Linked Life Data

19932772

Source:http://linkedlifedata.com/resource/pubmed/id/19932772

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-2-26
pubmed:abstractText
Enzymes catalyze biochemical reactions in highly crowded environments where the amount of macromolecules may occupy up to 40% of the volume. Here we report how cell-like conditions tune catalytic parameters for the monomeric multi-copper oxidase, Saccharomyces cerevisiae Fet3p, in vitro. At low amounts of crowding agent, we detect increases in both of K(M) (weaker substrate binding) and k(cat) (improved catalytic efficiency), whereas at higher crowding levels, both parameters were reduced. Presence of crowding agents does not affect Fet3p structural content but increases thermal resistance. The observations are compatible with ordering of a non-optimal substrate-binding site and restricted internal dynamics as a result of excluded volume effects making the protein less structurally 'strained'.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:copyrightInfo
Copyright 2009 Elsevier B.V. All rights reserved.
pubmed:issnType
Print
pubmed:volume
1804
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
740-4
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Non-linear effects of macromolecular crowding on enzymatic activity of multi-copper oxidase.
pubmed:affiliation
Department of Chemistry, Chemical Biological Center, Umeå University, 901 87 Umeå, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't