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Literature summary extracted from

  • Genthe, N.A.; Thoden, J.B.; Holden, H.M.
    Structure of the Escherichia coli ArnA N-formyltransferase domain in complex with N5-formyltetrahydrofolate and UDP-Ara4N (2016), Protein Sci., 25, 1555-1562 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.2.13 expressed in Escherichia coli Rosetta2(DE3) cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.1.2.13 N-formyltransferase domain of the enzyme in complex with N5-formyltetrahydrofolate and UDP-4-amino-4-deoxy-beta-L-arabinopyranose, hanging drop vapor diffusion method, using 20-22% poly(ethyleneglycol) 5000, 50 mM MgCl2, 100 mM HEPES (pH 8.0) at 21°C Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.2.13 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose 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 Escherichia coli W3110
-
5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.1.2.13 Escherichia coli F4SGI5
-
-
2.1.2.13 Escherichia coli W3110 F4SGI5
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.2.13 Ni-NTA resin column chromatography Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.2.13 10-formyltetrahydrofolate + UDP-4-amino-4-deoxy-beta-L-arabinopyranose
-
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
-
Escherichia coli W3110 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
?
2.1.2.13 additional information the bifunctional enzyme has N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively Escherichia coli ?
-
-
2.1.2.13 additional information the bifunctional enzyme has N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively Escherichia coli W3110 ?
-
-

Subunits

EC Number Subunits Comment Organism
2.1.2.13 hexamer x-ray crystallography Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.1.2.13 ArnA
-
Escherichia coli
2.1.2.13 Pmrl
-
Escherichia coli

General Information

EC Number General Information Comment Organism
2.1.2.13 metabolism the enzyme is involved in the formation of 4-amino-4-deoxy-L-arabinose. The addition of this sugar to the lipid A moiety of the lipopolysaccharide of pathogenic Gram-negative bacteria allows these organisms to evade the cationic antimicrobial peptides of the host immune system Escherichia coli