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3fvz
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fvz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fvz RCSB], [http://www.ebi.ac.uk/pdbsum/3fvz PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3fvz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fvz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fvz RCSB], [http://www.ebi.ac.uk/pdbsum/3fvz PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/AMD_RAT AMD_RAT]] Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 17:10, 25 December 2014
Structure of Peptidyl-alpha-hydroxyglycine alpha-Amidating Lyase (PAL)
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Categories: Peptidylamidoglycolate lyase | Rattus norvegicus | Amzel, L M | Chufan, E E | De, M | Eipper, B A | Mains, R E | Beta propeller | Cleavage on pair of basic residue | Cytoplasmic vesicle | Glycoprotein | Hg-mad | Lyase | Membrane | Metal-binding | Monooxygenase | Multifunctional enzyme | Oxidoreductase | Peptide amidation | Phosphoprotein | Sulfation | Transmembrane | Vitamin c | Zn-mad
