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Synonyms
ipp isomerase, isopentenyl diphosphate isomerase, idi-2, isopentenyl pyrophosphate isomerase, idi-1, slipi, isopentenyl-diphosphate delta-isomerase, isopentenyl diphosphate:dimethylallyl diphosphate isomerase, type 2 isopentenyl diphosphate isomerase, type 2 isopentenyl diphosphate:dimethylallyl diphosphate isomerase,
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Mn2+
the enzyme requires one Mn2+ or Mg2+ ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site
Cd2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Co2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Ni2+
-
reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Zinc
-
essential cofactor. Type I enzyme contains an atom of tinc. The metal is located in an unusual six-coordinate pocket and may facilitate protonation of the unactivated carbon-carbon double bond in isopentenyl diphosphate
Mg2+
dependent on
Mg2+
the enzyme requires one Mn2+ or Mg2+ ion to fold in its active conformation, forming a distorted octahedral metal coordination site composed of three histidines and two glutamates and located in the active site
Mg2+
-
required for activity
Mg2+
-
the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer
Mg2+
-
0.72 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Mn2+
-
the enzyme is fully active in the absence of Mn2+ as long as Mg2+ is present in the buffer
Mn2+
-
0.10 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Zn2+
-
0.92 mol per mol of enzyme. Reconstitution of metal-free enzyme with Mg2+, Mn2+, Zn2+, Co2+, Ni2+ or Cd2+ generates active enzyme
Zn2+
-
IDI-1 is a zinc-metalloprotein
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comparison of orthorhombic, monoclinic and trigonal crystal forms, up to 2.2 A resolution. Crystallization of free enzyme and in complex wih transition-state analogue N,N-dimethyl-2-amino-1-ethyl diphosphate
crystal structure of free and metal-bound C67A mutant enzyme
crystallographic investigation of phosphoantigen binding
hanging drop vapor diffusion method, crystal structures of complexes with transition state analogue N,N-dimethyl-2-amino-1-ethyl diphosphate and the covalently attached irreversible inhibitors 3,4-epoxy-3-methyl-1-butyl diphosphate at 1.96 A resolution
of wild-type and mutants Y104A, Y104F
crystal structure of the isomerase-bromohydrin complex
-
crystals soaked with transition state analogue (N,N-dimethylamino)-1-ethyl diphosphate
-
hanging drop vapor diffusion method, crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with the mechanism-based irreversible inhibitor 3,4-epoxy-3-methyl-1-butyl diphosphate
-
hanging drop vapour diffusion method, selenomethionyl form, crystals display trigonal symmetry, with unit-cell parameters, a = b = 71.3 A, c = 61.7 A, and diffract to 1.45 A resolution
-
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Oudjama, Y.; Durbecq, V.; Sainz, G.; Clantin, B.; Tricot, C.; Stalon, V.; Villeret, V.; Droogmans, L.
Preliminary structural studies of Escherichia coli isopentenyl diphosphate isomerase
Acta Crystallogr. Sect. D
57
287-288
2001
Escherichia coli
brenda
Durbecq, V.; Sainz, G.; Oudjama, Y.; Clantin, B.; Bompard-Gilles, C.; Tricot, C.; Caillet, J.; Stalon, V.; Droogmans, L.; Villeret, V.
Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase
EMBO J.
20
1530-1537
2001
Escherichia coli (Q46822), Escherichia coli
brenda
Wouters, J.; Oudjama, Y.; Ghosh, S.; Stalon, V.; Droogmans, L.; Oldfield, E.
Structure and mechanism of action of isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase
J. Am. Chem. Soc.
125
3198-3199
2003
Escherichia coli
brenda
Carrigan, C.N.; Poulter, C.D.
Zinc is an essential cofactor for type I isopentenyl diphosphate:dimethylallyl diphosphate isomerase
J. Am. Chem. Soc.
125
9008-9009
2003
Escherichia coli
brenda
Wouters, J.; Oudjama, Y.; Barkley, S.J.; Tricot, C.; Stalon, V.; Droogmans, L.; Poulter, C.D.
Catalytic mechanism of Escherichia coli isopentenyl diphosphate isomerase involves Cys-67, Glu-116, and Tyr-104 as suggested by crystal structures of complexes with transition state analogues and irreversible inhibitors
J. Biol. Chem.
278
11903-11908
2003
Escherichia coli (Q46822), Escherichia coli
brenda
Wouters, J.; Oudjama, Y.; Stalon, V.; Droogmans, L.; Poulter, C.D.
Crystal structure of the C67A mutant of isopentenyl diphosphate isomerase complexed with a mechanism-based irreversible inhibitor
Proteins
54
216-221
2004
Escherichia coli
brenda
Wouters, J.; Yin, F.; Song, Y.; Zhang, Y.; Oudjama, Y.; Stalon, V.; Droogmans, L.; Morita, C.T.; Oldfield, E.
A crystallographic investigation of phosphoantigen binding to isopentenyl pyrophosphate/dimethylallyl pyrophosphate isomerase
J. Am. Chem. Soc.
127
536-537
2005
Escherichia coli (Q46822)
brenda
Lee, S.; Poulter, C.D.
Escherichia coli type I isopentenyl diphosphate isomerase: structural and catalytic roles for divalent metals
J. Am. Chem. Soc.
128
11545-11550
2006
Escherichia coli
brenda
de Ruyck, J.; Durisotti, V.; Oudjama, Y.; Wouters, J.
Structural role for Tyr-104 in Escherichia coli isopentenyl-diphosphate isomerase: site-directed mutagenesis, enzymology, and protein crystallography
J. Biol. Chem.
281
17864-17869
2006
Escherichia coli (Q46822), Escherichia coli
brenda
de Ruyck, J.; Oudjama, Y.; Wouters, J.
Monoclinic form of isopentenyl diphosphate isomerase: a case of polymorphism in biomolecular crystals
Acta Crystallogr. Sect. F
F64
239-242
2008
Escherichia coli (Q46822)
brenda
Ghimire, G.P.; Lee, H.C.; Sohng, J.K.
Improved squalene production via modulation of the methylerythritol 4-phosphate pathway and heterologous expression of genes from Streptomyces peucetius ATCC 27952 in Escherichia coli
Appl. Environ. Microbiol.
75
7291-7293
2009
Escherichia coli
brenda
Ohto, C.; Muramatsu, M.; Obata, S.; Sakuradani, E.; Shimizu, S.
Prenyl alcohol production by expression of exogenous isopentenyl diphosphate isomerase and farnesyl diphosphate synthase genes in Escherichia coli
Biosci. Biotechnol. Biochem.
73
186-188
2009
Escherichia coli
brenda
Lai, D.; Lluncor, B.; Schroeder, I.; Gunsalus, R.P.; Liao, J.C.; Monbouquette, H.G.
Reconstruction of the archaeal isoprenoid ether lipid biosynthesis pathway in Escherichia coli through digeranylgeranylglyceryl phosphate
Metab. Eng.
11
184-191
2009
Escherichia coli (Q46822)
brenda
Sharma, N.K.; Pan, J.J.; Poulter, C.D.
Type II isopentenyl diphosphate isomerase: probing the mechanism with alkyne/allene diphosphate substrate analogues
Biochemistry
49
6228-6233
2010
Escherichia coli, Thermus thermophilus
brenda
Berthelot, K.; Estevez, Y.; Deffieux, A.; Peruch, F.
Isopentenyl diphosphate isomerase: A checkpoint to isoprenoid biosynthesis
Biochimie
94
1621-1634
2012
Homo sapiens (Q13907), Escherichia coli (Q46822)
brenda