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Literature summary extracted from

  • Senzani, S.; Li, D.; Bhaskar, A.; Ealand, C.; Chang, J.; Rimal, B.; Liu, C.; Joon Kim, S.; Dhar, N.; Kana, B.
    An Amidase_3 domain-containing N-acetylmuramyl-L-alanine amidase is required for mycobacterial cell division (2017), Sci. Rep., 7, 1140 .
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
3.5.1.28 drug development the enzyme is a potential drug target Mycolicibacterium smegmatis

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.28 additional information generation of a deletion mutant of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis, phenotype, detailed overview. deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Ability of the ami1 defective mutant to continue cell division, albeit in an aberrant manner. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cell. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.28 Mycolicibacterium smegmatis A0R5R2
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3.5.1.28 Mycolicibacterium smegmatis ATCC 700084 A0R5R2
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3.5.1.28 Mycolicibacterium smegmatis mc(2)155 A0R5R2
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Synonyms

EC Number Synonyms Comment Organism
3.5.1.28 AMI1
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 Mycolicibacterium smegmatis
3.5.1.28 MSMEG_6281
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 Mycolicibacterium smegmatis
3.5.1.28 Rv3717
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 Mycolicibacterium smegmatis

General Information

EC Number General Information Comment Organism
3.5.1.28 evolution Ami1 belongs to the amidase_3 domain family Mycolicibacterium smegmatis
3.5.1.28 malfunction deletion of MSMEG_6281 encoding enzyme Ami1 in Mycobacterium smegmatis results in the formation of cellular chains, illustrative of cells that are unable to complete division. Viability in the DELTAami1 mutant is maintained through atypical lateral branching, the products of which proceeded to form viable daughter cells. These lateral buds result from mislocalization of DivIVA, a major determinant in facilitating polar elongation in mycobacterial cells. Failure of DELTAami1 mutant cells to separate also leads to dysregulation of FtsZ ring bundling. Loss of Ami1 results in defects in septal peptidoglycan turnover with release of excess cell wall material from the septum or newly born cell poles. Signficant accumulation of 3-3 crosslinked muropeptides is observed in the DELTAami1 mutant. Deletion of ami1 leads to increased cell wall permeability and enhanced susceptiblity to cell wall targeting antibiotics. Lateral budding and ectopic polar growth in the DELTAami1 mutant is facilitated by mislocalization of the cell elongation machinery. Phenotype, detailed overview Mycolicibacterium smegmatis
3.5.1.28 additional information amino acids essential for amidase_3 domain catalytic activity of AmiA in Bacillus anthracis 4229 include H341, E355, H415 and E486 Mycolicibacterium smegmatis
3.5.1.28 physiological function Mycobacteria possess a multi-layered cell wall that requires extensive remodelling during cell division. The amidase_3 domain-containing N-acetylmuramyl-L-alanine amidase is a peptidoglycan remodelling enzyme. The enzyme is required for mycobacterial cell division. Peptidoglycan synthesis is localized to the cell poles and/or septum, a pattern, which is retained upon deletion of ami1 Mycolicibacterium smegmatis