Cleasby A, Wonacott A, Skarzynski T, Hubbard R E, Davies G J, Proudfoot A E, Bernard A R, Payton M A, Wells T N
Glaxo Wellcome Research and Development, Department of Biomolecular Structure, Stevenage, UK.
Nat Struct Biol. 1996 May;3(5):470-9. doi: 10.1038/nsb0596-470.
Phosphomannose isomerase (PMI) catalyses the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P). Absence of PMI activity in yeasts causes cell lysis and thus the enzyme is a potential target for inhibition and may be a route to antifungal drugs. The 1.7 A crystal structure of PMI from Candida albicans shows that the enzyme has three distinct domains. The active site lies in the central domain, contains a single essential zinc atom, and forms a deep, open cavity of suitable dimensions to contain M6P or F6P The central domain is flanked by a helical domain on one side and a jelly-roll like domain on the other.
磷酸甘露糖异构酶（PMI）催化6-磷酸果糖（F6P）和6-磷酸甘露糖（M6P）之间的可逆异构化反应。酵母中PMI活性的缺失会导致细胞裂解，因此该酶是一个潜在的抑制靶点，可能是开发抗真菌药物的一条途径。白色念珠菌PMI的1.7埃晶体结构表明，该酶具有三个不同的结构域。活性位点位于中央结构域，包含一个单一的必需锌原子，并形成一个深度合适、开口的空腔，足以容纳M6P或F6P。中央结构域一侧由一个螺旋结构域侧翼，另一侧由一个果冻卷状结构域侧翼。
