Hydrogen Bonding to Active-Site Histidine in Peptidyl Boronic Acid Inhibitor Complexes of Chymotrypsin and Subtilisin: Proton Magnetic Resonance Assignments and H/D Fractionation-Reference-Cited by-同舟云学术

Hydrogen Bonding to Active-Site Histidine in Peptidyl Boronic Acid Inhibitor Complexes of Chymotrypsin and Subtilisin: Proton Magnetic Resonance Assignments and H/D Fractionation

Published:1999-04-29 Issue:19 Volume:121 Page:4684-4689
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Bao Donghui¹,Huskey W. Phillip¹,Kettner Charles A.¹,Jordan Frank¹

Affiliation:

1. Contribution from the Department of Chemistry and the Program in Cellular and Molecular Biodynamics at Rutgers, The State University of New Jersey, Newark, New Jersey 07102-1811, and Du Pont Pharmaceutical Company, Wilmington, Delaware 19880-0328

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja990180g

Reference54 articles.

1. An explanation for rapid enzyme-catalyzed proton abstraction from carbon acids: importance of late transition states in concerted mechanisms

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5. Crystal Structure of Rat DNA Polymerase β: Evidence for a Common Polymerase Mechanism

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