Determination of the stereochemistry of hydride transfer from NADPH to FAD catalyzed by VlmR, a flavin reductase from the valanimycin biosynthetic pathway.
[structure: see text]. The stereospecificity of hydride transfer from NADPH to FAD catalyzed by VlmR, a flavin reductase from the valanimycin biosynthetic pathway has been determined. By using stereospecifically deuterated NADPH, it has been shown that the 4-pro R hydrogen of NADPH is transferred.
Skae
P
P
Department of Chemistry MS60, Rice University, PO Box 1892, Houston, Texas 77251-1892, USA.
Parry
R J
RJ
D000903:Antibiotics, Antineoplastic / Q000138:chemical synthesis* / Q000737:chemistry; D001391:Azo Compounds / Q000138:chemical synthesis* / Q000737:chemistry; D038181:FMN Reductase; D005182:Flavin-Adenine Dinucleotide / Q000737:chemistry*; D006859:Hydrogen / Q000378:metabolism*; D008956:Models, Chemical; D009247:NADH, NADPH Oxidoreductases / Q000737:chemistry*; D009249:NADP / Q000737:chemistry*
D000903:Antibiotics, Antineoplastic; D001391:Azo Compounds; C048267:valanimycin; D005182:Flavin-Adenine Dinucleotide; D009249:NADP; D006859:Hydrogen; D038181:FMN Reductase; C430115:VlmR protein, Streptomyces viridifaciens; D009247:NADH, NADPH Oxidoreductases