期刊
BIOCHEMISTRY
卷 47, 期 35, 页码 9051-9053出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi801159x
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资金
- Belgian Fonds pour la formation la Recherche dans l'Industrie et dans l'Agriculture (FRIA)
- NIH [GM 25521]
- FNRS [4.4505.00]
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 PPi 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.
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