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Sandbox Wabash 27 Fumarase

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==Fumarase: The Active Site Debate Answered==
==Fumarase: The Active Site Debate Answered==
<StructureSection load='1YFE' size='340' side='right' caption='Fumarase' scene=''>
<StructureSection load='1YFE' size='340' side='right' caption='Fumarase' scene=''>
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Fumarase (fumarate hydratase) is an enzyme found in eukaryotic cells which catalyzes the reaction between L-malate and fumarate.<ref>PMID: 9098893</ref> The catalysis proceeds via the deprotination of the C3 carbon of L-malate, which is followed by the loss of the -OH group attached to the C2 carbon; the intermediate for which is a carbanion transition state.<ref>Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry. 3rd ed. New York: Wiley, 1999. Print.</ref>
<ref>PMID: 9098893</ref> <ref>Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry. 3rd ed. New York: Wiley, 1999. Print.</ref>
<ref>PMID: 9098893</ref> <ref>Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry. 3rd ed. New York: Wiley, 1999. Print.</ref>

Revision as of 02:47, 28 February 2016

Fumarase: The Active Site Debate Answered

Fumarase

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References

  1. Weaver T, Lees M, Banaszak L. Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Protein Sci. 1997 Apr;6(4):834-42. PMID:9098893
  2. Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry. 3rd ed. New York: Wiley, 1999. Print.
  3. Weaver T, Lees M, Banaszak L. Mutations of fumarase that distinguish between the active site and a nearby dicarboxylic acid binding site. Protein Sci. 1997 Apr;6(4):834-42. PMID:9098893
  4. Voet, Donald, Judith G. Voet, and Charlotte W. Pratt. Fundamentals of Biochemistry. 3rd ed. New York: Wiley, 1999. Print.
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