Literature summary for 2.7.8.7 extracted from

Viala, J.P.; Puppo, R.; My, L.; Bouveret, E.
Posttranslational maturation of the invasion acyl carrier protein of Salmonella enterica serovar Typhimurium requires an essential phosphopantetheinyl transferase of the fatty acid biosynthesis pathway (2013), J. Bacteriol., 195, 4399-4405.

Search for more literature for 2.7.8.7

Protein Variants

Protein Variants	Comment	Organism
additional information	creation of an conditionally inactive acpS mutant	Salmonella enterica subsp. enterica serovar Typhimurium

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]	Salmonella enterica subsp. enterica serovar Typhimurium	-	adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]	-	?
additional information	Salmonella enterica subsp. enterica serovar Typhimurium	phosphopantetheinylation of IacP, i.e. SPI-1, a homologue of acyl carrier proteins. IacP from Salmonella enterica serovar Typhimurium is matured by addition of 4'-phosphopantetheine to the conserved serine 38 residue by enzyme AcpS, an enzyme normally required for the maturation of the canonical acyl carrier protein (ACP), which is involved in fatty acid biosynthesis. Interaction occurs between IacP and AcpS but not between IacP and the other PPTases, suggesting that AcpS is the PPTase responsible for the posttranslational modification occurring on IacP	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Salmonella enterica subsp. enterica serovar Typhimurium	P63466	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]	-	Salmonella enterica subsp. enterica serovar Typhimurium	adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]	-	?
additional information	phosphopantetheinylation of IacP, i.e. SPI-1, a homologue of acyl carrier proteins. IacP from Salmonella enterica serovar Typhimurium is matured by addition of 4'-phosphopantetheine to the conserved serine 38 residue by enzyme AcpS, an enzyme normally required for the maturation of the canonical acyl carrier protein (ACP), which is involved in fatty acid biosynthesis. Interaction occurs between IacP and AcpS but not between IacP and the other PPTases, suggesting that AcpS is the PPTase responsible for the posttranslational modification occurring on IacP	Salmonella enterica subsp. enterica serovar Typhimurium	?	-	?

Synonyms

Synonyms	Comment	Organism
AcpS	-	Salmonella enterica subsp. enterica serovar Typhimurium
phosphopantetheinyl transferase	-	Salmonella enterica subsp. enterica serovar Typhimurium
PPTase	-	Salmonella enterica subsp. enterica serovar Typhimurium

General Information

General Information	Comment	Organism
malfunction	growth defect due to depletion of AcpS. A conditional acpS mutant of AcpS does not catalyze the maturation of IacP, a homologue of acyl carrier proteins. IacP does not complement the lethal phenotype associated with ACP defect in Escherichia coli strain strain EB337	Salmonella enterica subsp. enterica serovar Typhimurium
metabolism	the demonstration that ACP homologue IacP is matured by AcpS establishes a cross-connection between virulence and fatty acid biosynthesis pathways	Salmonella enterica subsp. enterica serovar Typhimurium
physiological function	PPTase AcpS is essential in Salmonella. Acyl carrier proteins are mainly involved in fatty acid biosynthesis, and they require posttranslational maturation by addition of a 4'-phosphopantetheine prosthetic group to be functional, analysis of SPI-1 or IacP, a homologue of acyl carrier proteins, maturation in vivo, overview. Although IacP is similar to ACP and matured by using the same enzyme, IacP cannot replace the essential function of ACP in fatty acid synthesis	Salmonella enterica subsp. enterica serovar Typhimurium

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Release 2023.1 (January 2023)