EUKARYOTIC MEVALONATE KINASE

真核甲羟戊酸激酶

• 批准号: 6279862
• 负责人: HENRY M MIZIORKO
• 金额: $ 0.21万
• 依托单位: MEDICAL COLLEGE OF WISCONSIN
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-04-01 至 1999-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6279862
• 关键词: bioengineering /biomedical engineering; biological products; biomedical resource; enzymes; proteins

Mutagenic studies that implicate specific amino acids in reaction chemistry or in substrate binding are fully and accurately interpretable only when the structural integrity of the variant protein has been validated. This validation is facilitated by identification of spur-labeled metabolic analogs. Measurement of spin-probe affinity and binding stoichiometry, using K13M mutant and comparison of these parameters with the values for wild-type mevalonate kinase affords an elegant, rigorous, yet efficient solution-state method for validating the structural integrity of the engineered mutant enzyme. The spin-probe ATPSAP is being productively used to study the active site structure of mevalonate kinase which catalyzes a key step in cholesterol biosynthesis. Studies were conducted using X-band EPR spectroscopy.

涉及反应中特定氨基酸的诱变研究 化学或底物结合完全准确 仅当变体的结构完整性时才可解释 蛋白质已被验证。 此验证是通过以下方式促进的 支线标记的代谢类似物的鉴定。 测量 自旋探针亲和力和结合化学计量，使用 K13M 突变体和 将这些参数与野生型的值进行比较 甲羟戊酸激酶提供了一种优雅、严谨且高效的方法 用于验证结构完整性的解状态方法 工程突变酶。 自旋探针 ATPSAP 正在高效生产 用于研究甲羟戊酸激酶的活性位点结构 催化胆固醇生物合成的关键步骤。 研究是 使用 X 波段 EPR 光谱进行。