ENZYMATIC MECHANISMS OF SULFUR NUCLEOSIDE METABOLISM (NIH GM 31186)

爵士提供了I-Te-Met；1Og Te-Met是一个替代方案 S-腺苷蛋氨酸合成酶的底物 (三磷酸腺苷：L-蛋氨酸S-腺苷转移酶)催化 初级生物甲基化试剂ADOMet的合成。这个 反应生成Te-腺苷硫代蛋氨酸(Te-ADOMet) 通过鉴定一种新的化合物与预期的 色谱学性质。对Vmax的反应相当容易 约25%的反应与天然底物蛋氨酸和 KNI为0.5 mm，仅为蛋氨酸KNI的6倍。如果 Te-Met的这种反应发生在细胞中，它可能会影响许多 通过改变细胞内的ADOMet池进行甲基化反应， 这可能会对新陈代谢和基因调控产生很大影响。我们的 研究没有调查Te-Met的体内效应。我们是 继我们的实验研究和理论研究之后 碲取代硫对氢键和氢键的影响 在各种生物中可能发生的静电相互作用 设置。

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.