3n33: Difference between revisions
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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=3n33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n33 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n33 RCSB], [http://www.ebi.ac.uk/pdbsum/3n33 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=3n33 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n33 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3n33 RCSB], [http://www.ebi.ac.uk/pdbsum/3n33 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/Q52VH2_9SPHN Q52VH2_9SPHN]] Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar.<ref>PMID:16109932</ref> <ref>PMID:17064315</ref> | |||
==See Also== | ==See Also== | ||
*[[Aminopeptidase|Aminopeptidase]] | *[[Aminopeptidase|Aminopeptidase]] | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Revision as of 16:48, 25 December 2014
Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with pefabloc SC (AEBSF)Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with pefabloc SC (AEBSF)
Structural highlights
Function[Q52VH2_9SPHN] Beta-aminopeptidase that can cleave synthetic beta-peptides which consist of backbone-elongated beta-amino acid residues that are not processed by common proteolytic enzymes. Can cleave the beta-peptides beta-homoVal-beta-homoAla-beta-homoLeu and beta-homoAla-beta-homoLeu. Requires a beta-amino acid at the N-terminus of peptide substrates and cleaves the peptide bond between the N-terminal beta-amino acid and the amino acid at the second position of tripeptidic substrates of the general structure H-betahXaa-Ile-betahTyr-OH according to the following preferences with regard to the side chain of the N-terminal beta-amino acid: aliphatic and aromatic > OH-containing > hydrogen, basic and polar.[1] [2] See AlsoReferences
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