Sandbox Reserved 1057: Difference between revisions

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<ref name="gould"> Gould, T.; van de Langemheen, H.; Muñoz-Elías, E.; McKinney, D.; Sacchettini, J.; Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in ''Mycobacterium tuberculosis''. ''Molecular Microbiology''. '''2006'''. ''61(4)'':940-947. doi:10.1111/j.1365-2958.2006.05297.x. </ref>
<ref name="gould"> Gould, T.; van de Langemheen, H.; Muñoz-Elías, E.; McKinney, D.; Sacchettini, J.; Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in ''Mycobacterium tuberculosis''. ''Molecular Microbiology''. '''2006'''. ''61(4)'':940-947. doi:10.1111/j.1365-2958.2006.05297.x. </ref>


 
The active site of isocitrate lyase consists of two catalytic residues: Cys191 and His193. Additionally, there are several other amino acid side chains present that form hydrogen bonding opportunities with isocitrate to catalyze the breakdown reaction to glyoxylate and succinate. Ser91, Gly92, Trp93, and Arg228.





Revision as of 04:08, 10 April 2015

Bold text==Isocitrate Lyase from Mycobacterium tuberculosis==

Wild Type Protein

3-Bromopyruvate

3-Nitropropionate

Isocitrate Lyase

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References