Specificity of GDP‐Man:dolichyl‐phosphate mannosyltransferase for the guanosine diphosphate esters of mannose analogues containing deoxy and deoxyfluoro substituents

FEBS Letters

McDowell, William²  Schwarz, Ralph T.¹ 

[1] Laboratoire de Chimie Biologique, Université des Sciences et Techniques de Lille Flandres-Artois, F-59655 Villeneuve d'Ascq Cedex, France;Institut für Virologie, Justus-Liebig-Universität, Frankfurter Strasse 107, D-6300 Giessen, FRG

关键词: Deoxy-D-glucose;    2-;    Deoxy-2-fluoro-D-mannose;    2-;    Deoxy-D-mannose;    3-;    Deoxy-D-mannose;    4-;    Deoxy-D-mannose;    6-;    Enzyme inhibition;    (Chick embryo cell);   

DOI  :  10.1016/0014-5793(89)80173-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Guanosine diphosphate (GDP) esters of 2-deoxy-D-glucose (2dGlc), 2-deoxy-2-fluoro-D-mannose (2FMan), 3-deoxy-D-mannose (3dMan), 4-deoxy-D-mannose (4dMan) and 6-deoxy-D-mannose (6dMan) have been synthesised and tested for their ability to act as inhibitors of dolichyl phosphate mannose synthesis (enzyme: GDP-mannose:dolichyl-phosphate mannosyltransferase, EC 2.4.1.83) in chick embryo cell microsomal membranes. The following order of efficiency was found with the apparent K _i in parentheses: GDP-6dMan (0.40 μM±0.15) > GDP-3dMan (1.0 μM±0.1) = GDP-2dGlc (1.3 μM±0.2) > GDP-4dMan (3.1 μM±0.1) GDP-2FMan (15 μM±0). For comparison the K _m for GDP-Man was 0.52 μM±0.02 and the K _i for GDP was 56 μM±2. These results indicate that the 6-hydroxyl group of mannose is not crucial for emzyme-substrate recognition, whereas the 2- and 3-hydroxyls may have some involvement. The 4-hydroxyl appears to be an important determinant for enzyme-substrate recognition in this mannosyltransferase.

【 授权许可】

Unknown