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----<Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />
{{STRUCTURE_3hyq |  PDB=3hyq |  SCENE='Sandbox341/Active_site_one/3'}}
'''INTRODUCTION'''
'''INTRODUCTION'''


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This is a image of 3hq[[Image:Image:My_protein.png
This is a image of 3hq[[Image: My_protein.png |thumb]]
]]


Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.
Isoprenoid compounds are the most diverse family of metabolites that are found in nature(1). Here we look at IPP isomerase it's activity is found in a large number of essential processes and is a central posistion in terpenoid biosynthesis(1).IPP can be isomerized to DMAPP by Isopentenyl diphosphate(IDI)isomerase; which is a metal-ion requiring enzyme(3) utilizing mg or mn.
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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'''


<Structure load='3hyq' size='300' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />==This is a placeholder==
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.
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2. Caillet,Joel et al.(2001).Crystal structure of isopentenyl diphosphate:dimethylallyl diphosphate isomerase.The EMBO journal.Vol20.No7.pp1531-1537.
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{{STRUCTURE_3cin |  PDB=3cin  |  SCENE=  }}
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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