Linked Life Data

19735113

Source:http://linkedlifedata.com/resource/pubmed/id/19735113

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
2009-9-8
pubmed:abstractText
In an effort to determine the physiological role of Arabidopsis thaliana Glx2-1, we attempted to uncover a substrate for the enzyme. Glx2-1 did not effectively process 192 diverse substrates found in a commercial screen used for microorganism identification or exhibit arylsulfatase, lactonase, or phosphotriesterase activities. However, Glx2-1 does exhibit beta-lactamase activity with k(cat)/KM values from 10(3) to 10(5) M(-1) s(-1). Glx2-1 can hydrolyze cephalosporins and carbapenems, albeit with rate constants slower than those of most metallo-beta-lactamases. The potential role of a beta-lactamase in the mitochondria of plant cells is briefly discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
8491-3
pubmed:dateRevised
2010-9-16
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Arabidopsis thaliana mitochondrial glyoxalase 2-1 exhibits beta-lactamase activity.
pubmed:affiliation
Department of Chemistry and Biochemistry, 160 Hughes Hall, 701 East High Street, Miami University, Oxford, Ohio 45056, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural