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Two distinct glyceraldehyde‐3‐phosphate dehydrogenases in glycolysis and gluconeogenesis in the archaeon Haloferax volcanii
Author(s) -
Tästensen JuliaBeate,
Schönheit Peter
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13037
Subject(s) - haloferax volcanii , phosphoglycerate kinase , biochemistry , biology , glycolysis , gluconeogenesis , dehydrogenase , catabolism , glyceraldehyde , archaea , thermophile , gene , enzyme
The halophilic archaeon Haloferax volcanii degrades glucose via the semiphosphorylative Entner‐Doudoroff pathway and can also grow on gluconeogenic substrates. Here, the enzymes catalysing the conversion of glyceraldehyde‐3‐phosphate ( GAP ) to 3‐phosphoglycerate were analysed. The genome contains the genes gapI and gap II encoding two putative GAP dehydrogenases, and pgk encoding phosphoglycerate kinase ( PGK ). We show that gapI is functionally involved in sugar catabolism, whereas gap II is involved in gluconeogenesis. For pgk , an amphibolic function is indicated. This is the first report of the functional involvement of a phosphorylating glyceraldehyde‐3‐phosphate dehydrogenase and PGK in sugar catabolism in archaea. Phylogenetic analyses indicate that the catabolic gapI from H. volcanii is acquired from bacteria via lateral genetransfer, whereas the anabolic gap II as well as pgk are of archaeal origin.