|PROSITE documentation PDOC00753 [for PROSITE entry PS00978]|
FAD-dependent glycerol-3-phosphate dehydrogenase (EC 22.214.171.124) (GPD) catalyzes the conversion of glycerol-3-phosphate into dihydroxyacetone phosphate. In bacteria  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 126.96.36.199) [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:
December 2004 / Pattern and text revised.
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).|
|2||Authors||Roennow B. Kielland-Brandt M.C.|
|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).|