D-stereospecific aminopeptidase

D-aminopeptidase, domain C
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
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

D-aminopeptidase, domain B
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
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
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[edit]

MEROPS family S12

References[edit]

^ 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.

This article incorporates text from the public domain Pfam and InterPro: IPR012856

This article incorporates text from the public domain Pfam and InterPro: IPR012857

[pmid10986464-1] 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.

[1]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)