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https://doi.org/10.5562/cca2107

Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327

Nina Jajčanin-Jozić ; Division of Organic Chemistry and Biochemistry, Ruđer Bošković Institute, Bijenička cesta 54, HR-10002 Zagreb, Croatia
Peter Macheroux ; Institute of Biochemistry, Graz University of Technology, Petersgasse 12, A-8010 Graz, Austria
Marija Abramić ; Division of Organic Chemistry and Biochemistry, Ruđer Bošković Institute, Bijenička cesta 54, HR-10002 Zagreb, Croatia

Puni tekst: engleski, pdf (3 MB) str. 535-540 preuzimanja: 711* citiraj
APA 6th Edition
Jajčanin-Jozić, N., Macheroux, P. i Abramić, M. (2012). Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327. Croatica Chemica Acta, 85 (4), 535-540. https://doi.org/10.5562/cca2107
MLA 8th Edition
Jajčanin-Jozić, Nina, et al. "Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327." Croatica Chemica Acta, vol. 85, br. 4, 2012, str. 535-540. https://doi.org/10.5562/cca2107. Citirano 25.02.2021.
Chicago 17th Edition
Jajčanin-Jozić, Nina, Peter Macheroux i Marija Abramić. "Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327." Croatica Chemica Acta 85, br. 4 (2012): 535-540. https://doi.org/10.5562/cca2107
Harvard
Jajčanin-Jozić, N., Macheroux, P., i Abramić, M. (2012). 'Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327', Croatica Chemica Acta, 85(4), str. 535-540. https://doi.org/10.5562/cca2107
Vancouver
Jajčanin-Jozić N, Macheroux P, Abramić M. Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327. Croatica Chemica Acta [Internet]. 2012 [pristupljeno 25.02.2021.];85(4):535-540. https://doi.org/10.5562/cca2107
IEEE
N. Jajčanin-Jozić, P. Macheroux i M. Abramić, "Yeast Ortholog of Peptidase Family M49: the Role of Invariant Glu461 and Tyr327", Croatica Chemica Acta, vol.85, br. 4, str. 535-540, 2012. [Online]. https://doi.org/10.5562/cca2107

Sažetak
Metallopeptidase family M49 is characterized by five conserved sequence regions and the unique motif HEXXGH with two histidines - ligands of the active-site zinc ion. The crystal structure of the yeast ortholog represents a prototype for the whole family.
To investigate the role of two invariant amino acid residues, a Glu461 of the zinc-binding motif, and a Tyr327, 21Å from the catalytic zinc center, mutational analysis of the yeast enzyme was performed.
The substitution of Glu461 to glutamine decreased kcat for the substrate hydrolysis almost by 10 000-fold. The replacement of Tyr327 by Phe or Ala reduced the catalytic efficiency (kcat/Km) by two orders of magnitude. The affinity for the heptapeptide valorphin was siginificantly lowered in all mutants, in-dicating the contribution of both Glu461 and Tyr327 in substrate binding. Taken together, the effect of mutating Glu461 is consistent with this residue being essential in M49 peptidase catalysis. (doi: 10.5562/cca2107)

Ključne riječi
enzyme catalysis; metallopeptidase; protein structure-function; site-directed mutagenesis; yeast Saccharomyces cerevisiae

Hrčak ID: 94463

URI
https://hrcak.srce.hr/94463

Posjeta: 1.078 *