PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28577910-3	2017	Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction.	4,6-dinitro-o-cresol	148-154	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	101-106	
28577910-3	2017	Over the past decade, a variety of biochemical, spectroscopic, structural and mechanistic studies of IDI-2 have provided mounting evidence that the flavin coenzyme of IDI-2 acts in a most unusual manner - as an acid/base catalyst to mediate a 1,3-proton addition/elimination reaction.	4,6-dinitro-o-cresol	148-154	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	167-172	
28577910-4	2017	While not entirely without precedent, IDI-2 is by far the most extensively studied flavoenzyme that employs flavin-mediated acid/base catalysis.	4,6-dinitro-o-cresol	108-114	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	38-43	
28577910-5	2017	Thus, IDI-2 serves as an important mechanistic model for understanding this often overlooked, but potentially widespread reactivity of flavin coenzymes.	4,6-dinitro-o-cresol	135-141	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	6-11	
27003727-4	2016	For IDI-2 from the pathogenic bacterium Streptococcus pneumoniae, the flavin can be treated kinetically as a dissociable cosubstrate in incubations with IPP and excess NADH.	4,6-dinitro-o-cresol	70-76	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	4-9	
27003727-10	2016	Dithionite reduction of FMN in the IDI-2 FMN and IPP mixture was biphasic with k(red)(IDI-2 FMN IPP (fast)) = 326 s(-1) and k(red)(IDI-2 FMN IPP (slow)) = 6.9 s(-1) The pseudo-first-order rate constant for the slow component was similar to those for NADH reduction of the flavin in the IDI-2 FMN and IPP mixture and may reflect a rate-limiting conformational change in the enzyme.	4,6-dinitro-o-cresol	272-278	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	35-40	
20593767-6	2010	Linear free energy relationships (LFERs) between the electronic properties of the flavin and the steady state kinetic parameters of the IDI-2 catalyzed reaction were observed.	4,6-dinitro-o-cresol	82-88	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	136-141	
20593767-8	2010	Cumulatively, the data presented in this work (and in other studies) suggest that the reduced FMN coenzyme of IDI-2 functions as an acid/base catalyst, with the N5 atom of the flavin likely playing a critical role in the deprotonation of IPP en route to DMAPP formation.	4,6-dinitro-o-cresol	176-182	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	110-115	
18345677-3	2008	Type I IPP isomerase (IDI-1) utilizes a divalent metal in a protonation-deprotonation reaction; whereas, the type II enzyme (IDI-2) requires reduced flavin.	4,6-dinitro-o-cresol	149-155	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	125-130	
18345677-11	2008	These studies indicate that the irreversible inhibitors inactivate the reduced flavin required for catalysis by electrophilic alkylation and are consistent with a protonation-deprotonation mechanism for the isomerization catalyzed by IDI-2.	4,6-dinitro-o-cresol	79-85	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	234-239	
22158896-3	2011	Both the crystal structures of IDI-2 binding the flavin-inhibitor adduct and the UV-visible spectra of the adducts indicate that the covalent bond is formed at C4a of flavin rather than at N5, which had been proposed previously.	4,6-dinitro-o-cresol	49-55	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	31-36	
22158896-3	2011	Both the crystal structures of IDI-2 binding the flavin-inhibitor adduct and the UV-visible spectra of the adducts indicate that the covalent bond is formed at C4a of flavin rather than at N5, which had been proposed previously.	4,6-dinitro-o-cresol	167-173	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	31-36	
22158896-4	2011	In addition, the high-resolution crystal structures of IDI-2-substrate complexes and the kinetic studies of new mutants confirmed that only the flavin cofactor can catalyze protonation of the substrates and suggest that N5 of flavin is most likely to be involved in proton transfer.	4,6-dinitro-o-cresol	144-150	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	55-60	
22158896-4	2011	In addition, the high-resolution crystal structures of IDI-2-substrate complexes and the kinetic studies of new mutants confirmed that only the flavin cofactor can catalyze protonation of the substrates and suggest that N5 of flavin is most likely to be involved in proton transfer.	4,6-dinitro-o-cresol	226-232	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	55-60	
17580897-4	2007	In particular, the catalytic mechanisms of two of these enzymes, UGM and IDI-2, may involve novel flavin chemistry.	4,6-dinitro-o-cresol	98-104	isopentenyl-diphosphate delta isomerase 2	Homo sapiens	73-78