Undecaprenyl pyrophosphate synthetase from Lactobacillus plantarum: A dimeric protein☆
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Activation and inhibition of rubber transferases by metal cofactors and pyrophosphate substrates
2003, PhytochemistryCitation Excerpt :In addition, the study of biochemical parameters on the native particles is likely to provide kinetic information directly applicable to the in vivo situation, something always questionable in the study of solubilized membrane-bound enzymes. Other cis-prenyl transferases have been studied: the soluble, prokaryotic undecaprenyl pyrophosphate synthase (UPPS) (Baba and Allen, 1978; Muth and Allen, 1984; Shimizu et al., 1998; Apfel et al., 1999; Hemmi et al., 2001; Kharel et al., 2001; Ko et al., 2001) and the membrane-associated, eucaryotic dehydrodolichyl pyrophosphate synthase (DDPPS) (Adair and Cafmeyer, 1987; Matsuoka et al., 1991; Ericsson et al., 1992; Sato et al., 1999; Chang et al., 2001). Unlike RuT, both UPPS and DDPPS have products with defined molecular weights.
Substrate specificities of medium-prenylchain elongating enzymes, hexaprenyl- and heptaprenyl diphosphate synthases
2003, Journal of Molecular Catalysis B: EnzymaticModulations in hepatic branch-point enzymes involved in isoprenoid biosynthesis upon dietary and drug treatments of rats
1994, Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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This work was supported by USPHS Grant GM 23193.