Linked Life Data

20208154

Source:http://linkedlifedata.com/resource/pubmed/id/20208154

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2010-3-8
pubmed:databankReference
pubmed:abstractText
Fungal laccases are oxidoreductases that belong to the multinuclear copper-containing oxidases. They are able to oxidize a wide range of substrates, preferably phenolic compounds, which makes them suitable for employment in the bioremediation of soil and water as well as in other biotechnological applications. Here, the structural analysis of natural laccase B (LacB) from Trametes sp. AH28-2 is presented. This structure provides the opportunity to study the natural post-translational modifications of the enzyme. The overall fold shows a high homology to those of previously analyzed laccases with known three-dimensional structure. However, LacB contains a new structural element, a protruding loop near the substrate-binding site, compared with the previously reported laccase structures. This unique structural feature may be involved in modulation of the substrate recognition of LacB.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1744-3091
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
66
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
254-8
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Structure of native laccase B from Trametes sp. AH28-2.
pubmed:affiliation
Modern Experiment Technology Center and School of Life Sciences, Anhui University, Hefei 230039, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't