The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron
Marko Tomin
orcid.org/0000-0001-6894-6810
; Division of Organic Chemistry and Biochemistry, Ruđer Bošković Institute, Bijenička cesta 54, 10000 Zagreb, Croatia
Antonija Tomić
; Division of Organic Chemistry and Biochemistry, Ruđer Bošković Institute, Bijenička cesta 54, 10000 Zagreb, Croatia
Borislav Kovačević
; Division of Physical Chemistry, Ruđer Bošković Institute, Bijenička cesta 54, 10000 Zagreb, Croatia
Sanja Tomić
orcid.org/0000-0002-0550-0878
; Division of Organic Chemistry and Biochemistry, Ruđer Bošković Institute, Bijenička cesta 54, 10000 Zagreb, Croatia
APA 6th Edition Tomin, M., Tomić, A., Kovačević, B. i Tomić, S. (2018). The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron. Croatica Chemica Acta, 91 (2), 187-193. https://doi.org/10.5562/cca3343
MLA 8th Edition Tomin, Marko, et al. "The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron." Croatica Chemica Acta, vol. 91, br. 2, 2018, str. 187-193. https://doi.org/10.5562/cca3343. Citirano 04.03.2021.
Chicago 17th Edition Tomin, Marko, Antonija Tomić, Borislav Kovačević i Sanja Tomić. "The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron." Croatica Chemica Acta 91, br. 2 (2018): 187-193. https://doi.org/10.5562/cca3343
Harvard Tomin, M., et al. (2018). 'The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron', Croatica Chemica Acta, 91(2), str. 187-193. https://doi.org/10.5562/cca3343
Vancouver Tomin M, Tomić A, Kovačević B, Tomić S. The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron. Croatica Chemica Acta [Internet]. 2018 [pristupljeno 04.03.2021.];91(2):187-193. https://doi.org/10.5562/cca3343
IEEE M. Tomin, A. Tomić, B. Kovačević i S. Tomić, "The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron", Croatica Chemica Acta, vol.91, br. 2, str. 187-193, 2018. [Online]. https://doi.org/10.5562/cca3343
Sažetak Dipeptidyl peptidase III (DPP III) is a zinc-dependent peptidase that cleaves dipeptides off of N-termini of its substrates. Previous studies on human DPP III reveal a reaction mechanism similar to that of thermolysin. Since the active site is conserved within the DPP III family, it is not surprising that the mechanism determined for Bacteroides thetaiotaomicron DPP III (BtDPP III) closely resembles that of hDPP III. However, the hydrogen bond network within the model differs slightly from that in the human ortholog, which results in two proposed pathways. The calculated Gibbs activation energy of 90.1 kJ mol–1 is larger than the one calculated from kinetic data for the preferred substrate Arg2-2-naphthylamide at room temperature (69 kJ mol–1), suggesting the importance of treating the whole DPP III enzyme in the calculations.