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Information on EC 2.7.8.7 - holo-[acyl-carrier-protein] synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q12036

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EC Tree
IUBMB Comments
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 . The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty-acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes . 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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Saccharomyces cerevisiae
UNIPROT: Q12036
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pptase, phosphopantetheinyl transferase, surfactin synthetase, 4'-phosphopantetheinyl transferase, mtppt, type ii fatty acid synthase system, sfp-type pptase, schppt, holo-acyl carrier protein synthase, mtacps, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
cytoplasmic type I FAS multienzyme
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mitochondrial type II fatty acid synthase
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4'-phosphopantetheinyl transferase
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acyl carrier protein holoprotein (holo-ACP) synthetase
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acyl carrier protein synthetase
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coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine transferase
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holo-ACP synthase
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-
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holo-ACP synthetase
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holosynthase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
substituted phospho group transfer
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-
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PATHWAY SOURCE
PATHWAYS
-
-, -, -, -
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 system (EC 2.3.1.85) 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.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-30-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
show the reaction diagram
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-
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r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
-
-
r
CoA + apo-[acyl-carrier protein]
adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
show the reaction diagram
CoA + apo-[alpha-aminoadipate semialdehyde reductase Lys2]
adenosine 3',5'-bisphosphate + holo-[alpha-aminoadipate semialdehyde reductase Lys2]
show the reaction diagram
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-
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4'-phosphopantetheine
prosthetic group
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
yeast
Uniprot
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
isoenzyme, mutational loss of mitochondrial ACP has no effect on bulk cellular fatty acid synthesis
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20320
mitochondrial isoenzyme, calculated from open reading frame
21000
mitochondrial isoenzyme, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified as fatty acid synthetase complex
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
open reading frame YPL148C is the potential mitochondrial PPTase gene, expressed in Escherichia coli and Saccharomyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Prescott, D.J.; Vagelos, P.R.
Acyl carrier protein
Adv. Enzymol. Relat. Areas Mol. Biol.
36
269-311
1972
Saccharomyces cerevisiae, Clostridium kluyveri, Escherichia coli, Rattus norvegicus
Manually annotated by BRENDA team
Werkmeister, K.; Wieland, F.; Schweizer, E.
Coenzyme A: fatty acid synthetase apoenzyme 4-phosphopantetheine transferase in yeast
Biochem. Biophys. Res. Commun.
96
483-490
1980
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Stuible, H.P.; Meier, S.; Wagner, C.; Hannappel, E.; Schweizer, E.
A novel phosphopantetheine:protein transferase activating yeast mitochondrial acyl carrier protein
J. Biol. Chem.
273
22334-22339
1998
Saccharomyces cerevisiae (Q12036), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mootz, H.D.; Schoergendorfer, K.; Marahiel, M.A.
Functional characterization of 4'-phosphopantetheinyl transferase genes of bacterial and fungal origin by complementation of Saccharomyces cerevisiae lys5
FEMS Microbiol. Lett.
213
51-57
2002
Aspergillus nidulans, Aspergillus nidulans FGSC4, Bacillus subtilis, Brevibacillus brevis, no activity in Saccharomyces cerevisiae, Saccharomyces cerevisiae, Schizosaccharomyces pombe, Schizosaccharomyces pombe ATCC 24843
Manually annotated by BRENDA team