Kinetic properties and stereospecificity of the monomeric dUTPase from herpes simplex virus type 1

FEBS Letters

Nyman, Per Olof¹  Bergman, Anna-Carin¹  Larsson, Gunilla¹ 

[1]Department of Biochemistry, Center for Chemistry and Chemical Engineering, Lund University, P.O. Box 124, S-221 00 Lund, Sweden

关键词: dUTPase;    Nucleotide metabolism;    Kinetics;    Inhibition;    Substrate analogue;    Herpes simplex virus;    dUTPase;    deoxyuridine triphosphate nucleotidohydrolase;    HSV;    herpes simplex virus type 1;    EIAV;    equine infectious anemia virus;    MMTV;    mouse mammary tumor virus;    dU;    2′-deoxyuridine;    α;    β-imido-dUTP;    2′-deoxyuridine 5′-(α;    β-imido)triphosphate;    dUTPαS;    2′-deoxyuridine 5′-(α-thio)triphosphate;    dUMPαS;    2′-deoxyuridine 5′-(α-thio)monophosphate;    C12E8;    octaethylene glycol mono-n-dodecylether;   

DOI  :  10.1016/S0014-5793(98)01575-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Kinetic properties of the monomeric enzyme dUTPase from herpes simplex virus type 1 (HSV) were investigated and compared to those previously determined for homotrimeric dUTPases of bacterial and retroviral origins. The HSV and Escherichia coli dUTPases are equally potent as catalysts towards the native substrate dUTP with a k _cat/K _M of about 10⁷ M⁻¹ s⁻¹ and a K _M of 0.3 μM. However, the viral enzymes are less specific than the bacterial enzyme. The HSV and E. coli dUTPases show the same stereospecificity towards the racemic substrate analogue dUTPαS (2′-deoxyuridine 5′-(α-thio)triphosphate), suggesting that they have identical reaction mechanisms.

【 授权许可】

Unknown