Linked Life Data

18808205

Source:http://linkedlifedata.com/resource/pubmed/id/18808205

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-9-23
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0739-1102
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
395-402
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
The effect of histidine residue modification on tyrosinase activity and conformation: inhibition kinetics and computational prediction.
pubmed:affiliation
College of Life Science and State Key Laboratory for Plant Genetics and Breeding, Sichuan Agricultural University, Sichuan 625014, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't