Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-11-30
pubmed:abstractText
The effect of mutation proline 17 on the multiple conformations and catalytic function in chicken muscle adenylate kinase (AK) has been studied. The substitution of proline 17 with glycine or valine altered the distribution of multiple conformations. Compared with the wild-type enzyme, the P17G and P17V mutants contained decreased fraction of minor conformer from 18% to 9% and 11%, respectively. Due to the mutation, the enzyme showed lower secondary structural content, poorer affinity to substrates or substrate analogues, and reduced catalytic efficiency. The results revealed the significance of proline 17 in the conformation and function of AK.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/1-anilino-8-naphthalenesulfonate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Monophosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Kinase, http://linkedlifedata.com/resource/pubmed/chemical/Anilino Naphthalenesulfonates, http://linkedlifedata.com/resource/pubmed/chemical/Dinucleoside Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Glycine, http://linkedlifedata.com/resource/pubmed/chemical/P(1),P(5)-di(adenosine-5'-)pentaphos..., http://linkedlifedata.com/resource/pubmed/chemical/Proline, http://linkedlifedata.com/resource/pubmed/chemical/Valine
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
508
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
318-22
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11728443-Adenosine Diphosphate, pubmed-meshheading:11728443-Adenosine Monophosphate, pubmed-meshheading:11728443-Adenosine Triphosphate, pubmed-meshheading:11728443-Adenylate Kinase, pubmed-meshheading:11728443-Amino Acid Sequence, pubmed-meshheading:11728443-Amino Acid Substitution, pubmed-meshheading:11728443-Anilino Naphthalenesulfonates, pubmed-meshheading:11728443-Animals, pubmed-meshheading:11728443-Catalysis, pubmed-meshheading:11728443-Chickens, pubmed-meshheading:11728443-Dinucleoside Phosphates, pubmed-meshheading:11728443-Enzyme Inhibitors, pubmed-meshheading:11728443-Glycine, pubmed-meshheading:11728443-Kinetics, pubmed-meshheading:11728443-Molecular Weight, pubmed-meshheading:11728443-Muscles, pubmed-meshheading:11728443-Mutagenesis, Site-Directed, pubmed-meshheading:11728443-Proline, pubmed-meshheading:11728443-Protein Conformation, pubmed-meshheading:11728443-Protein Structure, Secondary, pubmed-meshheading:11728443-Spectrometry, Fluorescence, pubmed-meshheading:11728443-Valine
pubmed:year
2001
pubmed:articleTitle
Conformational and functional significance of residue proline 17 in chicken muscle adenylate kinase.
pubmed:affiliation
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 100101, Beijing, PR China. xrsheng@sun5.ibp.ac.cn
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't