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Literature summary for 6.2.1.59 extracted from

  • Simeone, R; Léger, M.; Constant, P.; Malaga, W.; Marrakchi, H.; Daffé, M.; Guilhot, C.; Chalut, C.
    Delineation of the roles of FadD22, FadD26 and FadD29 in the biosynthesis of phthiocerol dimycocerosates and related compounds in Mycobacterium tuberculosis (2010), FEBS J., 277, 2715-2725 .
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
a long-chain fatty-acyl adenylate ester + holo-[(phenol)carboxyphthiodiolenone synthase] Mycobacterium tuberculosis variant bovis
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AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
-
?
ATP + a long-chain fatty acid Mycobacterium tuberculosis variant bovis
-
diphosphate + a long-chain fatty-acyl adenylate ester
-
?
ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase] Mycobacterium tuberculosis variant bovis
-
AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
-
?
additional information Mycobacterium tuberculosis variant bovis in vivo, FadD26 specificallyactivates C22-24 fatty acyl chains that are loaded onto phenolcarboxyphthiodiolenone synthase PpsA for the formation of the phthiocerol chain, but FadD26 is not required for the production of phenolic glycolipids ?
-
?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis variant bovis A0A0H3M8A6
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
a long-chain fatty-acyl adenylate ester + holo-[(phenol)carboxyphthiodiolenone synthase]
-
Mycobacterium tuberculosis variant bovis AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
-
?
ATP + a long-chain fatty acid
-
Mycobacterium tuberculosis variant bovis diphosphate + a long-chain fatty-acyl adenylate ester
-
?
ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase]
-
Mycobacterium tuberculosis variant bovis AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]
-
?
additional information in vivo, FadD26 specificallyactivates C22-24 fatty acyl chains that are loaded onto phenolcarboxyphthiodiolenone synthase PpsA for the formation of the phthiocerol chain, but FadD26 is not required for the production of phenolic glycolipids Mycobacterium tuberculosis variant bovis ?
-
?
additional information in vivo, FadD26 specifically activates C22-24 fatty acyl chains that are loaded onto phenolcarboxyphthiodiolenone synthase PpsA for the formation of the phthiocerol chain, but FadD26 is not required for the production of phenolic glycolipids Mycobacterium tuberculosis variant bovis ?
-
?

General Information

General Information Comment Organism
physiological function FadD26 is required for the production of phthiodiolone dimycocerosates but not of phenolic glycolipids. Disruption of FadD26 in Mycobacterium bovis BCG abolishes the production of phthiocerol dimycocerosate (DIM A) and of phthiodiolone dimycocerosate (DIM B) Mycobacterium tuberculosis variant bovis