La. Petersen et Dm. Downs, IDENTIFICATION AND CHARACTERIZATION OF AN OPERON IN SALMONELLA-TYPHIMURIUM INVOLVED IN THIAMINE BIOSYNTHESIS, Journal of bacteriology, 179(15), 1997, pp. 4894-4900
Thiamine pyrophosphate (TPP) is synthesized de novo in Salmonella typh
imurium and is a required cofactor for many enzymes in the cell. Five
kinase activities have been implicated in TPP synthesis, which involve
s joining a 4-methyl-5-(beta-hydroxyethyl) thiazole (THZ) moiety and a
4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) moiety. We report he
re identification of a 2-gene operon involved in thiamine biosynthesis
and present evidence that the genes in this operon, thiMD, encode two
previously identified kinases, THZ kinase and HMP phosphate (HMP-P) k
inase, respectively. We further show that this operon belongs to the g
rowing class of genes involved in TPP synthesis that are transcription
ally regulated by TPP, Our data are consistent with ThiM being a salva
ge enzyme and ThiD being a biosynthetic enzyme involved in TPP synthes
is, as previously suggested.