Concerted nitrogen inversion and hydrogen bonding to Glu451 are responsible for protein-controlled suppression of the reverse reaction in human DPP III-Reference-Cited by-同舟云学术

Concerted nitrogen inversion and hydrogen bonding to Glu451 are responsible for protein-controlled suppression of the reverse reaction in human DPP III

Published:2016 Issue:39 Volume:18 Page:27245-27256
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Tomić A.¹²³⁴,Kovačević B.⁵²³⁴,Tomić S.¹²³⁴

Affiliation:

1. Department of Organic Chemistry and Biochemistry

2. Rudjer Boskovic Institute

3. Zagreb

4. Croatia

5. Department of Physical Chemistry

Abstract

Human dipeptidyl-peptidase III (h.DPP III) is a zinc-exopeptidase that hydrolyses dipeptides from the N-terminus of its substrates.

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CP/C6CP04580D

Reference38 articles.

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2. The HELLGH Motif of Rat Liver Dipeptidyl Peptidase III Is Involved in Zinc Coordination and the Catalytic Activity of the Enzyme

3. Inhibition of recombinant dipeptidyl peptidase III by synthetic hemorphin-like peptides

4. Human dipeptidyl peptidase III acts as a post-proline-cleaving enzyme on endomorphins

5. A genomic screen for activators of the antioxidant response element

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