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American Chemical Society, Biochemistry, 35(47), p. 9051-9053, 2008

DOI: 10.1021/bi801159x

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Crystal structure of type 2 Isopentenyl Diphosphate Isomerase from Thermus thermophilus in complex with inorganic pyrophosphate†

Journal article published in 2008 by Jérôme de Ruyck ORCID, Jenny Pouyez, Steven C. Rothman, C. Dale Poulter, Johan Wouters
This paper is available in a repository.
This paper is available in a repository.

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Abstract

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.