期刊
FEBS LETTERS
卷 585, 期 3, 页码 459-464出版社
WILEY
DOI: 10.1016/j.febslet.2010.12.035
关键词
Disulfide oxidoreductase; Carboxylase; Carbon dioxide; Acetoacetate; Coenzyme M
资金
- National Institutes of Health [GM51805]
- Department of Energy [DE-FG02-04ER15563]
- NASA Astrobiology Institute (NAI) [NNA08C-N85A]
- Montana State University (MSU) [W911NF0510255]
- NASA [NAG5-8807]
- US Department of Energy, Office of Biological and Environmental Research
- US National Institutes of Health
- National Center for Research Resources
- US National Institute of General Medical Sciences
- U.S. Department of Energy (DOE) [DE-FG02-04ER15563] Funding Source: U.S. Department of Energy (DOE)
The structure of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) has been determined in a state in which CO2 is observed providing insights into the mechanism of carboxylation. In the substrate encapsulated state of the enzyme, CO2 is bound at the base of a narrow hydrophobic substrate access channel. The base of the channel is demarcated by a transition from a hydrophobic to hydrophilic environment where CO2 is located in position for attack on the carbanion of the ketopropyl group of the substrate to ultimately produce acetoacetate. This binding mode effectively discriminates against H2O and prevents protonation of the ketopropyl leaving group. Structured summary: 2-KPCC binds to 2-KPCC by x-ray crystallography (View interaction) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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