CATH Classification
Level | CATH Code | Description |
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1 | Mainly Alpha |
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1.10 | Orthogonal Bundle |
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1.10.8 | Helicase, Ruva Protein; domain 3 |
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1.10.8.870 | Alpha-glycerophosphate oxidase, cap domain |
Domain Context
CATH Clusters
Superfamily | Alpha-glycerophosphate oxidase, cap domain |
Functional Family | Glycerol-3-phosphate dehydrogenase |
Enzyme Information
1.1.5.3 |
Glycerol-3-phosphate dehydrogenase.
based on mapping to UniProt P13035
sn-glycerol 3-phosphate + a quinone = glycerone phosphate + a quinol.
-!- 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 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. -!- Insect flight muscle uses only CoQ(10) as the physiological quinone whereas hamster and rat mitochondria use mainly CoQ(9). -!- The enzyme is activated by calcium. -!- Formerly EC 1.1.2.1 and EC 1.1.99.5.
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UniProtKB Entries (1)
P13035 |
GLPD_ECOLI
Escherichia coli K-12
Aerobic glycerol-3-phosphate dehydrogenase
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PDB Structure
PDB | 2R4E |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism.
Proc.Natl.Acad.Sci.Usa
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