Linked Life Data

8954906

Source:http://linkedlifedata.com/resource/pubmed/id/8954906

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-1-22
pubmed:abstractText
The hemorrhagic toxin (HT) from Clostridium sordellii is pharmacologically related to Clostridium difficile toxins A and B and Clostridium sordellii lethal toxin which have been recently identified as mono-glucosyl-transferases. Here we report that HT, which is coexpressed with lethal toxin, is also a glucosyltransferase. Whereas lethal toxin glucosylates the Rho subfamily proteins Rac and Cdc42 and the Ras subfamily proteins H-Ras and Rap, the substrate specificity of HT is strictly confined to the Rho subfamily proteins Rho, Rac and Cdc42. Comparable to lethal toxin, transferase activity of HT is stimulated by Mn2+. Acceptor amino acid in Rho was identified by mutagenesis as threonine-37. C. sordellii HT is a novel member of the family of clostridial mono-glucosyl-transferases, a family which modifies the Rho and Ras GTPases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
229
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
370-4
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1996
pubmed:articleTitle
Difference in protein substrate specificity between hemorrhagic toxin and lethal toxin from Clostridium sordellii.
pubmed:affiliation
Institut für Pharmakologie und Toxikologie der Albert-Ludwigs-Universität Freiburg, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't