title: Erythromycin biosynthesis. The 4-pro-S hydride of NADPH is utilized for ketoreduction by both module 5 and module 6 of the 6-deoxyerythronolide B synthase.
abstract: Incubation of chirally deuterated NADPH with 6-deoxyerythronolide B synthase (DEBS) modules 5 and module 6 and analysis of the derived triketide lactones established that the two ketoreductase domains, KR5 and KR6, are both specific for the 4-pro-S hydride of the nicotinamide cofactor.
authors: Department of Chemistry, Box H, Brown University, Providence, RI 02912-9108, USA.
authors: Y
authors: Y
authors: Yin
authors: R
authors: R
authors: Gokhale
authors: C
authors: C
authors: Khosla
authors: D E
authors: DE
authors: Cane
mesh_terms: D001419:Bacteria / Q000201:enzymology / Q000378:metabolism; D020134:Catalytic Domain; D003903:Deuterium; D004917:Erythromycin / Q000031:analogs & derivatives* / Q000096:biosynthesis* / Q000737:chemistry; D008401:Gas Chromatography-Mass Spectrometry; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D009249:NADP / Q000378:metabolism*; D010084:Oxidation-Reduction; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity
chemical_list: D009097:Multienzyme Complexes; C034277:6-deoxyerythronolide B; D009249:NADP; D004917:Erythromycin; D003903:Deuterium