Glycerol-3-phosphate dehydrogenase
| Glycerol-3-phosphate dehydrogenase (NAD+) | |||||||||
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Crystallographic structure of human glycerol-3-phosphate dehydrogenase 1.
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| Identifiers | |||||||||
| EC number | 1.1.1.8 | ||||||||
| CAS number | 9075-65-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
| Glycerol-3-phosphate dehydrogenase (quinone) | |||||||||
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| Identifiers | |||||||||
| EC number | 1.1.5.3 | ||||||||
| CAS number | 9001-49-4 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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| Search | |
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| PMC | articles |
| PubMed | articles |
| NCBI | proteins |
| NAD-dependent glycerol-3-phosphate dehydrogenase N-terminus | |||||||||
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crystal structure of the n-(1-d-carboxylethyl)-l-norvaline dehydrogenase from arthrobacter sp. strain 1c
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| Identifiers | |||||||||
| Symbol | NAD_Gly3P_dh_N | ||||||||
| Pfam | PF01210 | ||||||||
| Pfam clan | CL0063 | ||||||||
| InterPro | IPR011128 | ||||||||
| PROSITE | PDOC00740 | ||||||||
| SCOP | 1m66 | ||||||||
| SUPERFAMILY | 1m66 | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| NAD-dependent glycerol-3-phosphate dehydrogenase C-terminus | |||||||||
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structure of glycerol-3-phosphate dehydrogenase from archaeoglobus fulgidus
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| Identifiers | |||||||||
| Symbol | NAD_Gly3P_dh_C | ||||||||
| Pfam | PF07479 | ||||||||
| Pfam clan | CL0106 | ||||||||
| InterPro | IPR006109 | ||||||||
| PROSITE | PDOC00740 | ||||||||
| SCOP | 1m66 | ||||||||
| SUPERFAMILY | 1m66 | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
| glycerol-3-phosphate dehydrogenase 1 (soluble) | |
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| Identifiers | |
| Symbol | GPD1 |
| Entrez | 2819 |
| HUGO | 4455 |
| OMIM | 138420 |
| RefSeq | NM_005276 |
| UniProt | P21695 |
| Other data | |
| EC number | 1.1.1.8 |
| Locus | Chr. 12 q12-q13 |
| glycerol-3-phosphate dehydrogenase 2 (mitochondrial) | |
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| Identifiers | |
| Symbol | GPD2 |
| Entrez | 2820 |
| HUGO | 4456 |
| OMIM | 138430 |
| RefSeq | NM_000408 |
| UniProt | P43304 |
| Other data | |
| EC number | 1.1.5.3 |
| Locus | Chr. 2 q24.1 |
Glycerol-3-phosphate dehydrogenase (GPDH) is an enzyme that catalyzes the reversible redox conversion of dihydroxyacetone phosphate (a.k.a. glycerone phosphate, outdated) to sn-glycerol 3-phosphate.
Glycerol-3-phosphate dehydrogenase serves as a major link between carbohydrate metabolism and lipid metabolism. It is also a major contributor of electrons to the electron transport chain in the .
Older terms for glycerol-3-phosphate dehydrogenase include alpha glycerol-3-phosphate dehydrogenase (alphaGPDH) and glycerolphosphate dehydrogenase (GPDH). However, glycerol-3-phosphate dehydrogenase is not the same as glyceraldehyde 3-phosphate dehydrogenase (GAPDH), whose substrate is an aldehyde not an alcohol.
GPDH plays a major role in lipid biosynthesis. Through the reduction of dihydroxyacetone phosphate into glycerol 3-phosphate, GPDH allows the prompt dephosphorylation of glycerol 3-phosphate into glycerol. Additionally, GPDH is one of the enzymes involved in maintaining the redox potential across the .
The NAD+/NADH coenzyme couple act as an electron reservoir for metabolic redox reactions, carrying electrons from one reaction to another. Most of these metabolism reactions occur in the . To regenerate NAD+ for further use, NADH pools in the cytosol must be reoxidized. Since the is impermeable to both NADH and NAD+, these cannot be freely exchanged between the cytosol and .
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