Crystal structure of type 2 isopentenyl diphosphate isomerase from Thermus thermophilus in complex with inorganic pyrophosphate.
The 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.
de Ruyck
Jérôme
J
Department of Chemistry, University of Namur, Namur, Belgium. jerome.deruyck@fundp.ac.be
Pouyez
Jenny
J
Rothman
Steven C
SC
Poulter
Dale
D
Wouters
Johan
J
D001426:Bacterial Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D019748:Carbon-Carbon Double Bond Isomerases / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D018360:Crystallography, X-Ray; D011756:Diphosphates / Q000737:chemistry* / Q000378:metabolism*; D045782:Hemiterpenes; D007700:Kinetics; D008958:Models, Molecular; D013056:Spectrophotometry, Ultraviolet; D013379:Substrate Specificity; D016963:Thermus thermophilus / Q000201:enzymology* / Q000378:metabolism
D001426:Bacterial Proteins; D011756:Diphosphates; D045782:Hemiterpenes; D019748:Carbon-Carbon Double Bond Isomerases; C021453:isopentenyldiphosphate delta-isomerase