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Literature summary 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)

EC Number Cloned (Comment) Organism
1.1.1.305 overexpression of ArnA as a hexahistidine fusion protein, cloning and expression the separate domains in pET28b and pWSK29 Escherichia coli
2.1.2.13 overexpression of ArnA as a hexahistidine fusion protein, cloning and expression the separate domains in pET28b and pWSK29 Escherichia coli
2.7.8.B2
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.305 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+
-
 ?
2.1.2.13 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
-
 ?
2.7.8.B2 UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + undecaprenyl phosphate Escherichia coli
-
 UDP + 4-deoxy-4-formamido-beta-L-arabinopyranosyl undecaprenyl phosphate
-
 ?
3.5.1.B13 4-deoxy-4-formamido-beta-L-arabinopyranosyl undecaprenyl phosphate + H2O Escherichia coli because the L-Ara4N unit attached to lipid A is not derivatized with a formyl group, the existence of a deformylase, acting later in the pathway, is postulated. The requirement of the ArnA formyltransferase reaction for the maintenance of polymyxin resistance suggests that an as yet unidentified deformylase must also exist, since neither L-Ara4N-modified lipid A nor the L-Ara4N donor, undecaprenyl phosphate-L-Ara4N, is formylated when isolated from polymyxin resistant cells 4-amino-4-deoxy-alpha-L-arabinose-undecaprenyl phosphate + formate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.305 Escherichia coli
-
-
-
2.1.2.13 Escherichia coli
-
-
-
2.4.2.53 Escherichia coli
-
-
-
2.7.8.B2 Escherichia coli
-
-
-
3.5.1.B13 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.305 recombinant Escherichia coli
2.1.2.13 recombinant Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.305 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+
-
 ?
1.1.1.305 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+
-
 ?
2.1.2.13 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
-
 ?
2.1.2.13 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 ?
2.4.2.53 UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + ditrans,polycis-undecaprenyl phosphate
-
 Escherichia coli UDP + 4-deoxy-4-formamido-alpha-L-arabinopyranosyl ditrans,polycis-undecaprenyl phosphate
-
 ?
2.7.8.B2 UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + undecaprenyl phosphate
-
 Escherichia coli UDP + 4-deoxy-4-formamido-beta-L-arabinopyranosyl undecaprenyl phosphate
-
 ?
2.7.8.B2 UDP-4-deoxy-4-formamido-beta-L-arabinopyranose + undecaprenyl phosphate membranes of Escherichis coli cells overexpressing ArnC efficiently convert UDP-4-deoxy-4-formamido-beta-L-arabinose but not L-4-amino-4-deoxy-L-arabinose to lipid product Escherichia coli UDP + 4-deoxy-4-formamido-beta-L-arabinopyranosyl undecaprenyl phosphate
-
 ?
3.5.1.B13 4-deoxy-4-formamido-beta-L-arabinopyranosyl undecaprenyl phosphate + H2O
-
 Escherichia coli 4-amino-4-deoxy-alpha-L-arabinose-undecaprenyl phosphate + formate
-
 ?
3.5.1.B13 4-deoxy-4-formamido-beta-L-arabinopyranosyl undecaprenyl phosphate + H2O because the L-Ara4N unit attached to lipid A is not derivatized with a formyl group, the existence of a deformylase, acting later in the pathway, is postulated. The requirement of the ArnA formyltransferase reaction for the maintenance of polymyxin resistance suggests that an as yet unidentified deformylase must also exist, since neither L-Ara4N-modified lipid A nor the L-Ara4N donor, undecaprenyl phosphate-L-Ara4N, is formylated when isolated from polymyxin resistant cells Escherichia coli 4-amino-4-deoxy-alpha-L-arabinose-undecaprenyl phosphate + formate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.1.1.305 ArnA dehydrogenase
-
 Escherichia coli
1.1.1.305 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
1.1.1.305 UDP-GlcUA dehydrogenase
-
 Escherichia coli
2.1.2.13 ArnA formyltransferase
-
 Escherichia coli
2.1.2.13 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
2.4.2.53 ArnC
-
 Escherichia coli
3.5.1.B13 polymyxin resistance protein pmrJ
-
 Escherichia coli
3.5.1.B13 undecaprenyl-phosphate-alpha-L-Ara4FN deformylase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.305 30
-
 assay at Escherichia coli
2.1.2.13 30
-
 assay at Escherichia coli
2.7.8.B2 30
-
 assay at Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.305 7.5
-
 assay at Escherichia coli
2.1.2.13 7.5
-
 assay at Escherichia coli
2.7.8.B2 7.5
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.305 NAD+
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
2.4.2.53 physiological function enzyme takes part in the biosynthesis of UDP-4-amino-4-deoxy-L-arabinose in polymyxin-resistant Escherichia coli. The N-formylation of UDP-4-amino-4-deoxy-L-arabinose is an obligatory step in the biosynthesis of 4-amino-4-deoxy-L-arabinose-modified lipid A in polymyxin-resistant mutants. Only the formylated sugar nucleotide is converted in vitro to an undecaprenyl phosphate-linked form by the enzyme ArnC. Because the L-Ara4N unit attached to lipid A is not derivatized with a formyl group, a deformylase must be acting later in the pathway Escherichia coli