| pubmed-article:12488013 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12488013 | lifeskim:mentions | umls-concept:C0023861 | lld:lifeskim |
| pubmed-article:12488013 | lifeskim:mentions | umls-concept:C0089795 | lld:lifeskim |
| pubmed-article:12488013 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:12488013 | pubmed:dateCreated | 2002-12-18 | lld:pubmed |
| pubmed-article:12488013 | pubmed:abstractText | The animal and human pathogen Listeria monocytogenes secretes several virulence factors, including a phosphatidylinositol-specific phospholipase C (PI-PLC). Sufficient quantities of L. monocytogenes PI-PLC for biophysical studies were obtained by overexpression of the enzyme in Escherichia coli. The purified PI-PLC was examined in enzyme kinetics experiments using a new fluorogenic substrate, methyl-FLIP. Methyl-FLIP is a water-soluble monomeric substrate cleaved in a manner similar to the natural aggregate substrate, phosphatidylinositol (PI). Michaelis-Menten kinetics were observed with K(M) = 61 +/- 7 microM and V(max) = 120 +/- 5 micromol min(-1) mg(-1), corresponding to k(cat) = 66+/-3 s(-1). The catalysis is activated by the addition of a short-chain phospholipid, dihexanoyl phosphatidylcholine (diC(6)PC). The kinetics were fitted to a two-site model in which the substrate binds to the active site and diC(6)PC binds to a second site, with an interaction between the two sites. The result is a decrease in K(M) and an increase in V(max), producing an overall four to five-fold increase in catalytic efficiency (k(cat)/K(M)). The interaction is not a regulatory mechanism, as is the case for multimeric enzymes; rather, it suggests interfacial cooperativity between the active site and a lipid-binding subsite, presumably adjacent to the active site. | lld:pubmed |
| pubmed-article:12488013 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12488013 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12488013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12488013 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12488013 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:12488013 | pubmed:issn | 0301-4622 | lld:pubmed |
| pubmed-article:12488013 | pubmed:author | pubmed-author:GoldfineHowar... | lld:pubmed |
| pubmed-article:12488013 | pubmed:author | pubmed-author:ZaikovaTatian... | lld:pubmed |
| pubmed-article:12488013 | pubmed:author | pubmed-author:KeanaJohn F... | lld:pubmed |
| pubmed-article:12488013 | pubmed:author | pubmed-author:RyanMargretM | lld:pubmed |
| pubmed-article:12488013 | pubmed:author | pubmed-author:GriffithO... | lld:pubmed |
| pubmed-article:12488013 | pubmed:copyrightInfo | Copyright 2002 Elsevier Science B.V. | lld:pubmed |
| pubmed-article:12488013 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12488013 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:12488013 | pubmed:volume | 101-102 | lld:pubmed |
| pubmed-article:12488013 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12488013 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12488013 | pubmed:pagination | 347-58 | lld:pubmed |
| pubmed-article:12488013 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:meshHeading | pubmed-meshheading:12488013... | lld:pubmed |
| pubmed-article:12488013 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:12488013 | pubmed:articleTitle | Listeria monocytogenes phosphatidylinositol-specific phospholipase C: activation and allostery. | lld:pubmed |
| pubmed-article:12488013 | pubmed:affiliation | Institute of Molecular Biology, University of Oregon, Eugene, OR 97403-1253, USA. | lld:pubmed |
| pubmed-article:12488013 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12488013 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12488013 | lld:pubmed |
