PROSITE documentation PDOC00753FAD-dependent glycerol-3-phosphate dehydrogenase signatures
FAD-dependent glycerol-3-phosphate dehydrogenase (EC 1.1.99.5) (GPD) catalyzes the conversion of glycerol-3-phosphate into dihydroxyacetone phosphate. In bacteria [1] it is associated with the utilization of glycerol coupled to respiration. In Escherichia coli, two isozymes are known: one expressed under anaerobic conditions (gene glpA) and one in aerobic conditions (gene glpD). In eukaryotes, a mitochondrial form of GPD participates in the glycerol phosphate shuttle in conjunction with an NAD-dependent cytoplasmic GPD (EC 1.1.1.8) [2,3].
These enzymes are proteins of about 60 to 70 Kd which contain a probable FAD-binding domain in their N-terminal extremity. The mammalian enzyme differs from the bacterial or yeast proteins by having an EF-hand calcium-binding region (See <PDOC00018>) in its C-terminal extremity.
We developed two signature patterns. One based on the first half of the FAD-binding domain and one which corresponds to a conserved region in the central part of these enzymes.
Expert(s) to contact by email: Last update:December 2004 / Pattern and text revised.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Austin D. Larson T.J. |
| Title | Nucleotide sequence of the glpD gene encoding aerobic sn-glycerol 3-phosphate dehydrogenase of Escherichia coli K-12. | |
| Source | J. Bacteriol. 173:101-107(1991). | |
| PubMed ID | 1987111 |
| 2 | Authors | Roennow B. Kielland-Brandt M.C. |
| Source | Yeast 9:1121-1130(1993). |
| 3 | Authors | Brown L.J. McDonald M.J. Lehn D.A. Moran S.M. |
| Title | Sequence of rat mitochondrial glycerol-3-phosphate dehydrogenase cDNA. Evidence for EF-hand calcium-binding domains. | |
| Source | J. Biol. Chem. 269:14363-14366(1994). | |
| PubMed ID | 8182039 |
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