Sandbox341: Difference between revisions
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IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1) | IPP isomerase is composed of 182 amino acids and folds into a globular protein(2). Conformational changes create a distorted octohedral metal cordination site composed of residues H25, H32, H69, E114, and E116(2).As stated above the enzyme requires metal co-factors in the active site; which also consists of Cys and Glu catalytic residues(1). Studies show that the enzyme Km at the optimal pH 6.3 and the pI between 6.0-6.2 is 2.7iM and the Molecular weight is roughly 82 500(1).The size of the mammalian enzyme is 22kDa(1) | ||
'''REFRENCES''' | |||
1. Heijden,Robert Van Der.,Ramos-Valdivia,Ana C.,Verpoorte,Robert.(1997).Isopentenyl diphosphate isomerase:a core enzyme in isoprenoid biosynthesis.A review of its biochemistry and function.Natural products reports.pp591-602. | |||
2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537. | |||
3. Auria'D,John C et al.(2008).The Arabidopsis thaliana Type 1 Isopentenyl Diphosphate Isomerases Are Targeted to Multiple Subcellular Compartments and Have overlapping functions in Isoprenoid Biosynthesis.The Plant Cell.Vol29.pp677-696. | |||
4. Hemmi,Hisashi.(2004).Type 2 isopentenyl diphosphate isomerase from a thermoacidophilic archaeon Sulfolobus shibatae.Eur j biochem.271.pp1087-1093. | |||
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