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The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron

Tomin, Marko; Tomić, Antonija; Kovačević, Borislav; Tomić, Sanja (2018) The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron. Croatica chemica acta, 91 (2). pp. 187-193. ISSN 0011-1643

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Abstract

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.

Item Type: Article
Uncontrolled Keywords: dipeptidyl peptidase III ; DPP III ; peptide hydrolysis ; reaction mechanism ; Bacteroides thetaiotaomicron
Subjects: NATURAL SCIENCES > Chemistry
Divisions: Division of Organic Chemistry and Biochemistry
Division of Physical Chemistry
Projects:
Project titleProject leaderProject codeProject type
Povezanost fleksibilnosti, aktivnosti i strukture u porodici dipeptidil-peptidaza III-FlAcSSanja TomićIP-2013-11-7235HRZZ
Depositing User: Sofija Konjević
Date Deposited: 01 Aug 2018 11:24
Last Modified: 01 Aug 2018 11:24
URI: http://fulir.irb.hr/id/eprint/4114
DOI: 10.5562/cca3343

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