D-stereospecific aminopeptidase
| D-aminopeptidase, domain B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of a d-aminopeptidase from Brucella anthropi | |||||||||
| Identifiers | |||||||||
| Symbol | DAP_B | ||||||||
| Pfam | PF07930 | ||||||||
| Pfam clan | CL0013 | ||||||||
| InterPro | IPR012856 | ||||||||
| SCOP2 | 1ei5 / SCOPe / SUPFAM | ||||||||
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| D-aminopeptidase, domain C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
crystal structure of a d-aminopeptidase from Brucella anthropi | |||||||||
| Identifiers | |||||||||
| Symbol | DAP_C | ||||||||
| Pfam | PF07932 | ||||||||
| InterPro | IPR012857 | ||||||||
| SCOP2 | 1ei5 / SCOPe / SUPFAM | ||||||||
| |||||||||
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 Brucella 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.
