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Title 

The effect of histidine residue modification on tyrosinase activity and conformation: inhibition kinetics and computational prediction

Authors 

L GouZ R LuDaeui ParkSang Ho OhL ShiSung Jin ParkJong Hwa ParkY D ParkZ L RenF Zou

Publisher 

Adenine Press

Issue Date 

2008

Citation 

Journal of Biomolecular Structure & Dynamics, vol. 26, no. 3, pp. 395-401

Keywords 

docking simulationhistidine modificationinhibition kineticsstructure predictiontyrosinasehistidinebinding kineticschemical modificationconformationenzyme activity

Abstract 

We found that the histidine chemical modification of tyrosinase conspicuously inactivated enzyme activity. The substrate reactions with diethylpyridinecarbamate showed slow-binding inhibition kinetics (KI = 0.24 ± 0.03 mM). Bromoacetate, as another histidine modifier, was also applied in order to study inhibition kinetics. The bromoacetate directly induced the exposures of hydrophobic surfaces following by complete inactivation via ligand binding. For further insights, we predicted the 3D structure of tyrosinase and simulated the docking between tyrosinase and diethylpyridinecarbamate. The docking simulation was shown to the significant binding energy scores (-3.77 kcal/mol by AutoDock4 and -25.26 kcal/mol by Dock6). The computational prediction was informative to elucidate the role of free histidine residues at the active site, which are related to substrate accessibility during tyrosinase catalysis.

ISSN 

0739-1102

Link 

http://dx.doi.org/10.1080/07391102.2008.10507254

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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