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Enzyme Nomenclature
Information on EC 2.7.8.7 - holo-[acyl-carrier-protein] synthase
for references in articles please use BRENDA:EC2.7.8.7
Word Map on EC 2.7.8.7
- 2.7.8.7
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phosphopantetheinylation
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polyketide
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synthetases
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nonribosomal
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4'-phosphopantetheinylation
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peptidyl
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siderophore
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lipopeptide
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nrpss
- enterobactin
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holo-forms
- apo-acps
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biosurfactant
- alpha-aminoadipate
- analysis
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fengycin
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indigoidine
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iturins
- medicine
- synthesis
- drug development
- biotechnology
- molecular biology
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.7.8.7
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RECOMMENDED NAME
GeneOntology No.
holo-[acyl-carrier-protein] synthase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
sequential binding mechanism: initial CoA- and Mg2+-binding followed by binding of acyl-carrier protein (ACP), nucleophilic attack of ACP-serine-hydroxylate on beta-phosphate of CoA followed by charge migration, Lys185-protonation, diphosphate-cleavage, and product dissociation, rate limiting step: release of 3',5'-ADP, key acid/base catalysts: residues E181 (CoA-binding) and K185 (Mg2+-binding)
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
CoA-[4'-phosphopantetheine]:apo-[acyl-carrier protein] 4'-pantetheinephosphotransferase
Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain [3]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.
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CAS REGISTRY NUMBER
COMMENTARY
37278-30-1
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Streptomyces pneumoniae
isolated from Yunnan, China
UniProt
isolated from Yunnan, China
UniProt
strain ATCC15003, nucleotide sequence of the svp locus
SwissProt
strain ATCC15003, nucleotide sequence of the svp locus
SwissProt
Streptomyces pneumoniae
apcS gene, open reading frame starting at the second Met codon
SwissProt
strain Gv29-8, gene TRIVIDRAFT_194983; i.e. Hypocrea virens
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
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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
evolution
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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
evolution
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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 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain
evolution
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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 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain
evolution
BPSS2266 is a PPTase of the 4'-phosphopantetheinyl transferase superfamily
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; 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 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain; 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 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain; 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 4248 aa for AcpS (family I) and 3841 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
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
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
evolution
A0A0N2A6I3
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
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; 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; 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
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
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
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
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
evolution
phylogenetic analyses of plant PPT/PPT-like homologues, overview
evolution
PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively; PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively; PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively; PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively; PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively
evolution
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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 4248 aa for AcpS (family I) and 3841 aa for Sfp-type (family II) PPTases, and h is an amino acid with a hydrophobic side chain
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evolution
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BPSS2266 is a PPTase of the 4'-phosphopantetheinyl transferase superfamily
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evolution
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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
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evolution
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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
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evolution
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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
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evolution
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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
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evolution
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PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively; PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively; PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively; PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively; PPTases can be classified into three groups according to their structures. A group I PPTase, also named as an ACPS-type PPTase, consists of three identical peptide subunits with about 120 amino acid residues in each subunit. A group II PPTase, also named as a Sfp-type PPTase, consists of one peptide which is about twice the size of one group I PPTase subunit. A group III PPTase exists as a domain of a FAS or a PKS. FKPPT1, FKPPT2, FKPPT3, FKPPT4 contains three conserved motifs, PRWP, GID and FSAKESVYK, found in the Sfp-type PPTase motifs P1, P2 and P3, while FKACPS contains just last two conserved motifs found in ACPS-type PPTase. Thus, FKPPT1, FKPPT2, FKPPT3, and FKPPT4 belong to the Sfp-type PPTase group, and FKACPS belongs to the ACPS-type PPTase group, respectively
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evolution
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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
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evolution
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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
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malfunction
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enzyme silencing by small interfering RNA in A-549 cells prevents FDH modification. Enzyme-silenced cells demonstrate significantly reduced proliferation and undergo strong G1 arrest
malfunction
inactivation of the enzyme abolishes production of natamycin but not the spore pigment
malfunction
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after 18 h incubation at 37°C DELTApptB spores are swollen. Some germinate, but then arrest at this stage
malfunction
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The ppt1 deletion mutants are auxotrophic for lysine, produce nonpigmented conidia, and are unable to synthesize nonribosomal peptides. Although spore germination is severely compromised under both low and high iron availability, mycelial growth occurs faster than the wild type, and the mutants are able to efficiently colonize plant roots. The ppt1 deletion mutants are unable of inhibiting growth of phytopathogenic fungi in vitro and are defective in induction of salicylic acid-dependent defense responses in Arabidopsis thaliana
malfunction
deletion of PPT1 generates mutants that are auxotrophic for lysine, unable to synthesize melanin, hypersensitive to iron and oxidative stress (H2O2) and significantly reduced in virulence to barley cultivar Bowman
malfunction
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deletion of the ppt1 gene results in loss of polyketide synthase- and polyketide synthase/non-ribosomal peptide synthase-derived products and in transcriptional down-regulation of distinct secondary metabolite cluster genes
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
malfunction
Q9UVK7
pleiomorphic phenomena of npgA1 mutant, phenotype, overview
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; overproduction of AcpS cannot compensate the absence of EntD. Conversely, overexpressing entD on an inducible plasmid cannot complement the absence of acpS
malfunction
a conditional pptT mutant in Mycobacterium. tuberculosis H37Rv shows retarded growth and persistence. Mutant cells fail to multiply in vivo
malfunction
A0A0N2A6I3
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
malfunction
a VabD knockout strain shows no retarded growth under iron-rich conditions, but reduced growth under iron-depletion
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
malfunction
a T-DNA-tagged null mutant mtppt-1 allele shows an embryo-lethal phenotype. Arabidopsis thaliana RNAi transgenic lines with reduced mtPPT expression display typical phenotypes associated with a deficiency in the mtFAS system, namely miniaturized plant morphology, slow growth, reduced lipoylation of mitochondrial proteins, and the hyperaccumulation of photorespiratory intermediates, glycine and glycolate. the seeds in the mtppt-1 mutant plants failed to develop normally. These morphological and metabolic alterations are reversed when these plants are grown in a non-photorespiratory condition (i.e. 1% CO2 atmosphere), because they are a consequence of a deficiency in photorespiration due to the reduced lipoylation of the photorespiratory glycine decarboxylase. Phenotypes, detailed overview
malfunction
the enzyme mutant plants produce no elicitor hydrocarbon terpenes and are not protected against necrotrophic pathogen Botrytis cinerea; the enzyme mutant plants produce no elicitor hydrocarbon terpenes and are not protected against necrotrophic pathogen Botrytis cinerea
malfunction
inactivation of FKPPT1 or FKPPT3 decreases the FK506 yield in Streptomyces tsukubaensis strain L19; inactivation of FKPPT1 or FKPPT3 decreases the FK506 yield in Streptomyces tsukubaensis strain L19, and overexpression of FKPPT3 increases the FK506 production
malfunction
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after 18 h incubation at 37°C DELTApptB spores are swollen. Some germinate, but then arrest at this stage
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malfunction
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pleiomorphic phenomena of npgA1 mutant, phenotype, overview
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malfunction
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deletion of the ppt1 gene results in loss of polyketide synthase- and polyketide synthase/non-ribosomal peptide synthase-derived products and in transcriptional down-regulation of distinct secondary metabolite cluster genes
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malfunction
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a conditional pptT mutant in Mycobacterium. tuberculosis H37Rv shows retarded growth and persistence. Mutant cells fail to multiply in vivo
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malfunction
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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
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malfunction
-
inactivation of the enzyme abolishes production of natamycin but not the spore pigment
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malfunction
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inactivation of FKPPT1 or FKPPT3 decreases the FK506 yield in Streptomyces tsukubaensis strain L19; inactivation of FKPPT1 or FKPPT3 decreases the FK506 yield in Streptomyces tsukubaensis strain L19, and overexpression of FKPPT3 increases the FK506 production
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malfunction
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a VabD knockout strain shows no retarded growth under iron-rich conditions, but reduced growth under iron-depletion
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malfunction
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a xabA knockout strain does not produce albicidin, but when EntD is engineered into the mutant strain, production is restored to wild-type levels
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metabolism
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AcpS is a doubly promiscuous enzyme capable of activation of acyl-carrier proteins from both fatty acid and polyketide synthesis and catalyzes the transfer of modified CoA substrates
metabolism
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the enzyme is essential for activation of non-ribosomal peptide synthetase and polyketide synthase enzymes
metabolism
isoform AcpS specifically modifies a stand-alone acyl carrier protein that possesses a mitochondrial import signal; isoform Sfp in contrast is specific to type I multifunctional polyketide synthase/fatty acid synthase proteins and cannot modify the stand-alone acyl carrier protein
metabolism
-
isoform Ppt1 is essentially involved in lysine biosynthesis and production of bikaverins, fusarubins and fusarins, but not moniliformin
metabolism
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isoform PptT plays a role in the biosynthesis pathways for mycolic acids, polyketide-derived lipids and siderophores
metabolism
the demonstration that ACP homologue IacP is matured by AcpS establishes a cross-connection between virulence and fatty acid biosynthesis pathways
metabolism
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isoform AcpS specifically modifies a stand-alone acyl carrier protein that possesses a mitochondrial import signal; isoform Sfp in contrast is specific to type I multifunctional polyketide synthase/fatty acid synthase proteins and cannot modify the stand-alone acyl carrier protein
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metabolism
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isoform Ppt1 is essentially involved in lysine biosynthesis and production of bikaverins, fusarubins and fusarins, but not moniliformin
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metabolism
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isoform PptT plays a role in the biosynthesis pathways for mycolic acids, polyketide-derived lipids and siderophores
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physiological function
overexpression of the enzyme not only increases the natamycin production by about 40% but also accelerates productions of both natamycin and the spore pigment
physiological function
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isoform PPT1 in plays an important role antibiosis and induction of salicylic acid and camalexin-dependent plant defense responses
physiological function
Sfp-type 4-phosphopantetheinyl transferase is required for lysine synthesis, tolerance to oxidative stress and virulence of Cochliobolus sativus on barley cultivar Bowman. Isoform PPT1 is involved in conidiation, but does not affect the size, morphology and germination of conidia
physiological function
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isoform Ppt1 is involved in conidiation and sexual mating recognition. Isoform Ppt1 contributes to a functional iron uptake system that is controlled by the GATA-type transcription factor Sre1. Isoform Ppt1 is a pathogenicity factor in hydroponic rice cultures
physiological function
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the enzyme is required for Mycobacterium tuberculosis growth and persistence in vivo. The enzyme is involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors in mycobacteria. The enzyme is required for the replication and survival of the tubercle bacillus during the acute and chronic phases of infection in mice
physiological function
4'-phosphopantetheinyl transferase post-translationally modifies carrier proteins with a phosphopantetheine moiety, an essential reaction. In Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors
physiological function
4'-phosphopantetheinyl transferase post-translationally modifies carrier proteins with a phosphopantetheine moiety, an essential reaction. In Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors
physiological function
-
phosphopantetheinyl transferases play an essential role in the biosyntheses of fatty acids, polyketides, and nonribosomal peptides
physiological function
-
phosphopantetheinyl transferase activates biosynthetic pathways that synthesize both primary and secondary metabolites in bacteria
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
physiological function
Q9UVK7
the enzyme is essential for growth, and for formation of conidia and cleistothecium in development
physiological function
-
the enzyme is essential for the viability of the bacterium
physiological function
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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
physiological function
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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
physiological function
the PobA PPTase efficiently functionally complements an Escherichia coli entD mutant
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; 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; 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; 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
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
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
physiological function
A0A0N2A6I3
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
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 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 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
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
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
physiological function
the PPTase XabA is essential for albicidin production
physiological function
the mitochondrial enzyme catalyzes the phosphopantetheinylation and thus activation of mitochondrial acyl carrier protein (mtACP) of mitochondrial fatty acid synthase (mtFAS). A crucial role of mtPPT for embryogenesis. MtPPT contributes to mtFAS and photorespiration
physiological function
Trichoderma virens volatile organic compounds elicit both development and defense programs and enzyme PPT1 plays an important role in biosynthesis of terpenes (including the sesquiterpenes beta-caryophyllene, (-)-beta-elemene, germacrene D, Tau-cadinene, delta-cadinene, alpha-amorphene, and Tau-selinene and the monoterpenes beta-myrcene, trans-beta-ocimene, and cis-beta-ocimene) and plant protection against Botrytis cinerea, overview; Trichoderma virens volatile organic compounds elicit both development and defense programs and enzyme PPT1 plays an important role in biosynthesis of terpenes (including the sesquiterpenes beta-caryophyllene, (-)-beta-elemene, germacrene D, Tau-cadinene, delta-cadinene, alpha-amorphene, and Tau-selinene and the monoterpenes beta-myrcene, trans-beta-ocimene, and cis-beta-ocimene) and plant protection against Botrytis cinerea, overview
physiological function
The 4'-phosphopantetheine (4'PPT) portion of coenzyme A (CoA) is an essential group for many carrier proteins and enzymes. Addition of this group is required for the correct function of polyketide synthase (PKS), non-ribosomal peptide synthetase and fatty acid synthase. The 4'PPT group is transferred to a highly conserved serine motif in the acceptor protein in a magnesium dependent reaction by phosphopantetheinyl transferases (PPTases). Gene PPT2 encoding a phosphopantetheinyl transferase and is essential for growth in Candida albicans
physiological function
phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations; phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations; phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations; phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations; phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations
physiological function
-
the enzyme is essential for growth, and for formation of conidia and cleistothecium in development
-
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
-
physiological function
-
isoform Ppt1 is involved in conidiation and sexual mating recognition. Isoform Ppt1 contributes to a functional iron uptake system that is controlled by the GATA-type transcription factor Sre1. Isoform Ppt1 is a pathogenicity factor in hydroponic rice cultures
-
physiological function
-
the enzyme is essential for the viability of the bacterium
-
physiological function
-
the enzyme is required for Mycobacterium tuberculosis growth and persistence in vivo. The enzyme is involved in post-translational modification of various type-I polyketide synthases required for the formation of both mycolic acids and lipid virulence factors in mycobacteria. The enzyme is required for the replication and survival of the tubercle bacillus during the acute and chronic phases of infection in mice
-
physiological function
-
4'-phosphopantetheinyl transferase post-translationally modifies carrier proteins with a phosphopantetheine moiety, an essential reaction. In Mycobacteria, the Sfp-type PPTase activates pathways necessary for the biosynthesis of cell wall components and small molecule virulence factors; 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
-
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
-
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
-
physiological function
-
overexpression of the enzyme not only increases the natamycin production by about 40% but also accelerates productions of both natamycin and the spore pigment; phosphopantetheinyl transferases play an essential role in the biosyntheses of fatty acids, polyketides, and nonribosomal peptides
-
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
-
physiological function
-
phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations; phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations; phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations; phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations; phosphopantetheinyl transferases (PPTases) catalyze the phosphopantetheinylation of acyl carrier proteins (ACPs) in polyketide synthases (PKSs), peptidyl carrier proteins (PCPs) in nonribosomal peptide synthetases (NRPSs), and ACPs in fatty acid synthases (FASs) from inactive apo-forms into active holo-form. PPTases are essential to both primary metabolisms and secondary metabolisms. Phosphopantetheinylation of the ACP/PCP is involved in FK506 biosynthesis, FK506 (tacrolimus) is a clinical immunosuppressant widely used after allogeneic kidney, liver, and heart transplantations
-
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
-
physiological function
-
the PPTase XabA is essential for albicidin production
-
additional information
analysis and comparisons of cofactor binding and active site composition, CoA binding pocket, catalytic mechanism of PptT, overview. While important for CoA binding, Arg48 and Arg56 likely play very small roles in catalysis
additional information
analysis and comparisons of cofactor binding and active site composition, CoA binding pocket, overview
additional information
Q9UVK7
loss-of-function of LYS5 mutant DNPG, which encodes a PPTase in Saccharomyces cerevisiae strain BY4741, is functionally complemented by NpgA, and Escherichia coli-derived NpgA reveals phosphopantetheinylation activity with the elaboration of 3'5'-ADP
additional information
-
improved solubility of the full-length PptT compared to its N- and C-terminally truncated counterparts
additional information
-
the human pathogen Mycobacterium tuberculosis encodes two PPTases, a type-I PPTase and a type-II PPTase, that are both essential. Type-II PPTase PptT shows a bound CoA that is clearly defined with its pantetheinyl arm tucked into a hydrophobic pocket. Interactions involving the CoA diphosphate, bound Mg2+ and three active site acidic side chains suggest a plausible pathway for proton transfer during catalysis. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry. It is octahedrally coordinated to the alpha- and beta-phosphates, Asp114, Glu116, the peptide oxygen of Ala115 and a water molecule
additional information
-
loss-of-function of LYS5 mutant DNPG, which encodes a PPTase in Saccharomyces cerevisiae strain BY4741, is functionally complemented by NpgA, and Escherichia coli-derived NpgA reveals phosphopantetheinylation activity with the elaboration of 3'5'-ADP
-
additional information
-
improved solubility of the full-length PptT compared to its N- and C-terminally truncated counterparts; the human pathogen Mycobacterium tuberculosis encodes two PPTases, a type-I PPTase and a type-II PPTase, that are both essential. Type-II PPTase PptT shows a bound CoA that is clearly defined with its pantetheinyl arm tucked into a hydrophobic pocket. Interactions involving the CoA diphosphate, bound Mg2+ and three active site acidic side chains suggest a plausible pathway for proton transfer during catalysis. Three-dimensional structure of Mtb-PptT, modeling, overview. Mtb-PptT comprises two alpha/beta domains with pseudo 2fold symmetry. It is octahedrally coordinated to the alpha- and beta-phosphates, Asp114, Glu116, the peptide oxygen of Ala115 and a water molecule
-
additional information
-
analysis and comparisons of cofactor binding and active site composition, CoA binding pocket, catalytic mechanism of PptT, overview. While important for CoA binding, Arg48 and Arg56 likely play very small roles in catalysis
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
apo-[acyl-carrier protein] + acetyl-CoA
CoA + acetyl-[acyl-carrier protein]
pH 7, 37°C
reaction stop by 10% trichloroacetic acid, limited release of 3,5-ADP by interactions with guanidinium moieties of R74 and R86
-
?
benzoyl-CoA + apo-[acyl-carrier protein]
CoA + benzoyl-[acyl-carrier protein]
-
-
-
-
r
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
-
-
-
-
r
CoA + apo-[fredericamycin H acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[fredericamycin acyl-carrier protein]
-
-
-
?
CoA + apo-[Lys2-PCP-H6 Saccharomyces cerevisiae]
? + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
CoA + apo-[peptidyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
-
?
CoA + apo-[Streptomyces sp. frenolicin-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. frenolicin-acyl-carrier protein]
-
-
-
-
r
CoA + apo-[Streptomyces sp. granaticin-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. granaticin-acyl-carrier protein]
-
-
-
-
r
CoA + apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
-
-
-
-
r
CoA + apo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
adenosine 3',5'-bisphosphate + holo-[Streptomyces sp. tetracenomycin-acyl-carrier protein(His6)]
-
-
-
-
r
CoA + apo-[tetracenomycin M acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[tetracenomycin M acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
CoA-[4'-phosphopantetheine] + apo-[FDH protein]
adenosine 3',5'-bisphosphate + holo-[FDH protein]
-
the enzyme modifies the apo-FDH protein at serine 354 and activates its catalysis
-
-
?
desulfoCoA + apo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
? + holo-[Streptomyces sp. oxytetracycline-acyl-carrier protein]
-
-
-
-
r
myristoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
palmitoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
phenylacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
acetoacetyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
acetonyldethio-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
acetyl-CoA + acyl-carrier protein
CoA + acetyl-[acyl-carrier protein]
substrate for isoform AcpS
-
-
?
acetyl-CoA + acyl-carrier protein
CoA + acetyl-[acyl-carrier protein]
substrate for isoform AcpS
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
-
r
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
recombinant enzyme
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
-
-
-
-
?
acetyl-CoA + apo-[acyl-carrier protein]
CoA + acetyl-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
acetyl-CoA + polyketide synthase 1
CoA + acetyl-polyketide synthase 1
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 1
CoA + acetyl-polyketide synthase 1
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 16
CoA + acetyl-polyketide synthase 16
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 16
CoA + acetyl-polyketide synthase 16
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 2
CoA + acetyl-polyketide synthase 2
substrate for isoform Sfp
-
-
?
acetyl-CoA + polyketide synthase 2
CoA + acetyl-polyketide synthase 2
substrate for isoform Sfp
-
-
?
biotin-CoA + DSLEFIASKLA
D-(biotinyl-4'-phosphopantetheinyl)SLEFIASKLA + ?
-
-
-
-
?
biotin-CoA + DSLEFIASKLA
D-(biotinyl-4'-phosphopantetheinyl)SLEFIASKLA + ?
-
-
-
-
?
biotin-CoA + GDSLDMLEWSLM
GD-(biotinyl-4'-phosphopantetheinyl)SLDMLEWSLM + ?
-
-
-
-
?
biotin-CoA + GDSLDMLEWSLM
GD-(biotinyl-4'-phosphopantetheinyl)SLDMLEWSLM + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRCLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRCLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRLLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLLRLLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLLRSLN
GD-(biotinyl-4'-[N-{2-[2-(2-aminoethoxy)ethoxy]ethyl}-3-(2,5-dioxopyrrolidin-1-yl)propanamide]phosphopantetheinyl)SLSWLLRSLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLVRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRCLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLVRCLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRCLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLVRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRLLN + ?
-
-
-
-
?
biotin-CoA + GDSLSWLVRLLN
GD-(biotinyl-4'-phosphopantetheinyl)SLSWLVRLLN + ?
-
-
-
-
?
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
?
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
butyryl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme Sfp required for production of the lipoheptapeptide antibiotic surfactin
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
recombinant enzyme
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
transfers 4'-phosphopantetheine from reduced coenzyme A to acyl carrier proteon apoprotein
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
Dcp from Lactobacillus casei, NodF from Rhizobium leguminosarum and several polyketide synthase ACPs from Streptomyces sp. also serves as substrates
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
Streptomycess sp. acyl carrier proteins and coenzyme A analogs also serves as substrates for holo-ACP synthase in vitro
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
transfers 4'-phosphopantetheine from reduced coenzyme A to acyl carrier proteon apoprotein
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PcpS plays an essential role in both fatty acid and siderophore metabolism
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
posttranslational conversion of the alpha-aminoadipate semialdehyde reductase Lys2 in lysine biosynthesis
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
plays a role in polyketide biosynthesis
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
plays a role in polyketide biosynthesis
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
r
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
-
phosphopantetheinylation of the enzyme in volved in lysine catabolism
-
-
r
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
-
phosphopantetheinylation of the enzyme involved in lysine catabolism
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
r
CoA + apo-[peptidyl carrier protein]
adenosine 3',5'-bisphosphate + holo-[peptidyl-carrier protein]
-
-
-
r
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein AcpA]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein AcpA]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
assay with wild-type and mutant ACP substrates from Leishmania major (LmACP), mutants N35D, F44M, and F44A, the double mutants N35D/F44M and N35D/Q48E, triple mutant N35D/F44M/Q48E of LmACP, and with Escherichia coli ACP, the M44F mutant of Escherichia coli ACP, Plasmmodium falciparum ACP, and Mycobacterium tuberculosis ACP. No activity with LmACP F44A mutant
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
assay with wild-type and mutant ACP substrates from Leishmania major (LmACP), mutants N35D, F44M, and F44A, the double mutants N35D/F44M and N35D/Q48E, triple mutant N35D/F44M/Q48E of LmACP, and with Escherichia coli ACP, the M44F mutant of Escherichia coli ACP, Plasmmodium falciparum ACP, and Mycobacterium tuberculosis ACP. No activity with LmACP F44A mutant
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
?
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the mitochondrial enzyme catalyzes the phosphopantetheinylation and thus activation of mitochondrial acyl carrier protein (mtACP) of mitochondrial fatty acid synthase (mtFAS)
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
PPTase cleaves coenzyme A, transfers the P-pant moiety to a conserved residue of inactive substrates, and produces 3'5'-ADP
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
PPTase cleaves coenzyme A, transfers the P-pant moiety to a conserved residue of inactive substrates, and produces 3'5'-ADP
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
Bli is the PPTase that phosphopantetheinylates the PCP domain of this elongating synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
the enzyme activates bacitracin and in vitro also tyrocidin synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
the enzyme Sfp is active with surfactin synthase peptidyl carrier protein
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
the enzyme Sfp is active with surfactin synthase peptidyl carrier protein
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
catalytic activity of Ppt2 as a phosphopantetheinyl transferase and the acyl carrier protein Acp1 as a substrate, Acp12 is no substrate. The terminal thiol group of the 4'PPT is the site at which elongation occurs via thioester linkages and attachments are covalently linked
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the carrier protein of Colibactin is phosphopantetheinylated by the family II PPTase ClbA
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
assay with ACP substrates from Leishmania major (LmACP), Escherichia coli, Plasmodium falciparum, Mycobacterium tuberculosis, and Homo sapiens. The structure of the holo-acyl carrier protein of Leishmania major is similar to other type II ACPs, comprising a four-helix bundle, enclosing a hydrophobic core, but it displays a remarkably different phosphopantetheinyl transferase binding interface. Two- and three-dimensional NMR structure analysis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates mycobatin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
with the most soluble and compact ACP fragment (2042-2188) of ACP substrate from the type I polyketide synthase PpsC from Mycobacterium tuberculosis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
with the most soluble and compact ACP fragment (2042-2188) of ACP substrate from the type I polyketide synthase PpsC from Mycobacterium tuberculosis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates mycobatin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
broad specificity of the single PPTase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
broad specificity of the single PPTase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
A0A0N2A6I3
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
A0A0N2A6I3
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PPTases transfer 4'-phosphopantetheine from coenzyme A (CoA) to highly conserved serine residues in PCPs/ACPs, converting PCPs/ACPs from inactive apo-forms into active holo-forms
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
usage of ACP substrate kbB-ACP4, an ACP in FK506 biosynthetic PKS/NRPS hybrid from Streptomyces tsukubaensis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PPTases transfer 4'-phosphopantetheine from coenzyme A (CoA) to highly conserved serine residues in PCPs/ACPs, converting PCPs/ACPs from inactive apo-forms into active holo-forms
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
usage of ACP substrate kbB-ACP4, an ACP in FK506 biosynthetic PKS/NRPS hybrid from Streptomyces tsukubaensis
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
phosphopantetheinylation of VabF
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
phosphopantetheinylation of VabF
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
both VibB and VibF are phosphopantetheinylated by the PPTase VibD
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates the antibiotic albicidin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates the antibiotic albicidin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
the enzyme activates yersiniabactin
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
Bacillus subtilis ATCC 6633
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[BpsA protein]
adenosine 3',5'-bisphosphate + holo-[BpsA protein]
-
-
-
-
?
crotonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
crotonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
decanoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
decanoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
desulfo-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
homocysteamine-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
r
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
?
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
malonyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
-
-
r
myristoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
myristoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
palmitoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
palmitoleoyl-CoA + apo-[acyl-carrier protein]
? + holo-[acyl-carrier protein]
-
-
-
-
?
additional information
?
-
analysis of enzyme activities with three recombinant apo-mtACP isoforms, i.e. mtACP1 (AT2G44620), mtACP2 (AT1G65290) and mtACP3 (AT5G47630), overview
-
-
-
additional information
?
-
analysis of enzyme activities with three recombinant apo-mtACP isoforms, i.e. mtACP1 (AT2G44620), mtACP2 (AT1G65290) and mtACP3 (AT5G47630), overview
-
-
-
additional information
?
-
-
isoform PptB is unable to phosphopantetheinylate AarA protein
-
-
-
additional information
?
-
-
isoform PptB is unable to phosphopantetheinylate AarA protein
-
-
-
additional information
?
-
-
Sfp type exhibits an extraordinarily broad substrate specificity
-
-
-
additional information
?
-
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
-
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
-
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
-
additional information
?
-
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
-
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
-
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
-
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
-
additional information
?
-
isoform Sfp exhibits weak activity with acetyl-CoA
-
-
-
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
-
additional information
?
-
isoform AcpS shows weak activity with mycobacterial polyketide synthase 2
-
-
-
additional information
?
-
-
mutant ACP in which the target serine 36 has been mutated to a threonine residue is an inactive substrate for phosphopantetheinylation
-
-
-
additional information
?
-
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
-
additional information
?
-
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
-
additional information
?
-
-
isoform AcpT modifies two carrier proteins encoded in O-island 138, a cluster of fatty acid biosynthesis-like genes
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
Escherichia coli B / ATCC 11303
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
-
additional information
?
-
-
single broad specificity enzyme for all posttranslational 4'-phosphopantetheinylation reactions, also capable of phosphopantetheinylation of peptidyl carrier and acyl carrier proteins from prokaryotes
-
-
-
additional information
?
-
-
development of a direct and continuous assay for this enzyme class based upon monitoring polarization of a fluorescent phosphopantetheine analogue as it is transferred from a low molecular weight coenzyme A substrate to higher molecular weight protein acceptor, utility of the method for the biochemical characterization of phosphopantetheinyl transferase Sfp, a canonical enzyme, recombinant enzyme with substrates VibB and 90 amino acid ACP (hACP) from human fatty acid synthase, overview
-
-
-
additional information
?
-
-
recombinant expression of ACP substrates from Leishmania major (LmACP), Escherichia coli, Plasmodium falciparum, Mycobacterium tuberculosis, and Homo sapiens in Escherichia coli and purification by ion exchange chromatography. LmACP does not interact with the bacterial group I, 4'-phosphopantetheinyl transferase. Residues Asn 35 and Phe 44, present in LmACP modulate its interaction with AcpS
-
-
-
additional information
?
-
recombinant expression of ACP substrates from Leishmania major (LmACP), Escherichia coli, Plasmodium falciparum, Mycobacterium tuberculosis, and Homo sapiens in Escherichia coli and purification by ion exchange chromatography. LmACP does not interact with the bacterial group I, 4'-phosphopantetheinyl transferase. Residues Asn 35 and Phe 44, present in LmACP modulate its interaction with AcpS
-
-
-
additional information
?
-
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
-
additional information
?
-
-
enzyme is required for production of n-3 polyunsaturated fatty acids
-
-
-
additional information
?
-
-
SePptII is active in phosphopantetheinyl transfer with an acyl carrier protein-thioesterase didomain from the erythromycin polyketide synthase as substrate. SePptII provides complete modification of acyl-carrier protein-thioesterase and of an entire multienzymne subunit from the erythromycin polyketide synthase
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
specificity of the holo-ACP synthetase is not examined in detail, only CoA is the donor of the 4'-phosphopantetheine moiety, dephospho-CoA is essentially inactive
-
-
-
additional information
?
-
activates polyketide synthases and polypetide synthases, processes an aryl carrier protein domain ArCP, derived from the enterobactin synthetase of Escherichia coli, as well as a peptidyl carrier protein domain from a polypeptide synthase of yet unknown function from Sorangium cellulosum
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
-
additional information
?
-
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
-
additional information
?
-
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
-
additional information
?
-
-
substrate promiscuity of the phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins, SchPPT has a broad substrate specificity for ACPs
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in both type I polyketide synthases and type II polyketide synthases
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
-
additional information
?
-
the enzyme catalyzes the phosphopantetheinylation of acyl carrier proteins in type II polyketide synthases and fatty acid synthases
-
-
-
additional information
?
-
-
substrate promiscuity of the phosphopantetheinyl transferase SchPPT for coenzyme A derivatives and acyl carrier proteins, SchPPT has a broad substrate specificity for ACPs
-
-
-
additional information
?
-
enzyme is involved in fredericamycin biosynthesis
-
-
-
additional information
?
-
-
enzyme is involved in fredericamycin biosynthesis
-
-
-
additional information
?
-
Streptomyces pneumoniae
dephospho-CoA is no substrate
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
substrate specificities of isozymes with different ACPs: stw ACP, an ACP in a type II PKS, is phosphopantetheinylated by three PPTases FKPPT1, FKPPT3, and FKACPS. sts FAS ACP, the ACP in fatty acid synthase (FAS), is phosphopantetheinylated by three PPTases FKPPT2, FKPPT3, and FKACPS. TcsA-ACP, an ACP involved in FK506 biosynthesis, is phosphopantetheinylated by two PPTases FKPPT3 and FKACPS. FkbPPCP, an PCP involved in FK506 biosynthesis, is phosphopantetheinylated by all of these five PPTases FKPPT1-4 and FKACPS
-
-
-
additional information
?
-
posttranslational modification of carrier proteins, capable of modifying both type I and type II acyl carrier proteins and peptidyl carrier proteins, even form other Streptomyces sp.
-
-
-
additional information
?
-
-
posttranslational modification of carrier proteins, capable of modifying both type I and type II acyl carrier proteins and peptidyl carrier proteins, even form other Streptomyces sp.
-
-
-
additional information
?
-
posttranslational modification of carrier proteins, capable of modifying both type I and type II acyl carrier proteins and peptidyl carrier proteins, even form other Streptomyces sp.
-
-
-
additional information
?
-
Escherichia coli ACP and mutant ACP proteins rACP, V12G, F50A, I54L, I154V, A59G and Y71A are substrates, mutant I54A is no substrate
-
-
-
additional information
?
-
-
D35 in site A of acyl carrier protein is critical for enzyme activity
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA + apo-[alpha-aminoadipate semialdehyde dehydrogenase]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde dehydrogenase]
-
phosphopantetheinylation of the enzyme involved in lysine catabolism
-
-
r
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
-
-
-
-
r
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme Sfp required for production of the lipoheptapeptide antibiotic surfactin
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
ACP serves as cofactor in the biosynthesis of fatty acids and the biosynthesis of complex lipids
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Escherichia coli B / ATCC 11303
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PcpS plays an essential role in both fatty acid and siderophore metabolism
-
-
?
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q12036
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
posttranslational conversion of the alpha-aminoadipate semialdehyde reductase Lys2 in lysine biosynthesis
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9RFL1
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
plays a role in polyketide biosynthesis
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
functional activation of ACP in the fatty acid biosynthesis pathway
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
enzyme subunit required for both fatty acid and polyketide biosynthesis thought to be a single malonyltransferase
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
plays a role in polyketide biosynthesis
-
-
-
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
-
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Streptomyces pneumoniae
P0A2W7
transfer of acyl fatty acid intermediates during biosynthesis of fatty acids and lipids in the cell
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9F0Q6
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9F0Q6
-
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
P0A2W3
-
-
r
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
F4IRA7, Q8VYK1
the mitochondrial enzyme catalyzes the phosphopantetheinylation and thus activation of mitochondrial acyl carrier protein (mtACP) of mitochondrial fatty acid synthase (mtFAS)
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9UVK7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
Bli is the PPTase that phosphopantetheinylates the PCP domain of this elongating synthase
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
P39135
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
P39135
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q27IP6
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q63I03
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q63I03
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q5APF3
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
E2QFX9, P19925, Q0P7J0
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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
E2QFX9, P19925, Q0P7J0
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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9NRN7
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q4QCW3
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
O33336
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
P9WQD3
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
P9WQD3
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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
O33336
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
P9WQD3
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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
P9WQD3
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
A0PU93
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9I4H2
enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9I4H2
enzyme PaPcpS acts on FAS, PKS and NRPS acyl carrier proteins
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
P63466
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
A0A0N2A6I3
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
A0A0N2A6I3
-
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PPTases transfer 4'-phosphopantetheine from coenzyme A (CoA) to highly conserved serine residues in PCPs/ACPs, converting PCPs/ACPs from inactive apo-forms into active holo-forms
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
-
PPTases transfer 4'-phosphopantetheine from coenzyme A (CoA) to highly conserved serine residues in PCPs/ACPs, converting PCPs/ACPs from inactive apo-forms into active holo-forms
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
O86785, O88029
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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
O86785, O88029
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
-
-
?
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
O86785
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
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
A0A0X8EK72, A0A0Y0S258, A0A0Y0SAB4, A0A109R3N8, I2N4F3
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
A0A0X8EK72, A0A0Y0S258, A0A0Y0SAB4, A0A109R3N8, I2N4F3
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q5DK20
phosphopantetheinylation of VabF
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q5DK20
phosphopantetheinylation of VabF
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q9RCF2
both VibB and VibF are phosphopantetheinylated by the PPTase VibD
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
D2U8G6
the enzyme activates the antibiotic albicidin
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
D2U8G6
the enzyme activates the antibiotic albicidin
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CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
Q74V64
the enzyme activates yersiniabactin
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additional information
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isoform AcpT modifies two carrier proteins encoded in O-island 138, a cluster of fatty acid biosynthesis-like genes
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enzyme is required for production of n-3 polyunsaturated fatty acids
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enzyme is required for production of n-3 polyunsaturated fatty acids
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P63466
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
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additional information
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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
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Q2MGB1
enzyme is involved in fredericamycin biosynthesis
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enzyme is involved in fredericamycin biosynthesis
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
additional information
Mg2+
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dependent on, binding structure, overview. The edge strands beta4 and beta6 of the two beta-sheets provide the binding site for the CoA diphosphate and associated Mg2+ ion. The active site in Mtb-PptT is formed in the shallow cleft between the two domains, where CoA and Mg2+ are bound
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CuSO4, CdCl2 and CrCl2 does not stimulate the reaction at any ceoncentration, trivalent metal cations such as FeCl3 or AlCl3 are ineffective
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Ca2+, Fe2+, Co2+ and Zn2+ are ineffective, inhibitory or both, at intermediate and high concentrations
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Mg2+ results in the highest activity among the divalent ions tested followed by Mn2+, while Ca2+ has no effect on the activity of the enzyme
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE