Linked Life Data

11059277

Source:http://linkedlifedata.com/resource/pubmed/id/11059277

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2000-11-16
pubmed:abstractText
Site-directed mutagenesis was used to investigate the effects of S221C/P225A, N118S/S221C/P225A, D60N/N118S/S221C/P225A and Q103R/N118S/S221C/P225A mutations on the properties of Subtilisin E. It was found that S221C/P225A mutant is 73,000-fold decreased in amidase activity than subtilisin E and 3-fold increased than subtiligase in the ratio of esterase/amidase; N118S/S221C/P225A mutant has 3.6-fold and 15-fold decreased in amidase and esterase activity respectively and as a result, it has a 4-fold lower in the ratio of amidase/esterase than S221C/P225A mutant; Although it has no effect on the esterase activity, D60N/N118S/S221C/P225A mutant enhanced its ratio of amidase/esterase by 15 fold, 3.3-fold and 10.3 fold compared to N118S/S221C/P225A mutant, S221C/P225A mutant and subtiligase respectively; Q103R/N118S/S221C/P225A mutant, however, has a 5-fold enhanced in the amidase activity and 55-fold and 1000-fold decrease in the esterase activity and the ratio of esterase/amidase compared to N118S/S221C/P225A.
pubmed:language
chi
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1000-3061
pubmed:author
pubmed:issnType
Print
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
341-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
[Site-directed mutagenesis and effects on the enzymatic properties of subtilisin E].
pubmed:affiliation
Shanghai Research Center of Biotechnology, Chinese Academy of Sciences. yonghuayang@hotmail.com
pubmed:publicationType
Journal Article, English Abstract, Research Support, Non-U.S. Gov't