New Insights into the Mechanism of CDP-d-Tyvelose 2-Epimerase: An Enzyme-Catalyzing Epimerization at an Unactivated Stereocenter-Reference-Cited by-同舟云学术

New Insights into the Mechanism of CDP-d-Tyvelose 2-Epimerase: An Enzyme-Catalyzing Epimerization at an Unactivated Stereocenter

Published:2000-10-11 Issue:43 Volume:122 Page:10493-10503
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Hallis Tina M.¹,Zhao Zongbao¹,Liu Hung-wen¹

Affiliation:

1. Contribution from the Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja0022021

Reference55 articles.

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2. Soda, K.; Tanaka, H.; Tanizawa, K. InVitamin B6PyridoxalPhosphate; Dolphin, D., Poulson, R., Avramovic, O., Eds.; Wiley and Sons: New York, 1986; Part B, pp 223−251.

3. Proton transfer in methylmalonyl-CoA epimerase from Propionibacterium shermanii. The reaction of (2R)-methylmalonyl-CoA in tritiated water

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