Acylaminoacyl peptidase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
- 
{{STRUCTURE_2hu7| PDB=2hu7 | SIZE=400| SCENE=|right|CAPTION=Acylaminoacyl peptidase dimer complex with acetyl and glycerol [[2hu7]]}}
{{STRUCTURE_2hu7| PDB=2hu7 | SIZE=400| SCENE=|right|CAPTION=Acylaminoacyl peptidase dimer complex with acetyl and glycerol [[2hu7]]}}
Line 5: Line 4:
[[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.
 +
 +
== Structural highlights ==
 +
 +
AARE contains a C-terminal hydrolase and an N-terminal β-propeller domain. 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.
__NOTOC__
__NOTOC__

Revision as of 09:52, 25 October 2015

Template:STRUCTURE 2hu7

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.

Structural highlights

AARE contains a C-terminal hydrolase and an N-terminal β-propeller domain. 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 25-October-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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools