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Literature summary extracted from

  • Beld, J.; Sonnenschein, E.C.; Vickery, C.R.; Noel, J.P.; Burkart, M.D.
    The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life (2014), Nat. Prod. Rep., 31, 61-108.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.7.8.7 synthesis the broad specificity of the single PPTase present in Pseudomonas can be used to 4'-phosphopantetheinylate various carrier proteins Pseudomonas aeruginosa

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.8.7 gene bli, functional recombinant expression in Escherichia coli Bacillus licheniformis
2.7.8.7 gene BPSS2266 Burkholderia pseudomallei
2.7.8.7 gene clbA, in family II PPTases, the genes encoding the PPTase often reside in close proximity to, or part of, a synthase operon Escherichia coli
2.7.8.7 gene entD, in family II PPTases, the genes encoding the PPTase often reside in close proximity to, or part of, a synthase operon Escherichia coli
2.7.8.7 gene gsp Brevibacillus brevis
2.7.8.7 gene pobA Burkholderia cenocepacia
2.7.8.7 gene sfp, in family II PPTases, the genes encoding the PPTase often reside in close proximity to, or part of, a synthase operon Escherichia coli
2.7.8.7 gene XALc_0101, DNA and amino acid sequence determination and analysis, the Xab gene cluster is expressed on two plasmids in Xanthomonas axonopodis pv. vesicatoria, and showa a 6fold increased yield of the antibiotic albicidin Xanthomonas albilineans
2.7.8.7 genes PswP, SMA4147, and SMA2452 Serratia marcescens
2.7.8.7 genes sfp or entD, in family II PPTases, the genes encoding the PPTase often reside in close proximity to, or part of, a synthase operon Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
2.7.8.7 additional information construction of a conditional pptT mutant in Mycobacterium tuberculosis strain H37Rv showing retarded growth and persistence. Construction of mutants in which the PPTase gene is controlled by a tetracycline promoter, for conditional regulation of the PptT expression Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.8.7 28000
-
-
 Streptomyces coelicolor
2.7.8.7 28000
-
-
 Escherichia coli

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] Burkholderia cenocepacia
-
 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Burkholderia pseudomallei
-
 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Serratia marcescens
-
 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Bacillus licheniformis Bli is the PPTase that phosphopantetheinylates the PCP domain of this elongating synthase adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Vibrio cholerae both VibB and VibF are phosphopantetheinylated by the PPTase VibD adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Pseudomonas aeruginosa enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Vibrio anguillarum phosphopantetheinylation of VabF adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Streptomyces coelicolor PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The carrier protein tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Brevibacillus brevis PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Streptomyces coelicolor PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Escherichia coli PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Escherichia coli PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Bacillus subtilis PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Mycobacterium tuberculosis PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. The Mycobacterium tuberculosis enzyme activates mycobatin. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Xanthomonas albilineans the enzyme activates the antibiotic albicidin adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Bacillus anthracis the enzyme activates the siderophore petrobactin. The synthase-encoding cluster contains a stand-alone PCP domain, AsbD, which is phosphopantetheinylated by a PPTase. There is no PPTase present in the gene cluster itself and it is suggested that BA2375, an EntD homologue present in the enterobactin gene cluster, serves as the PPTase that installs the 4'-phosphopantetheinyl arm on AsbD. Holo-AsbD is loaded with 3,4-dihydroxybenzoic acid by AsbC and this AsbD conjugate functions as the substrate for AsbE. AsbE, together with the stand-alone synthases AsbA and AsbB, catalyze the formation of petrobactin adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Yersinia pestis the enzyme activates yersiniabactin adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Bacillus subtilis 168 PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Xanthomonas albilineans GPE PC73 the enzyme activates the antibiotic albicidin adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Serratia marcescens Db11
-
 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Vibrio anguillarum ATCC 68554 phosphopantetheinylation of VabF adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Pseudomonas aeruginosa DSM 22644 enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Streptomyces coelicolor ATCC BAA-471 PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Mycobacterium tuberculosis H37Rv PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. The Mycobacterium tuberculosis enzyme activates mycobatin. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Burkholderia pseudomallei K96243
-
 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.8.7 Bacillus anthracis
-
-
-
2.7.8.7 Bacillus licheniformis
-
-
-
2.7.8.7 Bacillus subtilis P39135
-
-
2.7.8.7 Bacillus subtilis 168 P39135
-
-
2.7.8.7 Brevibacillus brevis
-
-
-
2.7.8.7 Burkholderia cenocepacia Q27IP6
-
-
2.7.8.7 Burkholderia pseudomallei Q63I03
-
-
2.7.8.7 Burkholderia pseudomallei K96243 Q63I03
-
-
2.7.8.7 Escherichia coli E2QFX9
-
-
2.7.8.7 Escherichia coli P19925
-
-
2.7.8.7 Escherichia coli P24224
-
-
2.7.8.7 Escherichia coli Q0P7J0
-
-
2.7.8.7 Mycobacterium tuberculosis P9WQD3
-
-
2.7.8.7 Mycobacterium tuberculosis H37Rv P9WQD3
-
-
2.7.8.7 Pseudomonas aeruginosa Q9I4H2
-
-
2.7.8.7 Pseudomonas aeruginosa DSM 22644 Q9I4H2
-
-
2.7.8.7 Serratia marcescens Q75PZ2 Db11
-
2.7.8.7 Serratia marcescens Db11 Q75PZ2 Db11
-
2.7.8.7 Streptomyces coelicolor
-
-
-
2.7.8.7 Streptomyces coelicolor O86785
-
-
2.7.8.7 Streptomyces coelicolor O88029
-
-
2.7.8.7 Streptomyces coelicolor ATCC BAA-471 O86785
-
-
2.7.8.7 Vibrio anguillarum Q5DK20
-
-
2.7.8.7 Vibrio anguillarum ATCC 68554 Q5DK20
-
-
2.7.8.7 Vibrio cholerae Q9RCF2
-
-
2.7.8.7 Xanthomonas albilineans D2U8G6
-
-
2.7.8.7 Xanthomonas albilineans GPE PC73 D2U8G6
-
-
2.7.8.7 Yersinia pestis Q74V64
-
-

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]
-
 Brevibacillus brevis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Bacillus anthracis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Burkholderia cenocepacia adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Burkholderia pseudomallei adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Serratia marcescens adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Vibrio anguillarum adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Vibrio cholerae adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Xanthomonas albilineans adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] Bli is the PPTase that phosphopantetheinylates the PCP domain of this elongating synthase Bacillus licheniformis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] both VibB and VibF are phosphopantetheinylated by the PPTase VibD Vibrio cholerae adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins Pseudomonas aeruginosa adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] phosphopantetheinylation of VabF Vibrio anguillarum adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The carrier protein tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases Streptomyces coelicolor adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases Brevibacillus brevis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases Streptomyces coelicolor adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases Escherichia coli adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase Escherichia coli adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase Bacillus subtilis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. The Mycobacterium tuberculosis enzyme activates mycobatin. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis Mycobacterium tuberculosis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme activates the antibiotic albicidin Xanthomonas albilineans adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme activates the siderophore petrobactin. The synthase-encoding cluster contains a stand-alone PCP domain, AsbD, which is phosphopantetheinylated by a PPTase. There is no PPTase present in the gene cluster itself and it is suggested that BA2375, an EntD homologue present in the enterobactin gene cluster, serves as the PPTase that installs the 4'-phosphopantetheinyl arm on AsbD. Holo-AsbD is loaded with 3,4-dihydroxybenzoic acid by AsbC and this AsbD conjugate functions as the substrate for AsbE. AsbE, together with the stand-alone synthases AsbA and AsbB, catalyze the formation of petrobactin Bacillus anthracis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme activates yersiniabactin Yersinia pestis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] broad specificity of the single PPTase Pseudomonas aeruginosa adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the carrier protein of Colibactin is phosphopantetheinylated by the family II PPTase ClbA Escherichia coli adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the carrier protein of the enterobactin synthase complex, EntF, is phosphopantetheinylated by the family II PPTase EntD. In vitro EntD seems to modify apo-AcpP from Escherichia coli, albeit at a very slow rate Escherichia coli adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme AcpS is active with type II FAS ACP, AcpP, but the enzyme accepts not only bacterial AcpP but a variety of CPs from type II elongating systems including Lactobacillus casei D-alanyl carrier protein, Rhizobia protein NodF and Streptomyces ACPs involved in frenolicin, granaticin, oxytetracycline and tetracenomycin polyketide biosynthesis Escherichia coli adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme activates bacitracin and in vitro also tyrocidin synthase Bacillus licheniformis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme activates mycobatin Mycobacterium tuberculosis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme Sfp is active with surfactin synthase peptidyl carrier protein Bacillus subtilis adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme Sfp is active with surfactin synthase peptidyl carrier protein. Sfp shows highly permissive catalytic activity towards CPs using not only CoA but CoA-like substrates Escherichia coli adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Sfp is the PPTase necessary for installing PPant on the PCP of surfactin synthase Bacillus subtilis 168 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme Sfp is active with surfactin synthase peptidyl carrier protein Bacillus subtilis 168 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Xanthomonas albilineans GPE PC73 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme activates the antibiotic albicidin Xanthomonas albilineans GPE PC73 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Serratia marcescens Db11 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Vibrio anguillarum ATCC 68554 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] phosphopantetheinylation of VabF Vibrio anguillarum ATCC 68554 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins Pseudomonas aeruginosa DSM 22644 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] broad specificity of the single PPTase Pseudomonas aeruginosa DSM 22644 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases Streptomyces coelicolor ATCC BAA-471 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. The Mycobacterium tuberculosis enzyme activates mycobatin. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis Mycobacterium tuberculosis H37Rv adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] the enzyme activates mycobatin Mycobacterium tuberculosis H37Rv adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Burkholderia pseudomallei K96243 adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Streptomyces coelicolor ?
-
 ?
2.7.8.7 CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
-
 Streptomyces coelicolor ATCC BAA-471 ?
-
 ?
2.7.8.7 additional information besides enterobactin and colibactin, some Escherichia coli strains also produce yersiniabactin. Yersiniabactin is encoded by the high-pathogenicity island and in contrast to Yersinia pestis (in Yersinia pestis YbtD is the dedicated PPTase) no PPTase is found in the Escherichia coli genome that seems to activate this synthase Escherichia coli ?
-
 ?
2.7.8.7 additional information carrier proteins from type I elongating systems are not substrates for AcpS. Inability of Escherichia coli AcpS to install a PPant arm on apo-EntF, the bacterial enterobactin synthase, or apo-TycA, the Bacillus brevis tyrocidine synthase Escherichia coli ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.8.7 homodimer Sfp exists as a pseudo-homodimer of about 240 aa, resembling two AcpS monomers with one active site at the pseudo-dimer interface, and possesses a much broader substrate acceptance Brevibacillus brevis
2.7.8.7 homodimer Sfp exists as a pseudo-homodimer of about 240 aa, resembling two AcpS monomers with one active site at the pseudo-dimer interface, and possesses a much broader substrate acceptance Escherichia coli
2.7.8.7 homodimer Sfp exists as a pseudo-homodimer of about 240 aa, resembling two AcpS monomers with one active site at the pseudo-dimer interface, and possesses a much broader substrate acceptance Bacillus subtilis
2.7.8.7 homotrimer 3 * 28000, AcpS has a quaternary structure with active sites shared across each homotypic interface Streptomyces coelicolor
2.7.8.7 homotrimer 3 * 28000, AcpS has a quaternary structure with active sites shared across each homotypic interface Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Brevibacillus brevis
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Bacillus licheniformis
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Streptomyces coelicolor
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Bacillus anthracis
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Escherichia coli
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Bacillus subtilis
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Burkholderia cenocepacia
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Mycobacterium tuberculosis
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Yersinia pestis
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Serratia marcescens
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Vibrio anguillarum
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Vibrio cholerae
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Pseudomonas aeruginosa
2.7.8.7 4'-phosphopantetheinyl transferase
-
 Xanthomonas albilineans
2.7.8.7 AcpS
-
 Escherichia coli
2.7.8.7 AcpS
-
 Streptomyces coelicolor
2.7.8.7 Bli
-
 Bacillus licheniformis
2.7.8.7 BPSS2266
-
 Burkholderia pseudomallei
2.7.8.7 ClbA
-
 Escherichia coli
2.7.8.7 dpj
-
 Escherichia coli
2.7.8.7 EntD
-
 Bacillus subtilis
2.7.8.7 EntD
-
 Escherichia coli
2.7.8.7 gsp
-
 Brevibacillus brevis
2.7.8.7 holo-ACP synthase
-
 Streptomyces coelicolor
2.7.8.7 holo-ACP synthase
-
 Escherichia coli
2.7.8.7 holo-acyl carrier protein synthase
-
 Bacillus licheniformis
2.7.8.7 holo-acyl carrier protein synthase
-
 Streptomyces coelicolor
2.7.8.7 holo-acyl carrier protein synthase
-
 Bacillus anthracis
2.7.8.7 holo-acyl carrier protein synthase
-
 Escherichia coli
2.7.8.7 holo-acyl carrier protein synthase
-
 Mycobacterium tuberculosis
2.7.8.7 holo-acyl carrier protein synthase
-
 Yersinia pestis
2.7.8.7 holo-acyl carrier protein synthase
-
 Serratia marcescens
2.7.8.7 holo-acyl carrier protein synthase
-
 Vibrio anguillarum
2.7.8.7 holo-acyl carrier protein synthase
-
 Vibrio cholerae
2.7.8.7 holo-acyl carrier protein synthase
-
 Pseudomonas aeruginosa
2.7.8.7 holo-acyl carrier protein synthase
-
 Xanthomonas albilineans
2.7.8.7 MtAcpS
-
 Mycobacterium tuberculosis
2.7.8.7 PaPcpS
-
 Pseudomonas aeruginosa
2.7.8.7 PcpS
-
 Pseudomonas aeruginosa
2.7.8.7 pcpS PA1165 gene name, UniProt Pseudomonas aeruginosa
2.7.8.7 phosphopantetheinyl transferase
-
 Brevibacillus brevis
2.7.8.7 phosphopantetheinyl transferase
-
 Bacillus licheniformis
2.7.8.7 phosphopantetheinyl transferase
-
 Streptomyces coelicolor
2.7.8.7 phosphopantetheinyl transferase
-
 Bacillus anthracis
2.7.8.7 phosphopantetheinyl transferase
-
 Escherichia coli
2.7.8.7 phosphopantetheinyl transferase
-
 Bacillus subtilis
2.7.8.7 phosphopantetheinyl transferase
-
 Burkholderia cenocepacia
2.7.8.7 phosphopantetheinyl transferase
-
 Mycobacterium tuberculosis
2.7.8.7 phosphopantetheinyl transferase
-
 Yersinia pestis
2.7.8.7 phosphopantetheinyl transferase
-
 Serratia marcescens
2.7.8.7 phosphopantetheinyl transferase
-
 Vibrio anguillarum
2.7.8.7 phosphopantetheinyl transferase
-
 Vibrio cholerae
2.7.8.7 phosphopantetheinyl transferase
-
 Pseudomonas aeruginosa
2.7.8.7 phosphopantetheinyl transferase
-
 Xanthomonas albilineans
2.7.8.7 PobA
-
 Burkholderia cenocepacia
2.7.8.7 PPTase
-
 Brevibacillus brevis
2.7.8.7 PPTase
-
 Bacillus licheniformis
2.7.8.7 PPTase
-
 Streptomyces coelicolor
2.7.8.7 PPTase
-
 Bacillus anthracis
2.7.8.7 PPTase
-
 Escherichia coli
2.7.8.7 PPTase
-
 Bacillus subtilis
2.7.8.7 PPTase
-
 Burkholderia cenocepacia
2.7.8.7 PPTase
-
 Mycobacterium tuberculosis
2.7.8.7 PPTase
-
 Yersinia pestis
2.7.8.7 PPTase
-
 Serratia marcescens
2.7.8.7 PPTase
-
 Vibrio anguillarum
2.7.8.7 PPTase
-
 Vibrio cholerae
2.7.8.7 PPTase
-
 Pseudomonas aeruginosa
2.7.8.7 PPTase
-
 Xanthomonas albilineans
2.7.8.7 PptT
-
 Mycobacterium tuberculosis
2.7.8.7 PswP
-
 Serratia marcescens
2.7.8.7 redU
-
 Streptomyces coelicolor
2.7.8.7 SCO6673
-
 Streptomyces coelicolor
2.7.8.7 Sfp
-
 Brevibacillus brevis
2.7.8.7 Sfp
-
 Escherichia coli
2.7.8.7 Sfp
-
 Bacillus subtilis
2.7.8.7 Sfp-type PPTase
-
 Pseudomonas aeruginosa
2.7.8.7 surfactin phosphopantetheinyl transferase
-
 Brevibacillus brevis
2.7.8.7 surfactin phosphopantetheinyl transferase
-
 Escherichia coli
2.7.8.7 surfactin phosphopantetheinyl transferase
-
 Bacillus subtilis
2.7.8.7 VabD
-
 Vibrio anguillarum
2.7.8.7 VibD
-
 Vibrio cholerae
2.7.8.7 XabA
-
 Xanthomonas albilineans
2.7.8.7 XALc_0101
-
 Xanthomonas albilineans
2.7.8.7 YbtD
-
 Yersinia pestis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.8.7 additional information
-
 the MtAcpS enzyme protein undergoes conformational changes at pHs below pH 6.5, with results in decreases in AcpS activity Mycobacterium tuberculosis

Expression

EC Number Organism Comment Expression
2.7.8.7 Burkholderia pseudomallei the enzyme is upregulated during infection of the human host up

General Information

EC Number General Information Comment Organism
2.7.8.7 evolution BPSS2266 is a PPTase of the 4'-phosphopantetheinyl transferase superfamily Burkholderia pseudomallei
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Bacillus licheniformis
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Streptomyces coelicolor
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Bacillus anthracis
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Escherichia coli
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Mycobacterium tuberculosis
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Yersinia pestis
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Serratia marcescens
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Vibrio anguillarum
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Vibrio cholerae
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases Xanthomonas albilineans
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. Pseudomonas aeruginosa contains one Sfp-type PPTase, PaPcpS or PcpS with broad substrate specificity, but no AcpS-type PPTase Pseudomonas aeruginosa
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 42–48 aa for AcpS (family I) and 38–41 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain Brevibacillus brevis
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 42–48 aa for AcpS (family I) and 38–41 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain Escherichia coli
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 42–48 aa for AcpS (family I) and 38–41 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain Bacillus subtilis
2.7.8.7 evolution phosphopantetheinyl transferases (PPTases) are essential for cell viability across all three domains of life: bacteria, archaea and eukaryota. Holo-ACP synthase (AcpS) is the archetypical enzyme of the first family of PPTases recognized. Surfactin phosphopantetheinyl transferase (Sfp) represents the second family of PPTases. The third family of PPTases are translationally fused C-terminal transferases residing in the megasynthases as one of several catalytic domains acting in type I yeast and fungal FAS megasynthases. This third family of PPTases post-translationally modify apo-ACPs prior to assembly of the megasynthases. The second family enzymes contain two highly conserved regions, called ppt-1 and ppt-3, generalized as the bipartite sequence, (I/V/L)G(I/V/L/T)D(I/V/L/A)(x)n(F/W)(A/S/T/C)xKE(S/A)h(h/S)K(A/G), where x are chemically disparate amino acids, n is 42–48 aa for AcpS (family I) and 38–41 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain. The toxin found in a hybrid PKS-NRPS cluster, (also known as PKS island) produces colibactin. Within this cluster, clbA is identified as a PPTase Escherichia coli
2.7.8.7 malfunction a conditional pptT mutant in Mycobacterium. tuberculosis H37Rv shows retarded growth and persistence. Mutant cells fail to multiply in vivo Mycobacterium tuberculosis
2.7.8.7 malfunction a VabD knockout strain shows no retarded growth under iron-rich conditions, but reduced growth under iron-depletion Vibrio anguillarum
2.7.8.7 malfunction a xabA knockout strain does not produce albicidin, but when EntD is engineered into the mutant strain, production is restored to wild-type levels Xanthomonas albilineans
2.7.8.7 malfunction enzyme mutation is lethal Pseudomonas aeruginosa
2.7.8.7 malfunction gene entD knockout in Escherichia coli strain AN90-60 results in a strain that does not produce enterobactin. Overproduction of AcpS cannot compensate the absence of EntD. Conversely, overexpressing entD on an inducible plasmid cannot complement the absence of acpS. The pobA gene from Burkholderia cenocepacia is shown to efficiently complement an Escherichia coli entD mutant Escherichia coli
2.7.8.7 malfunction mutants of PswP are unable to produce pigment or surfactant but are still able to produce 2-methyl-3-n-amyl-pyrrole (MAP) and condense it with supplied 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC) to form prodigiosin. Althiomycin production is eliminated upon deletion of one PPTase gene, SMA2452, whereas the other PPTase gene mutation, SMA4147, has no effect Serratia marcescens
2.7.8.7 malfunction overproduction of AcpS cannot compensate the absence of EntD. Conversely, overexpressing entD on an inducible plasmid cannot complement the absence of acpS Escherichia coli
2.7.8.7 physiological function PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis. AcpSs are primarily used for post-translational modification and activation of the carrier proteins of FASs (primary metabolism) across a diversity of organisms making them the most commonly found PPTase Escherichia coli
2.7.8.7 physiological function PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis Escherichia coli
2.7.8.7 physiological function PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis Bacillus subtilis
2.7.8.7 physiological function PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis. Enzyme Gsp plays a role in gramicidin S biosynthesis Brevibacillus brevis
2.7.8.7 physiological function PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. The PPTase ClbA can activate both siderophore and genotoxin biosynthesis Escherichia coli
2.7.8.7 physiological function some Vibrio anguillarum strains produce the siderophore vanchrobactin utilizing the NRPS VabF. VabD is the dedicated PPTase used for 4'-phosphopantetheinylation of VabF. Vibrio anguillarum strains also contain a second, more dominant, siderophore anguibactin, located on the pJM1 plasmid. Anguibactin is also synthesized by an NRPS and requires the PPTase AngD. Both VabD and AngD can complement one another, but since anguibactin is the more potent siderophore, some strains have lost the vanchrobactin biosynthesis pathway Vibrio anguillarum
2.7.8.7 physiological function Streptomyces coelicolor contains 25 biosynthetic secondary metabolite clusters that produce natural products, including actinorhodin, coelichelin, coelibactin, TW95a, EPA, methylenomycin (encoded on a giant linear plasmid), prodiginines and the antibiotic CDA. All of these natural products are produced by synthases that require phoshopantetheinylation by an AcpS-type PPTase, which shows a high level of permissiveness for CoA substrates as well as carrier proteins. For example, type I mammalian FAS, type I fungal PKS, and several type II bacterial ACPs are efficiently phosphopantetheinylated. The genome of Streptomyces coelicolor contains two other PPTases: RedU, which is a dedicated PPTase for undecylprodigiosin biosynthesis, and SCO6673 required for CDA biosynthesis. Both RedU and SCO6673 have specific carrier protein targets, whereas ScAcpS shows broad activity. The crystal structure of ScAcpS shows the structural basis for relaxed substrate selection Streptomyces coelicolor
2.7.8.7 physiological function Streptomyces coelicolor contains 25 biosynthetic secondary metabolite clusters that produce natural products, including actinorhodin, coelichelin, coelibactin, TW95a, EPA, methylenomycin (encoded on a giant linear plasmid), prodiginines and the antibiotic CDA. All of these natural products are produced by synthases that require phoshopantetheinylation by an AcpS-type PPTase, which shows a high level of permissiveness for CoA substrates as well as carrier proteins. For example, type I mammalian FAS, type I fungal PKS, and several type II bacterial ACPs are efficiently phosphopantetheinylated. The genome of Streptomyces coelicolor contains two other PPTases: RedU, which is a dedicated PPTase for undecylprodigiosin biosynthesis, and SCO6673 required for CDA biosynthesis. Both RedU and SCO6673 have specific carrier protein targets, whereas ScAcpS shows broad activity. The crystal structure of ScAcpS shows the structural basis for relaxed substrate selection. In Streptomyces coelicolor, which also produces prodiginine, the PPTase RedU is responsible for 4'-phosphopantetheinylation of RedO but not for the other PCP and ACP domains Streptomyces coelicolor
2.7.8.7 physiological function the biosyntheses of the red pigment prodigiosin and the surfactant serrawettin W1 in Serratia marcescens depend on the presence of the PPTase PswP. Serratia species appear to employ two PPTases, one to activate the PCP of PigG and one to activate the ACPs of PigH. Besides PswP, PigL also is a PPTase. Two Sfp/EntD-type PPTases are identified, encoded by genes SMA4147 and SMA2452 Serratia marcescens
2.7.8.7 physiological function the enzyme is essential. Two siderophores, pyoverdin and pyochelin, are produced by NRPSs and associated with the virulence of these bacteria. Pyoverdine biosynthesis requires phoshopantetheinylation of PvdD, PvdI and PvdJ and pyochelin biosynthesis requires activation of PchE and PchF. PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins, but the PPTase is optimized for primary metabolism, since its activity drops 30-fold for ACPs or PCPs from secondary metabolism in vitro Pseudomonas aeruginosa
2.7.8.7 physiological function the enzyme PptT is the PPTase for the mycobactin synthase. Siderophores in Mycobacterium tuberculosis are peptide-based and fall into two categories, the water-soluble exochelins and the membrane-associated mycobactins. siderophore or other natural product production is regulated by the activity of the PPTase. PptT is necessary for in vitro growth of mycobacteria, but mycobacteria require enzymes in vitro that are not always required in vivo. PPTases posttranslationally modify modular and iterative synthases acting in a processive fashion, namely fatty acid synthases, polyketide synthases, and non-ribosomal peptide syntethases. The central component of these chain elongating synthases is non-catalytic and either a translationally linked domain of a larger polypeptide chain or an independently translated protein. Regardless, this protein component is referred to as a carrier protein, or alternatively a thiolation domain. The CP tethers the growing intermediates on a 4'-phosphopantetheine (PPant) arm of 20 A through a reactive thioester linkage. PPants are thought of as prosthetic arms on which all substrates and intermediates of these pathways are covalently yet transiently held during the orderly progression of enzymatic modifications to the extending chain. PPTases mediate the transfer and covalent attachment of PPant arms from coenzyme A (CoA) to conserved serine residues of the carrier protein domain through phosphoester bonds. These essential posttranslation protein modifications convert inactive apo-synthases to active holo-synthases. Mechanistically distinct classes of enzymes have been identified that require PPant arms for biosynthetic catalysis. These include enzymes involved in the biosynthesis of lipid A, D-alanyllipoteichoic acid, lipo-chitin nodulation factor, beta-alanine-dopamine conjugates, carboxylic acid reductions, and dehydrogenation of alpha-aminoadipate semialdehyde (lysine biosynthesis) and 10-formyl-tetrahydrofolate. Essential enzymatic role of PPTases in general fatty acid biosynthesis. AcpSs are primarily used for post-translational modification and activation of the carrier proteins of FASs (primary metabolism) across a diversity of organisms making them the most commonly found PPTase. Mycolic acid, mycobactin, polyketide-derived lipids, fatty acids, siderophores and some yet to be discovered natural products all depend on PPTase activity for biosynthesis Mycobacterium tuberculosis
2.7.8.7 physiological function the PobA PPTase efficiently functionally complements an Escherichia coli entD mutant Burkholderia cenocepacia
2.7.8.7 physiological function the PPTase XabA is essential for albicidin production Xanthomonas albilineans
2.7.8.7 physiological function Vibrio cholerae is a bacterial pathogen that biosynthesizes a unique siderophore, vibriobactin, using biosynthetic machinery similar to enterobactin synthase. Both VibB and VibF are phosphopantetheinylated by the PPTase VibD Vibrio cholerae