4rye
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The crystal structure of D-ALANYL-D-ALANINE CARBOXYPEPTIDASE from Mycobacterium tuberculosis H37Rv
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Structural highlights
FunctionDACB2_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 AlsoReferences
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This page was last modified 11:23, 6 November 2024.