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

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.5.3 - glycerol-3-phosphate dehydrogenase and Organism(s) Homo sapiens and UniProt Accession P43304

for references in articles please use BRENDA:EC1.1.5.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane , while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane . In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain . This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix [7,8]. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9 . The enzyme is activated by calcium .
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: P43304
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: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glycerol-3-phosphate dehydrogenase, glycerophosphate dehydrogenase, mitochondrial glycerol-3-phosphate dehydrogenase, sn-glycerol 3-phosphate dehydrogenase, glycerol-3-phosphate dehydrogenase 2, fad-dependent glycerol-3-phosphate dehydrogenase, fad-linked glycerol-3-phosphate dehydrogenase, fad-gpdh, glycerol-3-phosphate oxidoreductase, mitochondrial sn-glycerol 3-phosphate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycerophosphate dehydrogenase
mitochondrial, enzyme-bound FAD
FAD-linked glycerol-3-phosphate dehydrogenase
-
-
flavin-linked glycerol-3-phosphate ubiquinone oxidoreductase
-
-
GPD2
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
sn-glycerol 3-phosphate:quinone oxidoreductase
This flavin-dependent dehydrogenase is an essential membrane enzyme, functioning at the central junction of glycolysis, respiration and phospholipid biosynthesis. In bacteria, the enzyme is localized to the cytoplasmic membrane [6], while in eukaryotes it is tightly bound to the outer surface of the inner mitochondrial membrane [2]. In eukaryotes, this enzyme, together with the cytosolic enzyme EC 1.1.1.8, glycerol-3-phosphate dehydrogenase (NAD+), forms the glycerol-3-phosphate shuttle by which NADH produced in the cytosol, primarily from glycolysis, can be reoxidized to NAD+ by the mitochondrial electron-transport chain [3]. This shuttle plays a critical role in transferring reducing equivalents from cytosolic NADH into the mitochondrial matrix [7,8]. Insect flight muscle uses only CoQ10 as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ9 [4]. The enzyme is activated by calcium [3].
CAS REGISTRY NUMBER
COMMENTARY hide
9001-49-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
glycerol 3-phosphate + a quinone
dihydroxyacetone phosphate + a quinol
show the reaction diagram
-
-
-
?
sn-glycerol 3-phosphate + a quinone
glycerone phosphate + a quinol
show the reaction diagram
-
-
-
-
?
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
sn-glycerol 3-phosphate + a quinone
glycerone phosphate + a quinol
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2-dimethyl-5-nitro-2H-benzimidazole
-
-
2-[(7-nitro-3-oxo-2,1,3l5-benzoxadiazol-4-yl)oxy]phenol
-
-
2-[(E)-(4-hydroxyphenyl)diazenyl]-1-benzothiophene-3-ol
-
-
5-[(E)-(3-chlorophenyl)diazenyl]-2-hydroxybenzaldehyde
-
-
cisplatin
-
-
ethyl 4-(3-oxo-1,2-thiazol-2(3H)-yl)benzoate
-
-
N-(3,5-dibromo-4-hydroxyphenyl)-4-methylbenzene-1-sulfonamide
-
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
mGPDH overexpression enhances the wound healing ability in prostate cancer cells
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GPDM_HUMAN
727
1
80853
Swiss-Prot
Mitochondrion (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 70000, calculated from sequence
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
the 42 amino acid presequence is cleaved from N-terminus during mGPDH biogenesis. Only the processed form is part of the mGPDH dimer that is the prominent functional enzyme entity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Daoud, H.; Gruchy, N.; Constans, J.M.; Moussaoui, E.; Saumureau, S.; Bayou, N.; Amy, M.; Vedrine, S.; Vu, P.Y.; Roetig, A.; Laumonnier, F.; Vourch, P.; Andres, C.R.; Leporrier, N.; Briault, S.
Haploinsufficiency of the GPD2 gene in a patient with nonsyndromic mental retardation
Hum. Genet.
124
649-658
2009
Homo sapiens (P43304), Homo sapiens
Manually annotated by BRENDA team
Singh, G.
Mitochondrial FAD-linked glycerol-3-phosphate dehydrogenase: a target for cancer therapeutics
Pharmaceuticals
7
192-206
2014
Homo sapiens
Manually annotated by BRENDA team
Pecinova, A.; Alan, L.; Brazdova, A.; Vrbacky, M.; Pecina, P.; Drahota, Z.; Houstek, J.; Mracek, T.
Role of mitochondrial glycerol-3-phosphate dehydrogenase in metabolic adaptations of prostate cancer
Cells
9
1764
2020
Homo sapiens (P43304)
Manually annotated by BRENDA team