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Literature summary for 1.1.1.305 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.
UDP-glucuronate + NAD+ Escherichia coli 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). The two domains of ArnA are expressed independently as active proteins in Escherichia coli. Both are required for maintenance of polymyxin resistance and 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 UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
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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.
UDP-glucuronate + NAD+ 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). The two domains of ArnA are expressed independently as active proteins in Escherichia coli. Both are required for maintenance of polymyxin resistance and 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 UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
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UDP-glucuronate + NAD+ 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-4-amino-4-deoxy-L-arabinose, generating the sugar nucleotide, uridine 5'-diphospho-beta-(4-deoxy-4-formamido-L-arabinose) Escherichia coli UDP-beta-L-threo-pentapyranos-4-ulose + CO2 + NADH + H+
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Synonyms

Synonyms Comment Organism
ArnA dehydrogenase
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Escherichia coli
ArnADH ArnA is a bifunctional enzyme, ArnADH protein consists of the C-terminal 345 residues of ArnA, starting at Thr-316 converted to an initiating methionine Escherichia coli
UDP-GlcUA dehydrogenase
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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

Cofactor

Cofactor Comment Organism Structure
NAD+
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Escherichia coli