Purification and characterization of D-glyceraldehyde-3-phosphate dehydrogenase from the thermophilic archaebacterium Methanothermus fervidus.
The D-glyceraldehyde-3-phosphate dehydrogenase from the extremely thermophilic archaebacterium Methanothermus fervidus was purified and crystallized. The enzyme is a homomeric tetramer (molecular mass of subunits 45 kDa). Partial sequence analysis shows homology to the enzymes from eubacteria and from the cytoplasm of eukaryotes. Unlike these enzymes, the D-glyceraldehyde-3-phosphate dehydrogenase from Methanothermus fervidus reacts with both NAD+ and NADP+ and is not inhibited by pentalenolactone. The enzyme is intrinsically stable up to 75 degrees C. It is stabilized by the coenzyme NADP+ and at high ionic strength up to about 90 degrees C. Breaks in the Arrhenius and Van't Hoff plots indicate conformational changes of the enzyme at around 52 degrees C.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D004795:Enzyme Stability; D019605:Euryarchaeota / Q000201:enzymology* / Q000254:growth & development; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification* / Q000378:metabolism; D006358:Hot Temperature; D006801:Humans; D007700:Kinetics; D013045:Species Specificity; D013816:Thermodynamics
D000596:Amino Acids; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases