STRUCTURE DETERMINATION OF HALOGENASE CMLS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 CmlS是一种黄素依赖性卤化酶，被认为参与氯霉素的生物合成。 CmIS被认为是抗生素的乙酰基部分的二氯化物，尽管迄今为止还不知道它的作用机制或底物特异性。 CmlS是新颖的，因为它是被认为作用于脂肪族而不是芳香族底物的少数黄素依赖性卤化酶之一。 通过使CmlS结晶化，有希望获得关于其活性位点的信息，并有希望深入了解它可能作用于哪些子状态。 成功阐明CmlS的活性可能会导致进一步的抗生素研究，并有望产生新的候选药物。

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. CmlS is a flavin-dependent halogenase believed to take part in the biosynthesis of chloramphenical. CmlS is thought to dichlorinate the acetyl moiety of the antibiotic although nothing to date is known about it's mechanism of operation or substrate specificity. CmlS is novel in that it is one of few flavin-dependent halogenases believed to act upon a aliphatic rather than aromatic substrate. By crystallizing CmlS there is hope to gain information as to its active site and hopefully gain insight into what substates it may act upon. Successful elucidation of CmlS' activity may lead to furthering antibiotic research and hopefully produce new drug candidates.