Acylaminoacyl peptidase
From Proteopedia
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== Function == | == Function == | ||
| - | [[Acylaminoacyl peptidase]] or Acylamino-acid releasing enzyme ('''AARE''', EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1]) cleaves N-acetyl or N-formyl amino acid from the N-terminal of polypeptides. | + | [[Acylaminoacyl peptidase]] or Acylamino-acid releasing enzyme ('''AARE''', EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1]) cleaves N-acetyl or N-formyl amino acid from the N-terminal of polypeptides.<ref>PMID:21084296</ref> |
== Structural highlights == | == Structural highlights == | ||
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== References == | == References == | ||
| - | + | <references/> | |
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 11:59, 3 December 2015
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3D Structures of Acylaminoacyl peptidase
Updated on 03-December-2015
3o4g, 3o4h, 3o4i, 3o4j, 2hu5, 2hu7, 2hu8, 1ve6 – ApAARE – Aeropyrum pernix
2qr5, 2qzp – ApAARE (mutant)
1ve7 – ApAARE+p-nitrophenyl phosphate
3fnb – AARE – Streptococcus mutans
References
- ↑ 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
