Literature summary for 2.1.2.13 extracted from

  • Gatzeva-Topalova, P.Z.; May, A.P.; Sousa, M.C.
    Crystal structure and mechanism of the Escherichia coli ArnA (PmrI) transformylase domain. An enzyme for lipid A modification with 4-amino-4-deoxy-L-arabinose and polymyxin resistance (2005), Biochemistry, 44, 5328-5338.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
ArnA transformylase domain Escherichia coli

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion method, crystal structure of the ArnA transformylase domain is solved to 1.7 A resolution Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose Escherichia coli ArnA is a key enzyme in the 4-amino-4-deoxy-L-arabinose-lipid A modification pathway. It is a bifunctional enzyme catalyzing the oxidative decarboxylation of UDP-glucuronic acid to the UDP-4''-ketopentose (UDP-beta-L-threo-pentapyranosyl-4''-ulose) and the N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The transformylase activity of the Escherichia coli ArnA is contained in its 300 N-terminal residues 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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Organism

Organism UniProt Comment Textmining
Escherichia coli P77398
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Purification (Commentary)

Purification (Comment) Organism
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Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose ArnA is a key enzyme in the 4-amino-4-deoxy-L-arabinose-lipid A modification pathway. It is a bifunctional enzyme catalyzing the oxidative decarboxylation of UDP-glucuronic acid to the UDP-4''-ketopentose (UDP-beta-L-threo-pentapyranosyl-4''-ulose) and the N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The transformylase activity of the Escherichia coli ArnA is contained in its 300 N-terminal residues Escherichia coli 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose ArnA is a key enzyme in the 4-amino-4-deoxy-L-arabinose-lipid A modification pathway. It is a bifunctional enzyme catalyzing the oxidative decarboxylation of UDP-glucuronic acid to the UDP-4''-ketopentose (UDP-beta-L-threo-pentapyranosyl-4''-ulose) and the N-10-formyltetrahydrofolate-dependent formylation of UDP-4-amino-4-deoxy-L-arabinose. The transformylase activity of the Escherichia coli ArnA is contained in its 300 N-terminal residues. A mechanism for the transformylation reaction is proposed, catalyzed by ArnA involving residues N102, H104, and D140 Escherichia coli 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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