| Type: | Family | Name: | Glycerol-3-phosphate dehydrogenase, GlpC subunit |
| Description: | In bacteria, glycerol uptake is mediated by the glycerol diffusion facilitator, an integral membrane protein catalysing the rapid equilibration of concentration gradients of glycerol across the cytoplasmic membrane. Intracellular glycerol is converted to glycerol-3-phosphate that is further metabolised to dihydroxyacetone phosphate (DHAP) by either of two membrane-bound enzymes, depending on the growth conditions.Under aerobic growth conditions, in the presence of glycerol, a glycerol-3-phopshate dehydrogenase (encoded by the glpD gene) is induced, which passes the reducing equivalents to an electron transport chain terminating with oxygen as the electron acceptor. Under anaerobic growth conditions, in the presence of glycerol and fumarate, a different dehydrogenase is induced []. Electrons derived from this reaction are ultimately passed to fumarate as the terminal electron acceptor. The enzyme is composed of three subunits, encoded by the glpABC operon, which are all essential for anaerobic growth on glycerol-3-phosphate []. GlpA and B form the soluble subunit which carries the catalytic site of glycerol-3-phosphate oxidation; while GlpC forms a membrane-bound iron-sulphur subunit, which may act as an anchor for the soluble subunit, and is thought to function in electron transfer from GlpAB to the terminal electron acceptor.This entry represents the non-catalytic membrane-bound GlpC subunit. This protein lacks classical hydrophobic transmembrane helices; interaction with the membrane may involve amphipathic helices []. GlcC has conserved Cys-containing motifs suggestive of iron-sulphur binding. An archaeal homologue has also recently been characterised [], which appears to be used under aerobic conditions in halophilic archaea. | Short Name: | G3P_DH_GlpC_su |
