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.
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