2-KETO-3-DEOXY-D-MANNO-OCTULOSONATE 8-PHOSPHATE PHOSPHATASE

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 将2-酮-3-脱氧-D-甘露糖8-磷酸磷酸酶(KDO8PP)与结构同源的2-酮-3-脱氧-9-O-磷酸磷酸酶(KDN9PP)进行比较。两者都是类杆菌属的卤代烷酸脱卤酶超家族(HAD)磷酸酶。KDO8PP和KDN9PP在一级序列和三维结构上具有同源性，具有相似的配体和活性部位。通过这一分析，底物特异性残基将被鉴定。然后，这些残基将从一种酶交换到另一种酶，以实现特异性。通过分析这两种相似的酶，可以确定赋予底物专一性的手段。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. 2-keto-3-deoxy-D-manno-octulosonate 8-phosphate phosphatase (KDO8PP) will be compared against a structurally homologous enzyme, 2-keto-3-deoxy-9-O-phosphonononic acid phosphatase (KDN9PP). Both are haloalkanoate dehalogenase superfamily (HAD) phosphatase enzymes from Bacteroides Thetaiotaomicron. KDO8PP and KDN9PP are homologous in primary sequence and three-dimensional structure, and have similar ligands and active sites. Through this analysis, substrate specificity residues will be identified. Then these residues will be swapped from one enzyme to the other to engineer specificity. By analyzing these two similar enzymes, the means of endowing substrate specificity can be identified.