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Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III

Abramić, Marija; Karačić, Zrinka; Šemanjski, Maja; Vukelić, Bojana; Jajčanin-Jozić, Nina (2015) Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III. Biological Chemistry, 396 (4). pp. 359-366. ISSN 1431-6730

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Abstract

Human dipeptidyl peptidase III (hDPP III) is a member of the M49 metallopeptidase family, which is involved in intracellular protein catabolism and oxidative stress response. To investigate the structural basis of hDPP III preference for diarginyl arylamide, using site-directed mutagenesis, we altered its S2 subsite to mimic the counterpart in yeast enzyme. Kinetic studies revealed that the single mutant D496G lost selectivity due to the increase of the Km value. The D496G, but not S504G, showed significantly decreased binding of peptides with N-terminal arginine, and of tynorphin. The results obtained identify Asp496 as an important determinant of human DPP III substrate specificity.

Item Type: Article
Uncontrolled Keywords: metallopeptidase; site-directed mutagenesis; substrate specificity; zinc enzyme
Subjects: NATURAL SCIENCES > Chemistry
Divisions: Division of Organic Chemistry and Biochemistry
Projects:
Project titleProject leaderProject codeProject type
Molekularna enzimologija i proteinske interakcije hidrolaza-Marija Abramić098-1191344-2938MZOS
Depositing User: Zrinka Karačić
Date Deposited: 15 Nov 2018 12:56
Last Modified: 15 Nov 2018 12:56
URI: http://fulir.irb.hr/id/eprint/4281
DOI: 10.1515/hsz-2014-0247

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