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Literature summary extracted from

  • Pandey, S.; Pal, S.; N, G.; Bansal, A.; Mallick, S.; Ghosh, A.
    Two DD-carboxypeptidases from Mycobacterium smegmatis affect cell surface properties through regulation of peptidoglycan cross-linking and glycopeptidolipids (2018), J. Bacteriol., 200, e00760 .
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
3.4.17.8 Mycolicibacterium smegmatis A0QV34
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3.4.17.8 Mycolicibacterium smegmatis A0QV35
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3.4.17.8 Mycolicibacterium smegmatis ATCC 700084 A0QV34
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3.4.17.8 Mycolicibacterium smegmatis ATCC 700084 A0QV35
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Synonyms

EC Number Synonyms Comment Organism
3.4.17.8 DD-CPase
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 Mycolicibacterium smegmatis
3.4.17.8 msmeg_2432
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 Mycolicibacterium smegmatis
3.4.17.8 msmeg_2433
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 Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
3.4.17.8 physiological function deletion of two DD-CPase genes, msmeg_2433 and msmeg_2432, both individually and in combination. The single DD-CPase gene deletions have no significant impact on the mycobacterial physiology. In the double-deletion mutant, the predominance in peptidoglycan cross-link formation is shifted from 3-3 cross-links to 4-3, cell surface glycopeptidolipid expression is reduced, and susceptibility to beta-lactams and antitubercular agents is enhanced. The survival rate of the double mutant within murine macrophages is higher than that of the parent. The complementation with any one of the DD-CPase genes can restore the wild-type phenotype Mycolicibacterium smegmatis