Linked Life Data

17587692

Source:http://linkedlifedata.com/resource/pubmed/id/17587692

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2007-6-25
pubmed:abstractText
To elucidate the relationship between the substrate size and geometric shape of the catalytic site of Thermus maltogenic amylase, Gly50, Asp109, and Val431, located at the interface of the dimer, were replaced with bulky amino acids. The k(cat)/K(m) value of the mutant for amylose increased significantly, whereas that for amylopectin decreased as compared to that of the wild-type enzyme. Thus, the substituted bulky amino acid residues modified the shape of the catalytic site, such that the ability of the enzyme to distinguish between small and large molecules like amylose and amylopectin was enhanced.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0916-8451
pubmed:author
pubmed:issnType
Print
pubmed:volume
71
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1564-7
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Modulation of substrate preference of thermus maltogenic amylase by mutation of the residues at the interface of a dimer.
pubmed:affiliation
Department of Food Science and Agricultural Chemistry, McGill University, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't