INHIBITED COMPLEXES OF HUMAN TYPE I 17: DRUG DESIGN TARGET IN BREAST CANCER

利用稀有过渡金属的酶是感兴趣的， 帮助我们理解独特的酶反应。 甲酸脱氢酶H (FDH)来自大肠大肠杆菌就是这样一种酶。 FDH含有多种氧化还原 中心，其中包括一个多巴胺辅因子，铁硫 簇和天然硒代半胱氨酸残基在其活性位点。 这 蛋白质与其它的内切酶没有序列同源性， 都具有众所周知的蛋白质结合折叠。 我们希望了解 这类酶的机制是利用异蝶呤， 硒代半胱氨酸介导它们的氧化还原反应。 另一个独特的类 酶的催化机制尚不清楚， 血液转化酶，α-N-乙酰氨基半乳糖苷酶（α-NAGAL）和 α-半乳糖苷酶（α-GAL）。 人血ABO抗原特异性 是由末端单糖的性质和连接决定的 糖蛋白或糖脂的糖链 嵌在细胞膜上 一种提供大型 大量O型血是将A型和B型细胞转化为 通过使用适当的外切糖苷酶。 了解 碳水化合物链的转化机制， 三维结构的确定将有望提供 产生具有A和B的酶所必需的信息 转换函数

Enzymes that utilize rare transition metals are of interest to help us understand unique enzymic reactions. Formate dehydrogenase H (FDH) from E. coli is such an enzyme. FDH contains multiple redox centers, which include a molybdopterin cofactor, an iron-sulfur cluster and a natural selenocystein residue at its active site. This protein shares no sequence homology with other dehydrogenases which all have the well-known protein binding fold. We hope to understand the mechanism of this class of enzymes that utilizes molybdopterin and selenocystein to mediate their redox reaction. Another unique class of enzymes whose catalytic mechanism is not understood is that of the blood converting enzymes, a-N-acetylgalactosaminidase (a-NAGAL) and a-galactosidase (a-GAL). The ABO antigenic specificity in human blood is determined by the nature and linkage of monosaccharides at the end of the carbohydrate chains of either glycoproteins or glycolipids embedded in the cell membrane. An approach to providing large quantities of group O blood is to convert group A and B cells to group O by using the appropriate exoglycosidases. Understanding the mechanism of conversion of the carbohydrate chains through three-dimensional structure determination will hopefully provide the information necessary to produce an enzyme with both A and B converting function.