Literature summary for 6.2.1.59 extracted from

Vergnolle, O.; Chavadi, S.S.; Edupuganti, U.R.; Mohandas, P.; Chan, C.; Zeng, J.; Kopylov, M.; Angelo, N.G.; Warren, J.D.; Soll, C.E.; Quadri, L.E.
Biosynthesis of cell envelope-associated phenolic glycolipids in Mycobacterium marinum (2015), J. Bacteriol., 197, 1040-1050 .

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Organism

Organism	UniProt	Comment	Textmining
Mycobacterium marinum	B2HIN2	-	-
Mycobacterium marinum BAA-535	B2HIN2	-	-

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 marinum	AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]	-	?
a long-chain fatty-acyl adenylate ester + holo-[(phenol)carboxyphthiodiolenone synthase]	-	Mycobacterium marinum BAA-535	AMP + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]	-	?
ATP + a long-chain fatty acid	-	Mycobacterium marinum	diphosphate + a long-chain fatty-acyl adenylate ester	-	?
ATP + a long-chain fatty acid	-	Mycobacterium marinum BAA-535	diphosphate + a long-chain fatty-acyl adenylate ester	-	?
ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase]	-	Mycobacterium marinum	AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]	-	?
ATP + a long-chain fatty acid + holo-[(phenol)carboxyphthiodiolenone synthase]	-	Mycobacterium marinum BAA-535	AMP + diphosphate + a long-chain acyl-[(phenol)carboxyphthiodiolenone synthase]	-	?

General Information

General Information	Comment	Organism
physiological function	PpsA, the first-acting enzyme of a multisubunit noniterative polyketide synthase system is loaded with fatty acids by specific fatty acyl-AMP ligase FadD26 for biosynthesis of phthiocerol dimycocerosates. Deletion of fadD26 produces selective loss of phthiocerol dimycocerosates	Mycobacterium marinum

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Release 2023.1 (January 2023)