3dh7: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dh7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dh7 RCSB], [http://www.ebi.ac.uk/pdbsum/3dh7 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3dh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dh7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3dh7 RCSB], [http://www.ebi.ac.uk/pdbsum/3dh7 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/Q53W52_THET8 Q53W52_THET8]] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).[HAMAP-Rule:MF_00354] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 05:17, 25 December 2014
Structure of T. thermophilus IDI-2 in complex with PPiStructure of T. thermophilus IDI-2 in complex with PPi
Structural highlights
Function[Q53W52_THET8] Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).[HAMAP-Rule:MF_00354] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe N-terminal region is stabilized in the crystal structure of Thermus thermophilus type 2 isopentenyl diphosphate isomerase in complex with inorganic pyrophosphate, providing new insights about the active site and the catalytic mechanism of the enzyme. The PP i moiety is located near the conserved residues, H10, R97, H152, Q157, E158, and W219, and the flavin cofactor. The putative active site of isopentenyl diphosphate isomerase 2 provides interactions for stabilizing a carbocationic intermediate similar to those that stabilize the intermediate in the well-established protonation-deprotonation mechanism of isopentenyl diphosphate isomerase 1. Crystal structure of type 2 isopentenyl diphosphate isomerase from Thermus thermophilus in complex with inorganic pyrophosphate.,de Ruyck J, Pouyez J, Rothman SC, Poulter D, Wouters J Biochemistry. 2008 Sep 2;47(35):9051-3. Epub 2008 Aug 12. PMID:18693754[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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