Literature summary for 2.1.2.13 extracted from

  • Breazeale, S.D.; Ribeiro, A.A.; McClerren, A.L.; Raetz, C.R.
    A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-Amino-4-deoxy-L-arabinose. Identification and function oF UDP-4-deoxy-4-formamido-L-arabinose (2005), J. Biol. Chem., 280, 14154-14167.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
overexpression of ArnA as a hexahistidine fusion protein, cloning and expression the separate domains in pET28b and pWSK29 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 bi-functional enzyme, the oxidative decarboxylation of UDP-glucuronic acid is catalyzed by the 345-residue C-terminal domain of ArnA. The 304-residue N-terminal domain catalyzes the N-10-formyltetrahydrofolate-dependent formylation of the 4''-amine of UDP-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose). The two domains of ArnA are expressed independently as active proteins in Escherichia coli. Both are required for maintenance of polymyxin resistance and L-4-amino-4-deoxy-L-arabinose modification of lipid A. Only the formylated sugar nucleotide is converted in vitro to an undecaprenyl phosphate-linked form by the enzyme ArnC 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
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Organism

Organism UniProt Comment Textmining
Escherichia coli
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Purification (Commentary)

Purification (Comment) Organism
recombinant 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 bi-functional enzyme, the oxidative decarboxylation of UDP-glucuronic acid is catalyzed by the 345-residue C-terminal domain of ArnA. The 304-residue N-terminal domain catalyzes the N-10-formyltetrahydrofolate-dependent formylation of the 4''-amine of UDP-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose). The two domains of ArnA are expressed independently as active proteins in Escherichia coli. Both are required for maintenance of polymyxin resistance and L-4-amino-4-deoxy-L-arabinose modification of lipid A. Only the formylated sugar nucleotide is converted in vitro to an undecaprenyl phosphate-linked form by the enzyme ArnC 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 bi-functional enzyme. The oxidative decarboxylation of UDP-glucuronic acid is catalyzed by the 345-residue C-terminal domain of ArnA. The 304-residue N-terminal domain catalyzes the N-10-formyltetrahydrofolate-dependent formylation of the 4''-amine of UDP-L-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose) Escherichia coli 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose the major isomer is the cis-formamido rotamer ?

Synonyms

Synonyms Comment Organism
ArnAFT ArnA is a bifunctional enzyme, ArnAFT protein consists of the first 304 amino acids of ArnA, with Asn-305 converted to a stop codon Escherichia coli
ArnA formyltransferase
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Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
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assay at Escherichia coli