Acylaminoacyl peptidase

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

Acylaminoacyl peptidase 3D structures

ReferencesReferences

↑ 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
↑ 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

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Alexander Berchansky, Michal Harel, Joel L. Sussman

[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

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