Linked Life Data

1100829

Source:http://linkedlifedata.com/resource/pubmed/id/1100829

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1975-12-30
pubmed:abstractText
The alpha-ketoaldehydes methylglyoxal and substituted phenylglyoxals are similar in their abilities to inhibit the growth of Escherichia coli and yeast. When logarithmically growing cells are added to media containing 0.3-1 mM alpha-ketoaldehyde, growth stops for several hours, after which normal growth resumes. The period of growth inhibition does not appear to show any correlation with the ability of glyoxalase I to detoxify these alpha-ketoaldehydes. E. coli and yeast glyoxalase I show markedly different substrate specificities. For example, although both enzymes show broad specificity for both aliphatic and aromatic alpha-ketoaldehydes, 2,4,6-trimethylphenylglyoxal is a substrate for the E. coli enzyme but not for the yeast enzyme. Nevertheless, this alpha-ketoaldehyde inhibits the growth of both E. coli and yeast, similar to the other alpha-ketoaldehydes. Enzymes other than glyoxalase I must play a major role in the metabolism of these alpha-ketoaldehydes during the period of growth inhibition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1155-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1975
pubmed:articleTitle
Growth inhibitory properties of aromatic alpha-ketoaldehydes toward bacteria and yeast. Comparison of inhibition and glyoxalase I activity.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.