title: Studies on the active center of D- and L-lactate dehydrogenases using oxamate-diaminohexyl-Sepharose affinity chromatography.
abstract: Vertebrate and invertebrate L-lactate dehydrogenases (L-lactate:NAD+ oxidoreductase, EC 1.1.1.27) are effectively bound to oxamate-diaminohexyl-Sepharose, whereas several D-lactate dehydrogenases (D-lactate:NAD+ oxidoreductase, EC 1.1.1.28) do not bind to the same Sepharose. One explanation for our findings is that the enzymes' substrate is oriented in a reversed manner in the active center of the D- and L-lactate dehydrogenases.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002846:Chromatography, Affinity / Q000379:methods; D006737:Horseshoe Crabs / Q000201:enzymology; D007527:Isoenzymes; D007536:Isomerism; D007770:L-Lactate Dehydrogenase / Q000378:metabolism; D008121:Nephropidae; D011134:Polysaccharides / Q000378:metabolism*; D012685:Sepharose / Q000031:analogs & derivatives / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D007527:Isoenzymes; D011134:Polysaccharides; C027757:oxamate-diaminohexyl-sepharose; D012685:Sepharose; D007770:L-Lactate Dehydrogenase