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Literature summary for 2.4.2.43 extracted from

  • Impellitteri, N.A.; Merten, J.A.; Bretscher, L.E.; Klug, C.S.
    Identification of a functionally important loop in Salmonella typhimurium ArnT (2010), Biochemistry, 49, 29-35.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C148A/C149A/C173S/C216S/C318S/C383S/C400S/C411S when assayed for growth in the presence of polymyxin, the cysteine-free construct of ArnT supports growth at a level similar to that of the native protein Salmonella enterica subsp. enterica serovar Typhimurium
C148S/C149S/C173S/C216S/C318S/C383S/C400S/C411S mutant enzyme is inactive Salmonella enterica subsp. enterica serovar Typhimurium
C173S/C216S/C318S/C383S/C400S/C411S when assayed for growth in the presence of polymyxin, the cysteine-free construct of ArnT supports growth at 70% of the native protein Salmonella enterica subsp. enterica serovar Typhimurium
additional information analysis of 31 point mutations within a putative periplasmic loop of the cysteine-free ArnT protein, carried out using an in vivo growth assay coupled with expression studies, identification of the first time specific critical residues within the bacterial transferase. These critical residues fall into two categories: those that disrupt initial protein folding or membrane localization and those that fail to confer in vivo resistance to polymyxin despite being expressed to the inner membrane Salmonella enterica subsp. enterica serovar Typhimurium

Localization

Localization Comment Organism GeneOntology No. Textmining
inner membrane
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Salmonella enterica subsp. enterica serovar Typhimurium
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-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate + lipid IVA Salmonella enterica subsp. enterica serovar Typhimurium ArnT confers resistance to the antibiotic polymyxin in Salmonella typhimurium and Escherichia coli through the modification of lipid A, a major component of the outer surface of Gram-negative bacteria. ArnT transfers a neutral aminoarabinose moiety onto the negative phosphate groups of lipid A, reducing the surface charge of the bacteria and preventing cationic peptides such as polymyxin from electrostatically recognizing and killing the bacteria. Only small amounts of ArnT are necessary to provide resistance against polymyxin to the bacterial cell lipid IIA + di-trans,poly-cis-undecaprenyl phosphate
-
?

Organism

Organism UniProt Comment Textmining
Salmonella enterica subsp. enterica serovar Typhimurium
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate + lipid IVA
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Salmonella enterica subsp. enterica serovar Typhimurium lipid IIA + di-trans,poly-cis-undecaprenyl phosphate
-
?
4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,poly-cis-undecaprenyl phosphate + lipid IVA ArnT confers resistance to the antibiotic polymyxin in Salmonella typhimurium and Escherichia coli through the modification of lipid A, a major component of the outer surface of Gram-negative bacteria. ArnT transfers a neutral aminoarabinose moiety onto the negative phosphate groups of lipid A, reducing the surface charge of the bacteria and preventing cationic peptides such as polymyxin from electrostatically recognizing and killing the bacteria. Only small amounts of ArnT are necessary to provide resistance against polymyxin to the bacterial cell Salmonella enterica subsp. enterica serovar Typhimurium lipid IIA + di-trans,poly-cis-undecaprenyl phosphate
-
?

Subunits

Subunits Comment Organism
More the secondary structure of ArnT is not dependent on disulfide bridges, Salmonella typhimurium ArnT contains no disulfide bonds Salmonella enterica subsp. enterica serovar Typhimurium

Synonyms

Synonyms Comment Organism
arnT
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Salmonella enterica subsp. enterica serovar Typhimurium

General Information

General Information Comment Organism
physiological function ArnT confers resistance to the antibiotic polymyxin in Salmonella typhimurium and Escherichia coli through the modification of lipid A, a major component of the outer surface of Gram-negative bacteria. ArnT transfers a neutral aminoarabinose moiety onto the negative phosphate groups of lipid A, reducing the surface charge of the bacteria and preventing cationic peptides such as polymyxin from electrostatically recognizing and killing the bacteria. Only small amounts of ArnT are necessary to provide resistance against polymyxin to the bacterial cell Salmonella enterica subsp. enterica serovar Typhimurium