Sandbox Wabash 11 Fumarase
From Proteopedia
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<StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | ||
| - | == Fumarase C | + | == Fumarase C== |
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Found in E. Coli, Fumarase C is an enzyme that catalyzes L-malate and fumarate. It belongs to a family of enzymes that includes aspartase, arginosuccinate lyase, adenlosuccinate lyase, and gamma-crysatallin. It is tetrameric and has approximately 460 amino acids in each monomer. (Weaver et. al. 834. | Found in E. Coli, Fumarase C is an enzyme that catalyzes L-malate and fumarate. It belongs to a family of enzymes that includes aspartase, arginosuccinate lyase, adenlosuccinate lyase, and gamma-crysatallin. It is tetrameric and has approximately 460 amino acids in each monomer. (Weaver et. al. 834. | ||
| - | == The Debate About Two Possible Locations of the Active Site | + | == The Debate About Two Possible Locations of the Active Site== |
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Many studies of Fumarase have shown that there are two different binding sites for carboxylic acid. One site (Site A) A study conducted by Todd Weaver, Mason Lees, and Leonard Banaszak confirmed that Site A was the actual active site. | Many studies of Fumarase have shown that there are two different binding sites for carboxylic acid. One site (Site A) A study conducted by Todd Weaver, Mason Lees, and Leonard Banaszak confirmed that Site A was the actual active site. | ||
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== The Structure of the Active Site == | == The Structure of the Active Site == | ||
Revision as of 21:53, 28 February 2016
The Active Site of Fumarase C
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644
