Anthony Noles Sandbox: Difference between revisions
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=Aconitase= | =Aconitase= | ||
Aconitase (PDB [[7acn]]) is a single polypeptide (M<sub>r</sub> 83kD) that catalyzes the reversible isomerization of citrate and isocitrate.<ref name="Zheng">Zheng, L., Kennedy, MC., Beinert, H., Zalkin, H. "Mutational analysis of active site residues in pig heart aconitase." J Biol Chem 1992, 267, 7895-7903.</ref> It is the second enzyme is the Citric acid cycle. The <scene name='Anthony_Noles_Sandbox/Secondary_structure/1'>secondary structure</scene> consists of numerous alternating alpha helices and beta sheets (SCOP classification α/β alternating). The tertiary structure is somewhat bilobed with the active site in the middle, and, since there is only one subunit, there is no quaternary structure. Aconitase consists of four domains, three of which are tightly packed while the fourth is more flexible. <ref name="Frishman">Frishman, D., and Hentze, M.W., "Conservation of aconitase residues revealed by multiple sequence analysis: Implications for structure/function relationships." European Journal of Biochemistry, 1996, 239, 197-200.</ref> | Aconitase (PDB [[7acn]]) is a single polypeptide (M<sub>r</sub> 83kD) that catalyzes the reversible isomerization of citrate and isocitrate.<ref name="Zheng">Zheng, L., Kennedy, MC., Beinert, H., Zalkin, H. "Mutational analysis of active site residues in pig heart aconitase." J Biol Chem 1992, 267, 7895-7903.</ref> It is the second enzyme is the Citric acid cycle. | ||
==Structure== | |||
The <scene name='Anthony_Noles_Sandbox/Secondary_structure/1'>secondary structure</scene> consists of numerous alternating alpha helices and beta sheets (SCOP classification α/β alternating). The tertiary structure is somewhat bilobed with the active site in the middle, and, since there is only one subunit, there is no quaternary structure. Aconitase consists of four domains, three of which are tightly packed while the fourth is more flexible. <ref name="Frishman">Frishman, D., and Hentze, M.W., "Conservation of aconitase residues revealed by multiple sequence analysis: Implications for structure/function relationships." European Journal of Biochemistry, 1996, 239, 197-200.</ref> | |||
==Mechanism of Aconitase== | ==Mechanism of Aconitase== | ||