- D-stereospecific aminopeptidase
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D-aminopeptidase, domain B 
crystal structure of a d-aminopeptidase from ochrobactrum anthropi Identifiers Symbol DAP_B Pfam PF07930 Pfam clan CL0013 InterPro IPR012856 SCOP 1ei5 Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary D-aminopeptidase, domain C crystal structure of a d-aminopeptidase from ochrobactrum anthropi Identifiers Symbol DAP_C Pfam PF07932 InterPro IPR012857 SCOP 1ei5 Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary In molecular biology, D-stereospecific aminopeptidase (D-aminopeptidase) EC 3.4.11.19 is an enzyme which catalyses the release of an N-terminal D-amino acid from a peptide, Xaa-|-Yaa-, in which Xaa is preferably D-Ala, D-Ser or D-Thr. D-amino acid amides and methyl esters also are hydrolyzed, as is glycine amide.
It is a dimeric enzyme with each monomer being composed of three domains. Domain B is organised to form a beta barrel made up of eight antiparallel beta strands. It is connected to domain A, the catalytic domain, by an eight-residue sequence, and also interacts with both domains A and C via non-covalent bonds. Domain B probably functions in maintaining domain C in a good position to interact with the catalytic domain.[1] Domain C is organised to form a beta barrel made up of eight antiparallel beta strands. It is connected to domain B by a short linker sequence, and interacts extensively with the domain A, the catalytic domain. The gamma loop of domain C forms part of the wall of the catalytic pocket; domain C is in fact thought to confer substrate and inhibitor specificity to the enzyme.
External links
References
- ^ Bompard-Gilles C, Remaut H, Villeret V, Prange T, Fanuel L, Delmarcelle M, Joris B, Frere J, Van Beeumen J (September 2000). "Crystal structure of a D-aminopeptidase from Ochrobactrum anthropi, a new member of the 'penicillin-recognizing enzyme' family". Structure 8 (9): 971–80. doi:10.1016/S0969-2126(00)00188-X. PMID 10986464.
This article includes text from the public domain Pfam and InterPro IPR012856
This article includes text from the public domain Pfam and InterPro IPR012857
Categories:- Protein domains
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