Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus.
The glyceraldehyde 3-phosphate dehydogenase holoenzyme of Bacillus stearothermophilus possesses precise 222 symmetry: in this respect it differs from the reported structure of the lobster muscle enzyme. Pairs of active sites are linked through a flexible polypeptide loop which probably mediates the structural changes giving rise to cooperative effects. Three additional salt bridges made by each subunit to others would make a major contribution to thermostability of the tetramer.
D000494:Allosteric Regulation; D000595:Amino Acid Sequence; D000818:Animals; D001051:Apoenzymes; D001665:Binding Sites; D001411:Geobacillus stearothermophilus / Q000201:enzymology*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D008958:Models, Molecular; D009243:NAD / Q000378:metabolism; D008121:Nephropidae / Q000201:enzymology; D011487:Protein Conformation; D013057:Spectrum Analysis; D013329:Structure-Activity Relationship; D013696:Temperature
D001051:Apoenzymes; D009243:NAD; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases