Linked Life Data

20085763

Source:http://linkedlifedata.com/resource/pubmed/id/20085763

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2010-2-15
pubmed:abstractText
Human holocarboxylase synthetase shows a high degree of sequence homology in the catalytic domain with bacterial biotin ligases such as Escherichia coli BirA, but differs in the length and sequence of the N-terminus. Despite several studies having been undertaken on the N-terminal region of hHCS, the role of this region remains unclear. We determined the structure of the N-terminal domain of hHCS by limited proteolysis and showed that this domain has a crucial effect on the enzymatic activity. The domain interacts not only with biotin acceptor protein, but also with the catalytic domain of hHCS, as shown by nuclear magnetic resonance (NMR) experiments. We propose that the N-terminal domain of hHCS recognizes the charged region of biotin acceptor protein, distinctly from the recognition by the catalytic domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1873-3468
pubmed:author
pubmed:copyrightInfo
Copyright 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
19
pubmed:volume
584
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
675-80
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
The N-terminal domain of human holocarboxylase synthetase facilitates biotinylation via direct interaction with the substrate protein.
pubmed:affiliation
Division of Magnetic Resonance Research, Korea Basic Science Institute, Cheongwon-Gun, Chungbuk, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't