Reduction of background interference in the spectrophotometric assay of mevalonate kinase.
Mevalonate kinase can be conveniently assayed by coupling to two other reactions and monitoring the consumption of NADH optically at 340 nm. No mevalonate kinase was detected in crude extracts of Saccharomyces cerevisiae strains, however, because of background interference measured in the absence of mevalonate. A strain of S. cerevisiae over-expressing mevalonate kinase was used to establish conditions for reduction of background interference. This method has been successfully applied to S. cerevisiae strains containing a wild type level of mevalonate kinase.
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Linsheng
L
Song
D001681:Biological Assay; D013186:Farnesyl-Diphosphate Farnesyltransferase / Q000235:genetics / Q000378:metabolism; D008798:Mevalonic Acid / Q000378:metabolism; D009154:Mutation; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism; D013053:Spectrophotometry
D029701:Saccharomyces cerevisiae Proteins; C496127:ERG9 protein, S cerevisiae; D013186:Farnesyl-Diphosphate Farnesyltransferase; D017853:Phosphotransferases (Alcohol Group Acceptor); C021796:mevalonate kinase; D008798:Mevalonic Acid