ENZYMATIC MECHANISMS OF SULFUR NUCLEOSIDE METABOLISM (NIH GM 31186)

硫核苷代谢的酶促机制 (NIH GM 31186)

• 批准号: 6309050
• 负责人: GEORGE Douglas MARKHAM
• 金额: $ 2.74万
• 依托单位: UNIVERSITY OF CALIF-LOS ALAMOS NAT LAB
• 依托单位国家: 美国
• 财政年份: 2000
• 资助国家: 美国
• 起止时间: 2000-02-01 至 2002-01-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6309050
• 关键词: bacteria; biomedical resource; enzymes

The SIR provided I -Te-Met; . 1 OOg The Te-Met was an alternate substrate for the enzyme S-adenosylmethionine (AdoMet) synthetase (ATP: L-methionine S-adenosyltransferase) which catalyzes the synthesis of the primary biological methylating agent, AdoMet. The reaction yields Te-adenosyltelluromethionine (Te-AdoMet) as confirmed by identification of a novel compound with the expected chromatographic properties. The reaction was quite facile with a Vmax of ca. 25% of the reaction with the natural substrate methionine and a Kni of 0.5 mM, only 6 fold larger than the Kni for methionine. If this reaction of Te-Met occurs in cells, it could affect many methylation reactions by altering the intracellular AdoMet pools, which could have large effects on metabolism and gene regulation. Our studies did not investigate in vivo effects of the Te-met. We are following our experimental studies with theoretical investigations of the effects of Tellurium replacement of Sulfur on hydrogen bonding and electrostatic interactions that might occur in a variety of biological settings.

SIR提供了I-Te-Met。 100 g Te-Met是替代品 S-腺苷甲硫氨酸合成酶的底物 (ATP：L-甲硫氨酸S-腺苷转移酶），其催化 主要的生物甲基化剂，甲硫氨酸的合成。 的 经确认，反应产生了Te-AdoMet 通过鉴定一种新的化合物， 色谱性能 反应相当容易，Vmax 为约 25%的反应与天然底物蛋氨酸和 a Kni为0.5 mM，仅比甲硫氨酸的Kni大6倍。 如果 这种Te-Met反应发生在细胞中，它可以影响许多 通过改变细胞内的CD 3 Met池来进行甲基化反应， 这可能对新陈代谢和基因调控有很大的影响。 我们 研究没有调查Te-met的体内作用。 我们 在我们的实验研究和理论研究之后， 碲取代硫对氢键的影响， 静电相互作用可能发生在各种生物 设置.