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Information on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase and Organism(s) Sus scrofa and UniProt Accession Q8MIR4

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IUBMB Comments
The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.
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This record set is specific for:
Sus scrofa
UNIPROT: Q8MIR4
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The taxonomic range for the selected organisms is: Sus scrofa
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphopantetheine adenylyltransferase, 4'-phosphopantetheine adenylyltransferase, pantetheine phosphate adenylyltransferase, enterococcus faecalis ppat, pantetheine-phosphate adenylyltransferase, dephospho-coa pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3'-dephospho-CoA pyrophosphorylase
-
-
-
-
dephospho-CoA pyrophosphorylase
-
-
-
-
dephospho-coenzyme A pyrophosphorylase
-
-
-
-
pantetheine phosphate adenylyltransferase
-
-
-
-
PPAT
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:pantetheine-4'-phosphate adenylyltransferase
The enzyme from several bacteria (e.g. Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157, glucosamine-1-phosphate N-acetyltransferase.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-99-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
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
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
requirement, 2 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
PTX040334
-
no inhibition
PTX042695
-
no inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
-
activation, in vitro
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0147
3'-dephospho-CoA
25°C, pH 8
0.272
diphosphate
25°C, pH 8
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.61
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
assay at
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.75
-
chromatofocusing technique with a PBE 94 column and Polybuffer 74
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
COASY_PIG
562
0
61749
Swiss-Prot
Secretory Pathway (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
62000
gel filtration
115000
-
gel filtration
118000
-
gel filtration
57000
-
alpha2, 2 * 57000, SDS-PAGE
61000
-
alpha2, 2 * 61000, SDS-PAGE, subunit structure
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 62000, gel filtration
dimer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 0.5 mg protein/ml, at least 1 month
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to homogenity
partial
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hoagland, M.B.; Novelli, G.D.
Biosynthesis of coenzyme A from phosphopantetheine from pantothenate
J. Biol. Chem.
207
767-773
1954
Columba sp., Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Novelli, G.D.
Enzymatic synthesis and structure of CoA
Fed. Proc.
12
675-681
1953
Columba sp., Sus scrofa
Manually annotated by BRENDA team
Worrall, D.M.; Tubbs, P.K.
A bifunctional enzyme complex in coenzyme A biosynthesis: purification of pantetheine phosphate adenylyltransferase and dephospho-CoA kinase
Biochem. J.
215
153-157
1983
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Worrall, D.M.; Lambert, S.F.; Tubbs, P.K.
Limited proteolysis of pig liver CoA synthase: evidence for subunit identity
FEBS Lett.
187
277-279
1985
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Zhao, L.; Allanson, N.M.; Thomson, S.P.; Maclean, J.K.F.; Barker, J.J.; Primrose, W.U.; Tyler, P.D.; Lewendon, A.
Inhibitors of phosphopantetheine adenylyltransferase
Eur. J. Med. Chem.
38
345-349
2003
Escherichia coli, Sus scrofa
Manually annotated by BRENDA team
Aghajanian, S.; Worrall, D.M.
Identification and characterization of the gene encoding the human phosphopantetheine adenylyltransferase and dephospho-CoA kinase bifunctional enzyme (CoA synthase)
Biochem. J.
365
13-18
2002
Homo sapiens (Q13057), Homo sapiens, Sus scrofa (Q8MIR4), Sus scrofa
Manually annotated by BRENDA team