Abstract
Publisher Summary This chapter describes thiamine phosphate pyrophosphorylase. The systematic name for thiamine pyrophosphorylase is 2-methyl-4-amino-5-hydroxymethylpyrimidinepyrophosphate:4-methyl-5-(2'-phosphoethyl)-thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase. Trimethyl phosphate (TMP) is hydrolyzed to thiamine by Taka-diastase, oxidized to thiochrome with alkaline cyanogen bromide, and then determined fluorometrically. Specific activity is defined as the nanomoles of TMP formed per milligram of protein per minute. The purification procedure for thiamine phosphate pyrophosphorylase is described in the chapter. A thiamine regulatory mutant of Escherichia coli K12, strain PT-R1, containing a derepressed level of TMP pyrophosphorylase is used for purification. The chapter reviews the properties—molecular weight, kinetic properties, substrate specificity, and metal requirement—of thiamine phosphate pyrophosphorylase. .
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