 min
105
-
-
50% activity after 20 min
105
-
-
full activity after 10 min, 50% activity after 90 min
105
-
-
half-life: 13 min at 5 atm, 170 min at 275 atm, 360 min at 500 atm, 470 min at 750 atm, recombinant enzyme
107
-
-
50% activity after 10 min
110
-
-
half-life: 25 min
115
-
-
10 min, complete loss of activity
115
-
-
inactivation after 10 min
115
-
-
inactivation after 10 min
additional information
-
-
time-dependent changes in the activity of NADP-GDH at 60C are analysed: GDHII loses activity completely within 10 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
inactivated by freezing, less than 5% activity after one freeze/thaw cycle
-
1 mg/ml bovine serum albumin stabilizes
-
K2HPO4 enhances the thermostability optimally at 1 mM concentration
-
potassium phosphate enhances the thermostability
-
after incubation with chymotrypsin enzyme loses 50% activity within 30 min and a combination of 2-oxoglutarate and NADP+ affords near complete protection against chymotrypsin
-
50% v/v glycerol and or bovine serum albumin in buffer enhances the stability, inactivated by freezing/thawing
-
Aspergillus terreus NADP-GDH remains fully active even after 2 h of incubation with chymotrypsin
-
purification under anoxically conditions, 2 mM dithiothreitol stabilizes
-
inactivated by freezing/thawing
-
in absence of salt it is irreversibly inactivated, optimal NaCl concentration is 1.1 M
-
NaCl and KCl markedly increase the thermostability
-
unstable when frozen at -20C after a few h even with addition of 50% v/v glycerol
-
elevated pressures up to 750 atm have a strong stabilizing effect on two extremely thermophilic glutamate dehydrogenases: the native enzyme from the hyperthermophile Pyrococcus furiosus, and a recombinant mutant enzyme containing an extra tetrapeptide at the C-terminus. The presence of the tetrapeptide greatly destabilizes the recombinant mutant at ambient pressure; however, the destabilizing effect is largely reversed by the application of pressure. Destabilization is due to weakened intersubunit ion-pair interactions induced by thermal fluctuations of the tetrapeptide. For both enzymes, the stabilizing effect of pressure increases with temperature as well as pressure, reaching 36fold for recombinant enzyme at 105C and 750 atm
-
the purified enzyme can withstand at least three freezing (-20C) and thawing (25C) cycles without significant effects on activity the enzyme can be lyophilzed and stored for several months without loss of activity
-
Gdh3-encoded enzyme undergoes in vitro deamination at a particular asparaginyl residue which is absent in homologous isoenzyme, Gdh1p. Deamination of Asn54 is observed in vitro when Gdh3p is incubated at alkaline pH. The specific deamination of Asn54, could account, in part, for the relative lower stability of the GDH3-encoded protein
-
2-mercaptoethanol and dithiothreitol stabilizes
Sphaerostilbe repens
-
10 mM MOPS-NaOH pH 7.1 and 0.3-0.4 M NaCl is the best buffer
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, purified enzyme, stable for about 5 to 6 months without any significant loss of activity
-
4C after 7 days, 55% activity
-
4C, stable for at least 2 months
-
4C, 2 months, no activity loss
-
4C, 1 week
-
0-4C, after 15 or 30 days, 18% or 2% activity
-
-20C, phosphate buffer at pH 7.0, 0.2 mM 2-mercaptoethanol, 20 h, complete activity loss
-
5C, phosphate buffer at pH 7.0, 2 mM 2-mercaptoethanol, 6 months, no activity loss
-
0C, at the low stock enzyme dilutions necessary for kinetic assays GDH loses activity over the duration of an experiment, at 0.01 and 0.02 mg/ml GDH retains 90-95% activity over 24 h in glass tubes, whereas this declines with decreasing storage concentration (to 87%, 71%, and 47% at concentrations of GDH of 5, 2 and 0.5 mg/ml, respectively)
-
4C, 0.1 M phosphate buffer, several days, no loss of activity
-
4C, water, 20 mM potassium phosphate or sodium phosphate, pH 7.2, at least 3 months
-
room temperature, several months stable
-
25C, 20% v/v glycerol, 476 h, 50% activity
-
fully active at 4 M concentration NaCl at room temperature for months
-
-20C, potassium phosphate buffer, pH 7.4, containing 0.01% 2-mercaptoethanol and 10% glycerol, 100% activity
-
4C, purified enzymes, stable for about 5 to 6 months without any significant loss of activity
-
-20C, 40% v/v glycerol, no activity loss
-
25C, 20 mM potassium phosphate, pH 6.5, containing 7 mM 2-mercaptoethanol and 10% glycerol, stable for several weeks
-
4C, 10 mM potassium phosphate buffer, pH 7.2, 0.1 mM EDTA, 0.1 mM DTT, 5 months, no activity loss
-
4C, 20 mM potassium phosphate, pH 6.5, containing 7 mM 2-mercaptoethanol and 10% glycerol, stable for several weeks
-
4C, 10 mM potassium phosphate buffer, pH 7.2, 0.1 mM EDTA, 0.1 mM DTT, 5 months, no activity loss
-
4C, ten days and 25C, 15 h, both 100% activity
Sphaerostilbe repens
-
4C and -25C, 0.2 M Tris/HCl buffer, pH 7.4, 24 h or 2 months respectively, 100% activity
-
0-4C, Tris-HCl buffer, pH 9.0, 2 months, 100% activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native GDHI' 142fold from cells grown on isophthalate and 510fold from cells grown on 2YT
-
under semianoxically conditions
-
by Cibacron red LS-B dye-affinity purification with a step KCl gradient elution, more than 7fold purified to homogeneity
-
purified to homogeneity using novel reactive dye-affinity resins
-
recombinant His6-tagged GdhA from Escherichia coli by nickel affinity chromatography
-
purified to homogeneity using novel reactive dye-affinity resins
-
of the alpha-subunit, beta-subunit and a truncated subunit missing 40 amino acids at their N-terminus expressed in Escherichia coli
-
by Cibacron red LS-B dye-affinity purification with a step KCl gradient elution, 17fold purified
-
ammonium sulfate fractionation, Procion Red HE-3B Sepharose CL-6B column chromatography and Q-Sepharose column chromatography
-
recombinant wild-type and mutant enzymes
P00370
using dye-affintiy chromatography and anion-exchange chromatography
-
by gel filtration
-
co-purification with glutathione disulfide reductase
-
recombinant His6-tagged GDH2 from Escherichia coli strain KRX by nickel affinity chromatography and gel filtration
Q8ILF7, Q8ILT0
native isozymes GDHI and GDHII from strain PP4 grown on isophthalate and glucose, respectively. Enzyme yields are better in the presence of 1 mM 2-oxoglutarate, 1 mM EDTA, and 4.35% glycerol. GDHI and GDHII are purified 228fold and 428fold, respectively
-
recombinant N-terminally Met-Ala-Ser-tagged and C-terminally His6-tagged enzyme from Eschericia coli strain Rosetta(DE3) by affinity chromatography and gel filtration
A3MWK6
recombinant enzyme
-
recombinant enzyme
-
-
Thermophilic bacillus
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Escherichia coli JM109
-
gene gdhA, phylogenetic analysis, expression of His6-tagged GdhA in Escherichia coli, ectopic expression in the cytoplasm of transgenic Oryza sativa plants. The introduced gdhA, together with the endogenous glutamine synthetase, directly assimilates NH4 + absorbed from the roots. NADP(H)-GDH activities in the gdhA-transgenic lines are markedly higher than those in a control line
-
full-length cDNA encoding alpha-subunit, beta-subunit and a truncated subunit missing 40 amino acids at their N-terminus, DELTA40N, expression in Escherichia coli
-
expression in Escherichia coli, hybrid proteins containing the Pyrococcus furiosus glutamate and the Clostridium difficile cofactor binding domain with reduced substrate binding affinity
Clostridium difficile
-
overexpression of the gdhA gene, which encodes NADP-GDH, can modulate nitrogen metabolism in Lycopersicon esculentum, with resultsnt increase in levels od some free amino acids, in particular glutamate, in tomato fruits
-
expressed in Escherichia coli
-
expressed in Escherichia coli strain TG1
-
sequence comparisons, expression of wild-type and mutant enzymes
P00370
gene gdh, quantitative real-time PCR expression analysis in different cheese cultures
-, Q2WCS9
overexpression with the NICE system in Lactococcus lactis TIL46 induced with increasing concentrations of nisin, pGdh442 transferred by electroporation (TIL504) or by conjugation (TIL507) in Lactococcus lactis MG1363 or in its derivative TIL193 strain containing pGhost8, appears to be stable after several subcultures of the strains without selection pressure, in the presence of plasmid pLP712, pGdh442 is unstable
-
gene msmeg_5442, semi-quantitative real-time PCR expression analysis
A0R3E3, -
gene GDH1, DNA and amino acid sequence determination and analysis, overexpression as His6-tagged protein in Escherichia coli strain KRX; gene GDH1, expression as His6-tagged enzyme in Escherichia coli strain M15, method optimization
Q8ILF7, Q8ILT0
mutant GDH transformed into competent Escherichia coli PA340 cells, which are glutamate synthase and dehydrogenase-deficient
-
gene pcal_1606, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of N-terminally Met-Ala-Ser-tagged and C-terminally His6-tagged enzyme in Eschericia coli strain Rosetta(DE3)
A3MWK6
expression in Escherichia coli, hybrid proteins containing the Pyrococcus furiosus glutamate and the Clostridium difficile cofactor binding domain with reduced substrate binding affinity
-
genes GDH1 and GDH3, recombinant expression of FLAG-tagged wild-type and mutant GDH1 and GDH3 in yeast cells
-
expression in Escherichia coli DH5alpha under the control of a highly constitutive expresion promoter in a pHCE system
-
expression in Escherichia coli BL21
-
expression in Escherichia coli BL21
-
expressed in Escherichia coli
C6EVR5, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
GDH expression of strain DPPMA49 is downregulated by temperature below 13C, expression analysis
-, Q2WCS9
GDH expression of strain DPPMA49 is upregulated by NaCl at 1.87-5.62%
-, Q2WCS9
GDH expression of strain DPPMA49 is downregulated by temperature below 13C, expression analysis
Lactobacillus plantarum DPPMA49
-
-
GDH expression of strain DPPMA49 is upregulated by NaCl at 1.87-5.62%
Lactobacillus plantarum DPPMA49
-
-
enzyme expression is upregulated under N2-starvation, overview
A0R3E3, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
K286Q
P00370
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q
P00370
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
K286Q/R289Q/R292Q/S264L
P00370
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
R289Q
P00370
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
K419A
-
site-directed mutagenesis of GDH1
K420A
-
site-directed mutagenesis of GDH1
K423A
-
site-directed mutagenesis of GDH1
K419A
-
site-directed mutagenesis of GDH1
-
K420A
-
site-directed mutagenesis of GDH1
-
K423A
-
site-directed mutagenesis of GDH1
-
E158Q
-
3.3% as active as wild-type
T138E
-
1.6% as active as wild-type
N117R
-
80% activity of wild-type at optimum temperature for catalysis
R190A/E231A/K193A
-
mutation has no effect on the overall conformation of the protein
S128R
-
same activity as wild-type at optimum temperature for catalysis
S128R/T158E
-
120% activity of wild-type at optimum temperature for catalysis
S128R/T158E/N117R
-
same activity as wild-type at optimum temperature for catalysis
S128R/T158E/N117R/S160E
-
same activity as wild-type at optimum temperature for catalysis
S128R/T158E/S160E
-
same activity as wild-type at optimum temperature for catalysis
T158E
-
60% activity of wild-type at optimum temperature for catalysis
K286Q/R289Q/R292Q/S264L/S240A
P00370
site-directed mutagenesis, the mutant shows highly increased KM for NADP+ compared to the wild-type enzyme
additional information
-
an active chimera (CEC) consisting of the substrate-binding domain (domain I) of CsGDH and the coenzyme-binding domain (domain II) of Escherichia coli GDH is generated. Kinetic constants of chimeric protein: Km values for substrates L-glutamate, 2-oxoglutarate, NH4Cl highly increased compared to wild-type, Vmax values also highly increased compared to wild-type. The CEC chimera, like Escherichia coli GDH, has a marked preference for NADP(H) as coenzyme. selectivity for the phosphorylated coenzyme does indeed reside solely in domain II. Positive cooperativity toward L-glutamate, characteristic of wild-type CsGDH, retains with domain I. Although glutamate cooperativity occurs only at higher pH values in the wild-tpye CsGDH, the chimeric protein shows it over the full pH range explored. The chimera is capable of catalyzing severalfold higher reaction rates (Vmax) in both directions than either of the parent enzymes from which it is constructed
R292Q
P00370
site-directed mutagenesis, the mutant shows increased KM for NADP+ compared to the wild-type enzyme
additional information
-
gdh mutant TIL487, loss of ability to degrade amino acids
additional information
Lactococcus lactis NCDO1867
-
gdh mutant TIL487, loss of ability to degrade amino acids
-
additional information
-
disruption of the NADPH-dependent glutamate dehydrogenase gene leads to decreased beta-lactam production
additional information
Penicillium chrysogenum DS12975
-
disruption of the NADPH-dependent glutamate dehydrogenase gene leads to decreased beta-lactam production
-
additional information
-
deletion mutant lacking the first 19 amino acid residues, shows unchanged activity and forms hexamers, thus the unique extension does not appear to be essential for catalysis and subunit assembly, and presumably fulfils some other yet unknown function
K426A
-
site-directed mutagenesis of GDH1
additional information
-
promoter swapping and site-directed mutagenesis of GDH1 and GDH3, construction of gene disruption null mutants of both genes, phenotypes and mutant activities, overview
additional information
-
construction of enzyme deletion mutants DELTAgdh1 and DELTAgdh3, the mutants show less than 20% of wild-type activity, genotypes and phenotypes, overview
K426A
-
site-directed mutagenesis of GDH1
-
additional information
-
promoter swapping and site-directed mutagenesis of GDH1 and GDH3, construction of gene disruption null mutants of both genes, phenotypes and mutant activities, overview
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
food industry
-
is responsible for the capacity of Lactococcus lactis strains to catabolize amino acids to aroma compounds, pGdh442 can be naturally transmitted to other Lactococcus lactis strains by using cadmium or zinc resistance as a selectable marker, new prospects to intensify and diversify the production of aroma compounds in cheese
food industry
Lactococcus lactis NCDO1867
-
is responsible for the capacity of Lactococcus lactis strains to catabolize amino acids to aroma compounds, pGdh442 can be naturally transmitted to other Lactococcus lactis strains by using cadmium or zinc resistance as a selectable marker, new prospects to intensify and diversify the production of aroma compounds in cheese
-
molecular biology
C6EVR5, -
promoter of GDH from Xanthophyllomyces dendrorhous is shown to be a valuable tool for controlled gene expression in Basidiomycetes
molecular biology
-
results implicate glutamate dehydrogenase and NADP-GDH in particular, as a key target of in vivo isophthalate inhibition during ammonium assimilation
additional information
-
minor role in ammonium assimilation in ectomycorrhizal fungi, NADPH-GDH activity detected in ectomycorrhizas formed with Pseudotsuga menziesii
additional information
Cenococcum geophilum H5-3
-
minor role in ammonium assimilation in ectomycorrhizal fungi, NADPH-GDH activity detected in ectomycorrhizas formed with Pseudotsuga menziesii
-
additional information
-, P28998
lack of a structure called antenna, NAD(P)-binding motif GAGNVA, and a second putative coenzyme-binding motif GVLTGKG together with the four residues Lys, Ser, Arg and Thr involved in the binding of the reduced form of NADP, key role of GDH4 in ammonium assimilation
additional information
-
minor role in ammonium assimilation in ectomycorrhizal fungi
additional information
Q96UJ9
minor role in ammonium assimilation in ectomycorrhizal fungi
additional information
-
in order for the wild-type nitrogen assimilation control protein to exert strong repression of gdhA, it must form a tetramer that bridges the two sites at gdhA, similar to other DNA looping models, the negative control mutants of nitrogen assimilation control protein fail to tetramerize and cannot form this loop, thus fail to exert the strong repression at gdhA
additional information
Klebsiella pneumoniae MK53
-
in order for the wild-type nitrogen assimilation control protein to exert strong repression of gdhA, it must form a tetramer that bridges the two sites at gdhA, similar to other DNA looping models, the negative control mutants of nitrogen assimilation control protein fail to tetramerize and cannot form this loop, thus fail to exert the strong repression at gdhA
-
additional information
-
minor role in ammonium assimilation in ectomycorrhizal fungi
additional information
P54388
minor role in ammonium assimilation in ectomycorrhizal fungi, NADPH-GDH activity detected in ectomycorrhizas formed with Pseudotsuga menziesii
medicine
-
in the parasite protein, several salt-bridges mediate contacts between the subunits, possesses a unique N-terminal extension that does not occur in any other GDH sequence so far studied, design of peptidomimetics capable of disrupting the oligomeric organisation of the parasite enzyme
additional information
Q9HFR6
minor role in ammonium assimilation in ectomycorrhizal fungi