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Literature summary extracted from

  • Admiraal, S.; Walsh, C.; Khosla, C.
    The loading module of rifamycin synthetase is an adenylation - Thiolation didomain with substrate tolerance for substituted benzoates (2001), Biochemistry, 40, 6116-6123 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.74 additional information expression of the N-terminal adenylation and thiolation domain Amycolatopsis mediterranei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.74 ATP + 3-amino-5-hydroxybenzoate + a holo-[acyl-carrier protein] Amycolatopsis mediterranei
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 3-amino-5-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.74 Amycolatopsis mediterranei O54666
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.74 ATP + 3,5-diaminobenzoate + a holo-[acyl-carrier protein]
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 Amycolatopsis mediterranei 3,5-diaminobenzoyl-[acyl-carrier protein] + AMP + diphosphate
-
 ?
6.2.1.74 ATP + 3-amino-5-hydroxybenzoate + a holo-[acyl-carrier protein]
-
 Amycolatopsis mediterranei 3-amino-5-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate
-
 ?
6.2.1.74 ATP + 3-aminobenzoate + a holo-[acyl-carrier protein]
-
 Amycolatopsis mediterranei 3-aminobenzoyl-[acyl-carrier protein] + AMP + diphosphate
-
 ?
6.2.1.74 ATP + 3-hydroxybenzoate + a holo-[acyl-carrier protein]
-
 Amycolatopsis mediterranei 3-hydroxybenzoyl-[acyl-carrier protein] + AMP + diphosphate
-
 ?
6.2.1.74 additional information less than 5% of the activity with 3-amino-5-hydroxybenzoate: 3,5-dihydroxybenzoate, 3-chlorobenzoate, 3-bromobenzoate, benzoate Amycolatopsis mediterranei ?
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-

Synonyms

EC Number Synonyms Comment Organism
6.2.1.74 rifA
-
 Amycolatopsis mediterranei

General Information

EC Number General Information Comment Organism
6.2.1.74 physiological function rifamycin synthetase is primed with a 3-amino-5-hydroxybenzoate starter unit by a loading module that contains domains homologous to the adenylation and thiolation domains of nonribosomal peptide synthetases. The thiolation domain requires covalent attachment of the 4'-phosphopantetheine moiety of CoA to a conserved serine to be active. The catalytic models for the mechanism of the adenylation and thiolation didomain involve activation of 3-amino-5-hydroxybenzoate as the aryl-adenylate by the adenylation domain, followed by eventual formation of a covalent aryl thioester enzyme intermediate from attack of either aryl-CoA or the aryl-adenylate by the thiol nucleophile of the phosphopantetheine cofactor of the thiolation domain Amycolatopsis mediterranei