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The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron (CROSBI ID 252962)

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Tomin, Marko ; Tomić, Antonija ; Kovačević, Borislav ; Tomić, Sanja The Mechanism of Peptide Hydrolysis Catalysed by Dipeptidyl Peptidase III from Bacteroides thetaiotaomicron // Croatica chemica acta, 91 (2018), 2; 187-193. doi: 10.5562/cca3343

Podaci o odgovornosti

Tomin, Marko ; Tomić, Antonija ; Kovačević, Borislav ; Tomić, Sanja

engleski

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

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.

dipeptidyl peptidase III ; DPP III ; peptide hydrolysis ; reaction mechanism ; Bacteroides thetaiotaomicron

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Podaci o izdanju

91 (2)

2018.

187-193

objavljeno

0011-1643

1334-417X

10.5562/cca3343

Povezanost rada

Kemija

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