Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Protein Variants

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Salmonella enterica subsp. enterica serovar Typhimurium
-
 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 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

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Salmonella enterica subsp. enterica serovar Typhimurium adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 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

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

General Information

EC Number General Information Comment Organism
2.7.8.7 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
2.7.8.7 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
2.7.8.7 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