Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.4.1.4 - glutamate dehydrogenase (NADP+) and Organism(s) Pyrobaculum calidifontis and UniProt Accession A3MWK6

for references in articles please use BRENDA:EC1.4.1.4
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Pyrobaculum calidifontis
UNIPROT: A3MWK6 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Pyrobaculum calidifontis
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
nadp-gdh, nadp-dependent glutamate dehydrogenase, nadp-glutamate dehydrogenase, nadp-specific glutamate dehydrogenase, nadp-linked glutamate dehydrogenase, nadph-dependent glutamate dehydrogenase, glutamate dehydrogenase (nadp+), nadp+-dependent glutamate dehydrogenase, nadp+-dependent gdh, nadp-dependent gdh, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-glutamate dehydrogenase
-
dehydrogenase, glutamate (nicotinamide adenine dinucleotide phosphate)
-
-
-
-
glutamic acid dehydrogenase
-
-
-
-
glutamic dehydrogenase
-
-
-
-
L-glutamate dehydrogenase
-
-
-
-
NAD(P)H-dependent glutamate dehydrogenase
-
-
-
-
NADP-GDH
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative deamination
-
-
-
-
reductive amination
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-glutamate:NADP+ oxidoreductase (deaminating)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9029-11-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxobutanoate + NH3 + NADPH + H+
L-2-aminobutanoate + H2O + NADP+
show the reaction diagram
2.6% of the activity with 2-oxoglutarate
-
-
r
2-oxoglutarate + NH3 + NADPH + H+
L-glutamate + H2O + NADP+
show the reaction diagram
-
-
-
r
2-oxovalerate + NH3 + NADPH + H+
L-valine + H2O + NADP+
show the reaction diagram
4.2% of the activity with 2-oxoglutarate
-
-
r
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
r
L-norvaline + H2O + NADP+
2-oxopentanoate + NH3 + NADPH + H+
show the reaction diagram
3% of the activity with L-glutamate
-
-
r
additional information
?
-
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 SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-glutamate + H2O + NADP+
2-oxoglutarate + NH3 + NADPH + H+
show the reaction diagram
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
about 17% of the activity with NADP+
NADH
about 7% of the activity with NADPH
additional information
low activity with NAD+/NADH
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Hg2+
1 mM, 76% residual activity
isocitrate
10 M, 64% of initial activity
KCl
100 mM, 45% residual activity
NaCl
100 mM, 59% residual activity
oxaloacetate
10 mM, 63% residual activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.7
2-oxoglutarate
3.4
L-glutamate
0.035
NADP+
0.017
NADPH
2.2
NH3
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
95
2-oxoglutarate
13
L-glutamate
9.9
NADP+
92
NADPH
100
NH3
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
56
2-oxoglutarate
3.8
L-glutamate
280
NADP+
5400
NADPH
45
NH3
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
reductive deamination
9.5
oxidative deamination
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
270000
47700
6 * 47700, tagged recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 9.5
Pcal_1606 retains more than 80% of its activity after incubation for 30 min at pH 4.5-9.5 at 50°C
724938
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
Pcal_1606 retains full activity after incubation for 10 min at temperatures up to 90°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wakamatsu, T.; Higashi, C.; Ohmori, T.; Doi, K.; Ohshima, T.
Biochemical characterization of two glutamate dehydrogenases with different cofactor specificities from a hyperthermophilic archaeon Pyrobaculum calidifontis
Extremophiles
17
379-389
2013
Pyrobaculum calidifontis (A3MWK6), Pyrobaculum calidifontis JCM 11548 (A3MWK6)
Manually annotated by BRENDA team
Wakamatsu, T.; Higashi, C.; Ohmori, T.; Doi, K.; Ohshima, T.
Biochemical characterization of two glutamate dehydrogenases with different cofactor specificities from a hyperthermophilic archaeon Pyrobaculum calidifontis
Extremophiles
17
379-389
2013
Pyrobaculum calidifontis (A3MWK6), Pyrobaculum calidifontis JCM 11548 (A3MWK6)
Manually annotated by BRENDA team