Sandbox reserved 330: Difference between revisions
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==Tautomerase Superfamily== | ==Tautomerase Superfamily== | ||
The YdcE protein(EndoA) has been categorized as part of a subfamily of the tautomerase superfamily, which includes the 4-oxalocrotonate tautomerase. This superfamily is composed of structurally homologous proteins that are constructed from a simple β-α-β fold. These homologous proteins share a key mechanistic feature of using an amino terminal proline, which has an unsually low pKa, as a general base in a keto-enol tautomerization<ref > Almrud, J.J., Kern, A.D., Wang, S.C., Czerwinski, R.M., Johnson, W.H., Murzin, A.G., Hackert, M.L., Whitman, C.P. The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli., confirms the structural basis for oligomer diversity. Biochemistry.2002. August;41(40):12010-12024</ref>. | The YdcE protein(EndoA) has been categorized as part of a subfamily of the tautomerase superfamily, which includes the 4-oxalocrotonate tautomerase. This superfamily is composed of structurally homologous proteins that are constructed from a simple β-α-β fold. These homologous proteins share a key mechanistic feature of using an amino terminal proline, which has an unsually low pKa, as a general base in a keto-enol tautomerization<ref name="Almrud"> Almrud, J.J., Kern, A.D., Wang, S.C., Czerwinski, R.M., Johnson, W.H., Murzin, A.G., Hackert, M.L., Whitman, C.P. The crystal structure of YdcE, a 4-oxalocrotonate tautomerase homologue from Escherichia coli., confirms the structural basis for oligomer diversity. Biochemistry.2002. August;41(40):12010-12024</ref>. | ||
==Structure== | ==Structure== | ||
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The active site of the YdcE protein is composed of residues from both monomers, with key active site residues consisting of Pro1, Arg 11, Arg 38, Phe50. Dimerization of the two monomers include Pro1, which is presumed to be the catalytic base and is from one subunit, while Phe8, Arg 10, Trp 51, and Tyr72 are from the other monomer. | The active site of the YdcE protein is composed of residues from both monomers, with key active site residues consisting of Pro1, Arg 11, Arg 38, Phe50. Dimerization of the two monomers include Pro1, which is presumed to be the catalytic base and is from one subunit, while Phe8, Arg 10, Trp 51, and Tyr72 are from the other monomer. | ||
<ref>PMID:14517982</ref> | <ref name="Gogos">PMID:14517982</ref> | ||
<references/> | <references/> | ||
