Sandbox Wabash 03 fumarase

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(New page: ==Active Site of Fumarase== <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> Fumarase is a tetrameric enzyme that catalyzes the dehydrat...)
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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 is a tetrameric enzyme that catalyzes the dehydration of L-malate to Fumarate and vice versa. It does so by deprotonating the C3 carbon of L-malate and removing an OH group from the C2 carbon, or by adding a water across the double bond of fumarate.
Fumarase is a tetrameric enzyme that catalyzes the dehydration of L-malate to Fumarate and vice versa. It does so by deprotonating the C3 carbon of L-malate and removing an OH group from the C2 carbon, or by adding a water across the double bond of fumarate.
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Fumarase has two sites where substrates can bind. The first site, which is referred to as "site A" in a Weaver et al. 1997 study <ref>PMID:9098893<ref/> is deeper in the enzyme structure than the second site, "site B". In addition it is composed of atoms from 3 of the four subunits, where as site B is completely composed of atoms from a single sub unit. <ref>PMID:9098893<ref/>
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Fumarase has two sites where substrates can bind. The first site, which is referred to as "site A" in a Weaver et al. 1997 study <ref>PMID:9098893</ref> is deeper in the enzyme structure than the second site, "site B". In addition it is composed of atoms from 3 of the four subunits, where as site B is completely composed of atoms from a single sub unit. <ref>PMID:9098893</ref>
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A dilemma arose over which was the active site. A 1996 crystallographic study showed L-malate and beta-trimethylsilyl maleate in site B.<ref>PMID:8909293<ref/> However, it was suspected that site A was the active site, because no active monomeric unit of fumerase had ever been described. Furthermore, in the previously mentioned study, citrate, which is a known competitive inhibitor of fumarase activity, was used at high concentration as the crystallizing agent. Hence, this would explain L-malate's association at site B rather than A. In a 1997 study by Weaver et. al, mutations were introduced at each site. Since Histidine was suggested to be one of the bases participating in the catalytic activity of fumarase '''Sandbox Wabash 03 fumarase'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
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A dilemma arose over which was the active site. A 1996 crystallographic study showed L-malate and beta-trimethylsilyl maleate in site B.<ref>PMID:8909293</ref> However, it was suspected that site A was the active site, because no active monomeric unit of fumerase had ever been described. Furthermore, in the previously mentioned study, citrate, which is a known competitive inhibitor of fumarase activity, was used at high concentration as the crystallizing agent. Hence, this would explain L-malate's association at site B rather than A. In a 1997 study by Weaver et. al, mutations were introduced at each site. Since Histidine was suggested to be one of the bases participating in the catalytic activity of fumarase '''Sandbox Wabash 03 fumarase'''. Click above on '''edit this page''' to modify. Be careful with the &lt; and &gt; signs.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.
You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue.

Revision as of 02:00, 29 February 2016

Active Site of Fumarase

Caption for this structure

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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. ↑ 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
  3. ↑ Weaver T, Banaszak L. Crystallographic studies of the catalytic and a second site in fumarase C from Escherichia coli. Biochemistry. 1996 Nov 5;35(44):13955-65. PMID:8909293 doi:http://dx.doi.org/10.1021/bi9614702
  4. ↑ 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
  5. ↑ 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
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