Paired Carboxylic Acids in Enzymes and Their Role in Selective Substrate Binding, Catalysis, and Unusually Shifted pKa Values-Reference-Cited by-同舟云学术

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Paired Carboxylic Acids in Enzymes and Their Role in Selective Substrate Binding, Catalysis, and Unusually Shifted pKa Values

Published:2019-06-13 Issue:52 Volume:58 Page:5351-5365
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Khavrutskii Ilja V.¹,Compton Jaimee R.²,Jurkouich Kayla M.³,Legler Patricia M.²^ORCID

Affiliation:

1. Armed Forces Radiobiology Research Institute, Uniformed Services University, Bethesda, Maryland 20889-5648, United States

2. U.S. Naval Research Laboratory, 4555 Overlook Avenue, Washington, D.C. 20375, United States

3. Department of Biomedical Engineering, Case Western Reserve University, Cleveland, Ohio 44106, United States

Funder

Congressionally Directed Medical Research Programs

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b00429

Reference94 articles.

1. Inactivation of endothelin I by deamidase (lysosomal protective protein).

2. Ebelactone B, an inhibitor of urinary carboxypeptidase Y-like kininase, prevents the development of deoxycorticosterone acetate-salt hypertension in rats

3. Novel β-Amino Acid Derivatives as Inhibitors of Cathepsin A

4. Lysosomal Cathepsin A Plays a Significant Role in the Processing of Endogenous Bioactive Peptides

5. Cathepsin A-like activity is possibly the main acidic carboxypeptidase in human platelets

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