Precise structural elucidation of dehydroaltenusin, a specific inhibitor of mammalian DNA polymerase alpha.
The X-ray crystal structure of dehydroaltenusin, a specific inhibitor of mammalian DNA polymerase alpha, has previously been reported. We show that dehydroaltenusin exists in an equilibrium mixture of two tautomers possessing gamma-lactone or delta-lactone in polar solvents by NMR experiments. Acetylation of dehydroaltenusin afforded two types of diacetates and two types of monoacetate, possessing gamma-lactone or delta-lactone, respectively. The inhibitory activities of these acetate derivatives against DNA polymerase alpha were all much weaker than that of dehydroaltenusin.
Kamisuki
Shinji
S
Department of Applied Biological Science, Tokyo University of Science, Noda, Chiba 278-8510, Japan.
Takahashi
Shunya
S
Mizushina
Yoshiyuki
Y
Sakaguchi
Kengo
K
Nakata
Tadashi
T
Sugawara
Fumio
F
D000107:Acetylation; D001578:Benzopyrans / Q000737:chemistry* / Q000494:pharmacology*; D018360:Crystallography, X-Ray; D004256:DNA Polymerase I / Q000037:antagonists & inhibitors*; D012997:Solvents / Q000737:chemistry
D001578:Benzopyrans; D012997:Solvents; D004256:DNA Polymerase I; C095645:dehydroaltenusin