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丝氨酸蛋白酶催化机制的量子化学研究(Ⅱ) 被引量：2

Ouantum Chemical Study on Catalytic Mechanism of Serine Proteases
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摘要 用半经验的 MNDO 法对几个模拟丝氨酸蛋白酶活性中心的系统作了研究,发现稳定化能与攻击基团的亲核能力密切相关。活化能的减少估计为9千卡/摩。表明氨键的形成并不能改变底物的形变。 Using the semiempirical MNDO method,several systems simulating the active site of serine proteases have been studied.The stabilization energy was found depending strongly on the nucleophilicity of the attacking group.the decrease of the activation energy has been esti- mated at 9 kca/mole.It was shown that the substrate distortion did not vary with the form- ing of hydrogen bonds.
作者 黄大荣
机构地区 昆明医学院化学教研室
出处 《昆明医学院学报》 1991年第4期36-38,共3页 Journal of Kunming Medical College
关键词 NMDO法 丝氨酸蛋白酶 催化机制 Serine proteases Catalytic mechanism MNDO method
分类号 R977.3 [医药卫生—药品]
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  • 6Rinaldi D.QCPE N290 Program in GEOMO[M].Clarendon Press,Oxford,1974.
  • 7Scheraga HA.Conformational Properties of the CalliFMRE-Amide Series Neuropeptides[J].Adv.Phys.Org.Chem.,1968(6):103 -184.
  • 8Abrahamson S,et al.The Crystal Structure of Phenoxymethyl Penicilin[J].Biochem J,1963 (86):514-535.
  • 9Perricaudet M,Pullman A.Theoretical Studies of Molecular Conformation.Ⅱ:Application of the SIBFA Procedure to molecules Containing Carbonyl and Carboxylate Oxyens and Amide Nitrogens[J] Int J Peptid and Protein Res,1973(5):99 -107.
  • 10黄大荣.丝氨酸蛋白酶催化机制的量子化学研究(Ⅲ)[J].昆明医学院学报,1992,13(1):49-53. 被引量：2

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昆明医学院学报
1991年 第4期

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