4rye

Structural highlights

Function

DACB2_MYCTU Probably cleaves the terminal D-Ala-D-Ala dipeptide of the peptidoglycan stem peptide (Probable). Shows significant D,D-carboxypeptidase activity in vitro (PubMed:22906310). Acts on the synthetic penta-peptide substrate Penta-DAP (L-Ala-gamma-D-Gln-DAP-D-Ala-D-Ala). Shows also weak activity on Penta-Lys (L-Ala-gamma-Glu-L-Lys-D-Ala-D-Ala) (PubMed:22906310). The catalytic domain binds weakly to peptidoglycan in vitro (PubMed:25551456). Plays an important role in the maintenance of colony morphology and cell wall permeability and integrity (PubMed:25467937).^{[1] [2] [3] [4]}

See Also

• Carboxypeptidase 3D structures
• Penicillin-binding protein 3D structures

References

1. ↑ Kumar P, Arora K, Lloyd JR, Lee IY, Nair V, Fischer E, Boshoff HI, Barry CE 3rd. Meropenem inhibits D,D-carboxypeptidase activity in Mycobacterium tuberculosis. Mol Microbiol. 2012 Oct;86(2):367-81. PMID:22906310 doi:10.1111/j.1365-2958.2012.08199.x
2. ↑ Kandasamy S, Narayanan S. Phenotypic characterization of a novel double knockout PknI/DacB2 from Mycobacterium tuberculosis. Microbiol Res. 2015 Jan;170:255-62. PMID:25467937 doi:10.1016/j.micres.2014.10.002
3. ↑ Prigozhin DM, Krieger IV, Huizar JP, Mavrici D, Waldo GS, Hung LW, Sacchettini JC, Terwilliger TC, Alber T. Subfamily-Specific Adaptations in the Structures of Two Penicillin-Binding Proteins from Mycobacterium tuberculosis. PLoS One. 2014 Dec 31;9(12):e116249. doi: 10.1371/journal.pone.0116249., eCollection 2014. PMID:25551456 doi:http://dx.doi.org/10.1371/journal.pone.0116249
4. ↑ Kumar P, Arora K, Lloyd JR, Lee IY, Nair V, Fischer E, Boshoff HI, Barry CE 3rd. Meropenem inhibits D,D-carboxypeptidase activity in Mycobacterium tuberculosis. Mol Microbiol. 2012 Oct;86(2):367-81. PMID:22906310 doi:10.1111/j.1365-2958.2012.08199.x