User:Alexander Rudecki/Sandbox 1: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 9: | Line 9: | ||
===Protein Family=== | ===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 on catalysis is found in the | 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 on catalysis is found in the 'Catalytic Mechanism' section on this page. | ||
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. | 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. | ||
===Location=== | ===Location=== | ||
DromeQC is known to localize in the brain and peripheral nerves of ''D. melanogaster''. This fact was unveiled by the discovery of adipokinetic hormone; this protein has an N-terminal pGlu, supporting that DromeQC is involved in its post translational modification. Adipokinetic hormone was found to localize in neurone and nerve endings by immunohistochemistry, suggesting that it functions as a locally released modulator in tissues such as heart and skeletal muscle<ref>PMID: 6342796</ref>. Thus, It has been suggested that DromeQC is part of the secretory pathway, being targeted to secretory vesicles where hormone maturation takes place. This claim is supported by a 27 residue signal sequence contained at the N-terminus of DromeQC. Further support stems from immunohistochemical evidence that DromeQC and its modified substrate are excreted from the cell, where they can be found in the extracellular medium<ref name="schilling"/>. | |||
==Structure== | ==Structure== | ||