HEAVY-ATOM ISOTOPE EFFECTS ON ENZYMATIC REACTIONS

重原子同位素对酶反应的影响

• 批准号: 3301955
• 负责人: MARION H OLEARY
• 金额: $ 13.38万
• 依托单位: UNIVERSITY OF NEBRASKA LINCOLN
• 依托单位国家: 美国
• 财政年份: 1989
• 资助国家: 美国
• 起止时间: 1989-06-01 至 1994-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3301955
• 关键词: aspartate carbamoyltransferase; catalyst; enzyme mechanism; enzyme model; enzyme structure; enzyme substrate; glutamate ammonia ligase; mass spectrometry; nonradiation isotope effect; phosphoenolpyruvate carboxylase

Enzymes are the catalysts that control virtually all chemical reactions in living systems. The mechanisms by which these catalysts work and are controlled continues to be an important objective of biological studies, with implications for drug design regulation of biological processes, and other areas. The goal of this work is to determine in detail the mechanisms by which enzymes function. The principal technique being applied is heavy-atom isotope effects which can provide a number of important details of mechanism, including order of addition of various substrates to the enzyme, relative rates of various steps, nature of various intermediates and transition states, and the role of various enzyme functional groups in the overall catalytic process. Enzymes being studied include aspartate transcarbamylase, glutamine synthetase, and phosphoenolpyruvate carboxykinase. Model studies will provide important reference points for interpreting the results of these studies.

酶是几乎控制所有化学反应的催化剂