Inhibition of prolidase by phosphoenolpyruvate is biphasic. avoidance of endogenous-metabolite inactivation by cooperativity within an enzyme dimer-Reference-Cited by-同舟云学术

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Inhibition of prolidase by phosphoenolpyruvate is biphasic. avoidance of endogenous-metabolite inactivation by cooperativity within an enzyme dimer

Published:1995-03 Issue:6 Volume:5 Page:627-630
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Mock William L.,Liu Yaya

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference16 articles.

1. Proline-Dependent Structural and Biological Properties of Peptides and Proteins

2. Human kidney prolidase—purification, preincubation properties and immunological reactivity

3. Specificity and pH dependence for acylproline cleavage by prolidase.

4. Mechanism and inhibition of prolidase.

5. Phosphoenolpyruvate as a natural bisubstrate analog inhibitor of pig kidney prolidase

Cited by 4 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Evolution of Negative Cooperativity in Glutathione Transferase Enabled Preservation of Enzyme Function;Journal of Biological Chemistry;2016-12

2. Xaa-Pro Dipeptidase (Eukaryotes);Handbook of Proteolytic Enzymes;2013

3. X-Pro dipeptidase (eukaryotes);Handbook of Proteolytic Enzymes;2004

4. Peptide mimics of glycylproline as inhibitors of prolidase;Bioorganic & Medicinal Chemistry Letters;1995-12

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