Acylaminoacyl peptidase

From Proteopedia

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spinqualitylabelsall models Acylaminoacyl peptidase dimer complex with acetyl and glycerol 2hu7 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Acylaminoacyl peptidase or Acylamino-acid releasing enzyme (AARE, EC number 3.4.19.1) cleaves N-acetyl or N-formyl amino acid from the N-terminal of polypeptides.[1] Structural highlights AARE contains a (in olive) and an (in green). . [2] The enzyme exists in an open state in which the oxyanion active site is accessible to the substrate and in a closed state where the active site is blocked.

3D Structures of Acylaminoacyl peptidase

Updated on 03-October-2017

3o4g, 3o4h, 3o4i, 3o4j, 2hu5, 2hu7, 2hu8, 1ve6 – ApAARE – Aeropyrum pernix
2qr5, 2qzp – ApAARE (mutant)
1ve7 – ApAARE+p-nitrophenyl phosphate
4re5, 4re6 – ApAARE+ inhibitor
3fnb – AARE – Streptococcus mutans
4hxe, 4hxg – PhAARE - Pyrococcus horikoshii
4hxf – PhAARE+ peptide chloromethyl ketone

References

1. ↑ Harmat V, Domokos K, Menyhard DK, Pallo A, Szeltner Z, Szamosi I, Beke-Somfai T, Naray-Szabo G, Polgar L. Structure and catalysis of acylaminoacyl peptidase: closed and open subunits of a dimer oligopeptidase. J Biol Chem. 2010 Nov 16. PMID:21084296 doi:10.1074/jbc.M110.169862
2. ↑ Kiss AL, Hornung B, Radi K, Gengeliczki Z, Sztaray B, Juhasz T, Szeltner Z, Harmat V, Polgar L. The acylaminoacyl peptidase from Aeropyrum pernix K1 thought to be an exopeptidase displays endopeptidase activity. J Mol Biol. 2007 Apr 27;368(2):509-20. Epub 2007 Feb 20. PMID:17350041 doi:10.1016/j.jmb.2007.02.025