User:Alexander Rudecki/Sandbox 1: Difference between revisions

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===Protein Family===

DromeQC belongs to the α/β-hydrolase fold superfamily; this superfamily exhibits a β-sheet core (5-8 strands) connected to α helices forming an α/β/α sandwhich<ref name=“family”>PMID: 23193256</ref>. As of present, the ESTHER database (ESTerases and α/β-Hydrolase Enzymes and Relatives) contains 168 protein families<ref>Lenfant, N., Hotelier, T., Velluet, E., Bourne, Y., Marchot, P., and A Chatonnet. (2013) ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins: tools to explore diversity of functions. Nucleic Acids Research 41: D423-9. [http://bioweb.ensam.inra.fr/ESTHER/general?what=index]</ref>. Most of the proteins in this superfamily function via a conserved catalytic triad - a nucleophile, acid and base - with the residues present on the loops of the active site<ref name=~~“family”~~/>. Further information of this is found in the section #REDIRECT [[Alexander Rudecki/Sandbox 1#Catalytic Mechanism]].

DromeQC belongs to the α/β-hydrolase fold superfamily; this superfamily exhibits a β-sheet core (5-8 strands) connected to α helices forming an α/β/α sandwhich<ref name=“family”>PMID: 23193256</ref>. As of present, the ESTHER database (ESTerases and α/β-Hydrolase Enzymes and Relatives) contains 168 protein families<ref>Lenfant, N., Hotelier, T., Velluet, E., Bourne, Y., Marchot, P., and A Chatonnet. (2013) ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins: tools to explore diversity of functions. Nucleic Acids Research 41: D423-9. [http://bioweb.ensam.inra.fr/ESTHER/general?what=index]</ref>. Most of the proteins in this superfamily function via a conserved catalytic triad - a nucleophile, acid and base - with the residues present on the loops of the active site<ref name="family"/>. Further information of this is found in the section #REDIRECT [[Alexander Rudecki/Sandbox 1#Catalytic Mechanism]].

It is interesting that DromeQC prevents protein degradation from aminopeptidases, yet theses two enzymes share a common fold and active site residues<ref>PMID: 15028118</ref>. This suggests that the enzymes act in a similar manner, with contrasting effects on substrate.

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 ===Protein Family===
-DromeQC belongs to the α/β-hydrolase fold superfamily; this superfamily exhibits a β-sheet core (5-8 strands) connected to α helices forming an α/β/α sandwhich<ref name=“family”>PMID: 23193256</ref>. As of present, the ESTHER database (ESTerases and α/β-Hydrolase Enzymes and Relatives) contains 168 protein families<ref>Lenfant, N., Hotelier, T., Velluet, E., Bourne, Y., Marchot, P., and A Chatonnet. (2013) ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins: tools to explore diversity of functions. Nucleic Acids Research 41: D423-9. [http://bioweb.ensam.inra.fr/ESTHER/general?what=index]</ref>. Most of the proteins in this superfamily function via a conserved catalytic triad - a nucleophile, acid and base - with the residues present on the loops of the active site<ref name=“family”/>. Further information of this is found in the section #REDIRECT [[Alexander Rudecki/Sandbox 1#Catalytic Mechanism]].
+DromeQC belongs to the α/β-hydrolase fold superfamily; this superfamily exhibits a β-sheet core (5-8 strands) connected to α helices forming an α/β/α sandwhich<ref name=“family”>PMID: 23193256</ref>. As of present, the ESTHER database (ESTerases and α/β-Hydrolase Enzymes and Relatives) contains 168 protein families<ref>Lenfant, N., Hotelier, T., Velluet, E., Bourne, Y., Marchot, P., and A Chatonnet. (2013) ESTHER, the database of the alpha/beta-hydrolase fold superfamily of proteins: tools to explore diversity of functions. Nucleic Acids Research 41: D423-9. [http://bioweb.ensam.inra.fr/ESTHER/general?what=index]</ref>. Most of the proteins in this superfamily function via a conserved catalytic triad - a nucleophile, acid and base - with the residues present on the loops of the active site<ref name="family"/>. Further information of this is found in the section #REDIRECT [[Alexander Rudecki/Sandbox 1#Catalytic Mechanism]].
 It is interesting that DromeQC prevents protein degradation from aminopeptidases, yet theses two enzymes share a common fold and active site residues<ref>PMID: 15028118</ref>. This suggests that the enzymes act in a similar manner, with contrasting effects on substrate.