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Pregled bibliografske jedinice broj: 758298

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


Abramić, Marija; Karačić, Zrinka; Šemanjski, Maja; Vukelić, Bojana; Jajčanin-Jozić, Nina
Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III // Biological chemistry, 396 (2015), 4; 359-366 doi:10.1515/hsz-2014-0247 (međunarodna recenzija, članak, znanstveni)


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

Autori
Abramić, Marija ; Karačić, Zrinka ; Šemanjski, Maja ; Vukelić, Bojana ; Jajčanin-Jozić, Nina

Izvornik
Biological chemistry (1431-6730) 396 (2015), 4; 359-366

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
metallopeptidase ; site-directed mutagenesis ; substrate specificity ; zinc enzyme

Sažetak
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.

Izvorni jezik
Engleski

Znanstvena područja
Kemija, Biologija



POVEZANOST RADA


Projekti:
098-1191344-2938 - Molekularna enzimologija i proteinske interakcije hidrolaza (Abramić, Marija, MZOS ) ( POIROT)

Ustanove:
Institut "Ruđer Bošković", Zagreb

Poveznice na cjeloviti tekst rada:

doi fulir.irb.hr www.degruyter.com

Citiraj ovu publikaciju:

Abramić, Marija; Karačić, Zrinka; Šemanjski, Maja; Vukelić, Bojana; Jajčanin-Jozić, Nina
Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III // Biological chemistry, 396 (2015), 4; 359-366 doi:10.1515/hsz-2014-0247 (međunarodna recenzija, članak, znanstveni)
Abramić, M., Karačić, Z., Šemanjski, M., Vukelić, B. & Jajčanin-Jozić, N. (2015) Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III. Biological chemistry, 396 (4), 359-366 doi:10.1515/hsz-2014-0247.
@article{article, author = {Abrami\'{c}, Marija and Kara\v{c}i\'{c}, Zrinka and \v{S}emanjski, Maja and Vukeli\'{c}, Bojana and Jaj\v{c}anin-Jozi\'{c}, Nina}, year = {2015}, pages = {359-366}, DOI = {10.1515/hsz-2014-0247}, keywords = {metallopeptidase, site-directed mutagenesis, substrate specificity, zinc enzyme}, journal = {Biological chemistry}, doi = {10.1515/hsz-2014-0247}, volume = {396}, number = {4}, issn = {1431-6730}, title = {Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III}, keyword = {metallopeptidase, site-directed mutagenesis, substrate specificity, zinc enzyme} }
@article{article, author = {Abrami\'{c}, Marija and Kara\v{c}i\'{c}, Zrinka and \v{S}emanjski, Maja and Vukeli\'{c}, Bojana and Jaj\v{c}anin-Jozi\'{c}, Nina}, year = {2015}, pages = {359-366}, DOI = {10.1515/hsz-2014-0247}, keywords = {metallopeptidase, site-directed mutagenesis, substrate specificity, zinc enzyme}, journal = {Biological chemistry}, doi = {10.1515/hsz-2014-0247}, volume = {396}, number = {4}, issn = {1431-6730}, title = {Aspartate 496 from the subsite S2 drives specificity of human dipeptidyl peptidase III}, keyword = {metallopeptidase, site-directed mutagenesis, substrate specificity, zinc enzyme} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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