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Literature summary for 2.1.2.13 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 PubMed
Search for more literature for 2.1.2.13

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
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)

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
-
 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
 ?
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

Organism UniProt Comment Textmining
Escherichia coli F4SGI5
-
-
Escherichia coli W3110 F4SGI5
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA resin column chromatography 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
-
 Escherichia coli 5,6,7,8-tetrahydrofolate + UDP-4-deoxy-4-formamido-beta-L-arabinopyranose
-
 ?
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
-
 ?
additional information the bifunctional enzyme has N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively Escherichia coli ?
-
 ?
additional information the bifunctional enzyme has N- and C-terminal domains catalyzing formylation and oxidative decarboxylation reactions, respectively Escherichia coli W3110 ?
-
 ?

Subunits

Subunits Comment Organism
hexamer x-ray crystallography Escherichia coli

Synonyms

Synonyms Comment Organism
ArnA
-
 Escherichia coli
Pmrl
-
 Escherichia coli

General Information

General Information Comment Organism
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