FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2108666301> ?p ?o ?g. }

• W2108666301 endingPage "650" @default.
• W2108666301 startingPage "635" @default.
• W2108666301 abstract "Phosphoinositide-specific phospholipases C (PI-PLCs) are ubiquitous enzymes that catalyse the hydrolysis of phosphoinositides to inositol phosphates and diacylglycerol (DAG). Whereas the eukaryotic PI-PLCs play a central role in most signal transduction cascades by producing two second messengers, inositol-1,4,5-trisphosphate and DAG, prokaryotic PI-PLCs are of interest because they act as virulence factors in some pathogenic bacteria. Bacterial PI-PLCs consist of a single domain of 30 to 35 kDa, while the much larger eukaryotic enzymes (85 to 150 kDa) are organized in several distinct domains. The catalytic domain of eukaryotic PI-PLCs is assembled from two highly conserved polypeptide stretches, called regions X and Y, that are separated by a divergent linker sequence. There is only marginal sequence similarity between the catalytic domain of eukaryotic and prokaryotic PI-PLCs. Recently the crystal structures of a bacterial and a eukaryotic PI-PLC have been determined, both in complexes with substrate analogues thus enabling a comparison of these enzymes in structural and mechanistic terms. Eukaryotic and prokaryotic PI-PLCs contain a distorted (βα)8-barrel as a structural motif with a surprisingly large structural similarity for the first half of the (βα)8-barrel and a much weaker similarity for the second half. The higher degree of structure conservation in the first half of the barrel correlates with the presence of all catalytic residues, in particular two catalytic histidine residues, in this portion of the enzyme. The second half contributes mainly to the features of the substrate binding pocket that result in the distinct substrate preferences exhibited by the prokaryotic and eukaryotic enzymes. A striking difference between the enzymes is the utilization of a catalytic calcium ion that electrostatically stabilizes the transition state in eukaryotic enzymes, whereas this role is filled by an analogously positioned arginine in bacterial PI-PLCs. The catalytic domains of all PI-PLCs may share not only a common fold but also a similar catalytic mechanism utilizing general base/acid catalysis. The conservation of the topology and parts of the active site suggests a divergent evolution from a common ancestral protein." @default.
• W2108666301 created "2016-06-24" @default.
• W2108666301 creator A5022473461 @default.
• W2108666301 creator A5033695434 @default.
• W2108666301 creator A5035350917 @default.
• W2108666301 date "1998-01-01" @default.
• W2108666301 modified "2023-10-16" @default.
• W2108666301 title "Structural and mechanistic comparison of prokaryotic and eukaryotic phosphoinositide-specific phospholipases C 1 1Edited by K. Nagai" @default.
• W2108666301 cites W1493567759 @default.
• W2108666301 cites W1505216348 @default.
• W2108666301 cites W1584598819 @default.
• W2108666301 cites W16780149 @default.
• W2108666301 cites W1774489767 @default.
• W2108666301 cites W1785056813 @default.
• W2108666301 cites W1902385984 @default.
• W2108666301 cites W1938975553 @default.
• W2108666301 cites W1963618443 @default.
• W2108666301 cites W1970692622 @default.
• W2108666301 cites W1978649670 @default.
• W2108666301 cites W1980166477 @default.
• W2108666301 cites W1999989347 @default.
• W2108666301 cites W2003143189 @default.
• W2108666301 cites W2009310436 @default.
• W2108666301 cites W2009333697 @default.
• W2108666301 cites W2010840688 @default.
• W2108666301 cites W2013083986 @default.
• W2108666301 cites W2014621836 @default.
• W2108666301 cites W2015096311 @default.
• W2108666301 cites W2015478270 @default.
• W2108666301 cites W2019704247 @default.
• W2108666301 cites W2022058405 @default.
• W2108666301 cites W2023067478 @default.
• W2108666301 cites W2026868609 @default.
• W2108666301 cites W2028231353 @default.
• W2108666301 cites W2033071347 @default.
• W2108666301 cites W2038736974 @default.
• W2108666301 cites W2041389129 @default.
• W2108666301 cites W2048497567 @default.
• W2108666301 cites W2055916570 @default.
• W2108666301 cites W2058628523 @default.
• W2108666301 cites W2062748780 @default.
• W2108666301 cites W2063831812 @default.
• W2108666301 cites W2069907055 @default.
• W2108666301 cites W2078248419 @default.
• W2108666301 cites W2078470147 @default.
• W2108666301 cites W2079853404 @default.
• W2108666301 cites W2079943317 @default.
• W2108666301 cites W2080550444 @default.
• W2108666301 cites W2085693261 @default.
• W2108666301 cites W2086524338 @default.
• W2108666301 cites W2088347357 @default.
• W2108666301 cites W2091918398 @default.
• W2108666301 cites W2092249847 @default.
• W2108666301 cites W2093970541 @default.
• W2108666301 cites W2094253868 @default.
• W2108666301 cites W2104982236 @default.
• W2108666301 cites W2111513838 @default.
• W2108666301 cites W2112397485 @default.
• W2108666301 cites W2112742429 @default.
• W2108666301 cites W2115121494 @default.
• W2108666301 cites W2118224224 @default.
• W2108666301 cites W2125083705 @default.
• W2108666301 cites W2129515516 @default.
• W2108666301 cites W2139014308 @default.
• W2108666301 cites W2151977734 @default.
• W2108666301 cites W2152050010 @default.
• W2108666301 cites W2161827223 @default.
• W2108666301 cites W2169317674 @default.
• W2108666301 cites W2175428614 @default.
• W2108666301 cites W2200640757 @default.
• W2108666301 cites W2951343790 @default.
• W2108666301 cites W4239102874 @default.
• W2108666301 doi "https://doi.org/10.1006/jmbi.1997.1490" @default.
• W2108666301 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9466937" @default.
• W2108666301 hasPublicationYear "1998" @default.
• W2108666301 type Work @default.
• W2108666301 sameAs 2108666301 @default.
• W2108666301 citedByCount "116" @default.
• W2108666301 countsByYear W21086663012012 @default.
• W2108666301 countsByYear W21086663012013 @default.
• W2108666301 countsByYear W21086663012014 @default.
• W2108666301 countsByYear W21086663012015 @default.
• W2108666301 countsByYear W21086663012016 @default.
• W2108666301 countsByYear W21086663012017 @default.
• W2108666301 countsByYear W21086663012018 @default.
• W2108666301 countsByYear W21086663012019 @default.
• W2108666301 countsByYear W21086663012020 @default.
• W2108666301 countsByYear W21086663012022 @default.
• W2108666301 countsByYear W21086663012023 @default.
• W2108666301 crossrefType "journal-article" @default.
• W2108666301 hasAuthorship W2108666301A5022473461 @default.
• W2108666301 hasAuthorship W2108666301A5033695434 @default.
• W2108666301 hasAuthorship W2108666301A5035350917 @default.
• W2108666301 hasConcept C104317684 @default.
• W2108666301 hasConcept C139489369 @default.
• W2108666301 hasConcept C163235415 @default.
• W2108666301 hasConcept C167625842 @default.
• W2108666301 hasConcept C181199279 @default.

• next