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Inactivation of human hepatitis b virus dna polymerase by pyridoxal 5′-phosphate

✍ Scribed by Sang-Hwan Oh; Yeon-Hee Park; Koo Woo

Publisher
John Wiley and Sons
Year
1989
Tongue
English
Weight
503 KB
Volume
28
Category
Article
ISSN
0146-6615

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✦ Synopsis

Human hepatitis B virus (HBV) DNA polymerase activity was inhibited by pyridoxal 5'-phosphate (PLP) specifically and noncompetitively with respect to deoxythymidine triphosphate (dTTP). NaBH, reduction of PLP-HBV core proteins resulted in the complete inactivation of HBV DNA polymerase, and PLP modification of the enzyme was thought to be mediated through Schiff-base formation.

HBV DNA polymerase has a Michaelis constant (Km) of 0.31 p, M for dTTP and an apparent inhibition constant (Ki) of 0.2 mM for PLP. Its inactivation and modification by PLP may be useful in the study of not only the reaction mechanism of catalysis, but also the physicochemical nature of the enzyme.

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