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Literature summary for 1.3.3.16 extracted from

  • Li, Y.M.; Milne, J.C.; Madison, L.L.; Kolter, R.; Walsh, C.T.
    From peptide precursors to oxazole and thiazole-containing peptide antibiotics microcin B17 synthase (1996), Science, 274, 1188-1193 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2 Escherichia coli
-
a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2
-
?
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2 Escherichia coli
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a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P23184 and P23185 and P23186 P23184 i.e. subunit McbB, P23185 i.e. subunit McBC, P23186 i.e. subunit McbD
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a [protein]-(1S,4R)-2-(C-substituted-aminomethyl)-4-acyl-2-thiazoline + O2
-
Escherichia coli a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-thiazole + H2O2
-
?
a [protein]-(S,S)-2-(C-substituted-aminomethyl)-4-acyl-2-oxazoline + O2
-
Escherichia coli a [protein]-(S)-2-(C-substituted-aminomethyl)-4-acyl-1,3-oxazole + H2O2
-
?

Subunits

Subunits Comment Organism
? x * 33000, subunit McbB, x * 31000, subunit McbC, x * 45000, subunit McbD, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
McbB
-
Escherichia coli
McbC
-
Escherichia coli
McbD
-
Escherichia coli
microcin B17 synthase
-
Escherichia coli

General Information

General Information Comment Organism
physiological function enzyme is part of microcin B17 synthase. The complex three proteins, McbB, McbC, and McbD, that convert 14 residues into the eight mono- and bisheterocyclic moieties in vitro that confer antibiotic activity on mature microcin B17 via a three-step sequence of cyclization, net dehydration, and subsequent two-electron dehydrogenation Escherichia coli