Information on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase

New: Word Map on EC 2.7.7.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
2.7.7.3
-
RECOMMENDED NAME
GeneOntology No.
pantetheine-phosphate adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adenosyl group transfer
-
-
nucleotidyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme A biosynthesis I
-
-
coenzyme A biosynthesis II (mammalian)
-
-
coenzyme A metabolism
-
-
Metabolic pathways
-
-
Pantothenate and CoA biosynthesis
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Rv2965c
-
-
Manually annotated by BRENDA team
no activity in Plasmodium lophurae
avian malaria parasite
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain HB8
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2'-deoxy-ATP + pantetheine 4'-phosphate
?
show the reaction diagram
-
phosphorylation at 27% the rate of ATP
-
-
?
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
show the reaction diagram
4'-phosphopantetheine + Mg2+-ATP
3'-dephospho-CoA + diphosphate
show the reaction diagram
-
PPAT does not accept 4'-phosphopantothenoyl-Cys as a substrate
-
-
r
ATP + 4'-phosphopantetheine
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
diphosphate + 3'-dephospho-CoA
ATP + pantetheine 4'-phosphate
show the reaction diagram
phosphopantetheine + Mg-ATP
dephospho-CoA + diphosphate
show the reaction diagram
phosphopantetheine + MgATP2- + 4 H+
dephospho-CoA + diphosphate + Mg2+
show the reaction diagram
-
coenzyme A (CoA) biosynthesis
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
show the reaction diagram
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
phosphopantetheine + Mg-ATP
dephospho-CoA + diphosphate
show the reaction diagram
-
essential hexameric enzyme that catalyzes the penultimate step in coenzyme A biosynthesis
-
-
r
phosphopantetheine + MgATP2- + 4 H+
dephospho-CoA + diphosphate + Mg2+
show the reaction diagram
-
coenzyme A (CoA) biosynthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3'-Dephospho-CoA
-
-
adenosine-5'-[(alpha,beta)-methyleno]triphosphate
-
-
coenzyme A
deoxycholate
-
inactivation at 0.2%, activation at 0.01%
dephospho-CoA
-
-
diphosphate
-
-
pantetheine
-
potent inhibitor
phosphopantetheine
-
-
PTX040334
PTX042695
additional information
-
no inhibition is observed with AMPCPP, ATP-gamma-S, ADPPNP, or ADP at concentrations up to 1 mM and although no inhibition is observed with acetyl-CoA, desulfo-CoA, and palmitoyl-CoA at concentrations up to 500 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cysteine
deoxycholate
-
stimulation at 0.01%, inactivation at 0.2%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0067 - 0.0147
3'-Dephospho-CoA
0.1157 - 1
ATP
0.017
dephospho-CoA
-
; reverse reaction
0.022 - 0.272
diphosphate
0.22
Mg-ATP
-
forward reaction
0.015 - 0.19
pantetheine 4'-phosphate
0.0047
phosphopantetheine
-
; forward reaction
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000917 - 4.808
3'-Dephospho-CoA
4.547
ATP
Mycobacterium tuberculosis
-
at 25C in 75 mM HEPES (pH 7.0)
4.853
pantetheine 4'-phosphate
Mycobacterium tuberculosis
-
at 25C in 75 mM HEPES (pH 7.0)
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.388
adenosine-5'-[(alpha,beta)-methyleno]triphosphate
-
at 25C in 75 mM HEPES (pH 7.0)
0.011 - 0.117
CoA
0.121 - 0.192
dephospho-CoA
0.12
diphosphate
-
Substrate: ATP, Cosubstrate: phosphopantetheine (300 microM)
0.0084 - 0.131
phosphopantetheine
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038
CoA
Arabidopsis thaliana
-
-
0.03
PTX040334
Escherichia coli
-
IC50: 0.03 mM
0.000006
PTX042695
Escherichia coli
-
IC50: 0.000006 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.07
reverse reaction using the purified His-tag fusion protein
7.61
-
-
9.1
-
recombinant enzyme
22.3
-
wild-type enzyme
300
-
diphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.75
-
chromatofocusing technique with a PBE 94 column and Polybuffer 74
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
normal and Plasmodium lophurae-infected
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Bacillus subtilis (strain 168)
Burkholderia pseudomallei (strain 1710b)
Burkholderia pseudomallei (strain 1710b)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Enterococcus faecalis (strain ATCC 700802 / V583)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Helicobacter pylori (strain ATCC 700392 / 26695)
Helicobacter pylori (strain ATCC 700392 / 26695)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Staphylococcus aureus (strain MW2)
Staphylococcus aureus (strain MW2)
Staphylococcus aureus (strain MW2)
Staphylococcus aureus (strain MW2)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
19990
MALDI-TOF mass spectrometry of His-tag fusion protein
62000
gel filtration
67000
-
analytical ultracentrifugation
71000
-
gel filtration
108000
115000
-
gel filtration
118000
-
gel filtration
120000
-
dynamic light-scattering analysis
128600
analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexamer
homohexamer
monomer
trimer
-
alpha3, 3 * 35400, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method, using 0.2 M ammonium sulfate, 0.1 M sodium acetate pH 4.6, 30% (w/v) PEG 2000
ligand-unbound state and in complex with ATP and pantetheine, using 3.5 M sodium formate and 100 mM Tris-HCl (pH 8.5)
-
The best crystals are grown with a reservoir solution consisting of 0.1 M sodium HEPES pH 7.5, 0.8 M sodium dihydrogen phosphate, and 0.8 M potassium dihydrogen phosphate. Tetragonal bipyramidal crystals grew to approximate dimensions of 0.1 x 0.1 x 0.1 mm within a few days.
-
at pH 5.0, 100 mM sodium acetate, pH 5.0, 1.1 M ammonium sulfate, 200 mM NaCl
-
co-crystallization with CoA, space group: I23, with a dimer in the asymmetric unit, a solvent content of 0.57 and a volume-to-protein mass ratio of 288 A3 Da-1
-
co-crystallization with inhibitor PTX040334 in 5% DMSO, 22-32% polyethylene glycol 8000, 200 mM ammonium sulfate in 100 mM cacodylate buffer, pH 6-6.5 at 21C
-
co-crystallization with pantetheine 4'-phosphate or ATP, space group: I23, with a dimer in the asymmetric unit, a solvent content of 57% and a volume-to-protein mass ratio of 288 A3 Da-1
-
hanging drop vapor diffusion method, using 0.1 M TrisHCl, pH 7.0, containing 2.0 M (NH4)2SO4 and 0.2 M Li2SO4
hanging-drop vapour-diffusion method, using sodium chloride as precipitant, trigonal space group P3121 or P3221 with six monomers in the asymmetric unit, a solvent content of 49% and a volume-to-protein mass ratio of 2.39 A3 Da-1
-
mutant enzyme I4V/N76Y
-
apo form and in complex with ATP, counter-diffusion method, using 40 mM cacodylate buffer pH 5.5 containing 10 mM MgCl2, 0.15 mM NaCl, 20 mM cobalt hexamine and 15% (w/v) 2-methyl-2,4-pentanediol as precipitant solution
-
enzyme in complex with pantetheine 4'-phosphate and adenosine-5'-[(alpha,beta)-methyleno]triphosphate, sitting drop vapor diffusion method, using 38% (v/v) polyethylene glycol 200 and 0.1 M HEPES (pH 7.2), at 21C
-
hanging drop vapor diffusion method
-
in complex with coenzyme A, hanging drop vapor diffusion method, using 0.1 M Tris base pH 8.0 and 0.15 M magnesium formate
-
hanging-drop vapour-diffusion method, 23.85C
oil batch method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
-
2 min, inactivation at 46C
643176
6.7
-
t1/2: 2 min at 46C
643176
10
-
2 min, 10% loss of activity at 46C
643176
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
2 min, partial inactivation
46
-
t1/2: 2 min at pH 6.7, pH 10: 10% loss of activity, pH 5.5: 2 min, inactivation
50
-
2 min, inactivation
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 0.5 mg protein/ml, at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Co2 + affinity column chromatography
copurification as hexamer with 0.5 equivalents of CoA tightly bound per PPAT monomer
-
His Trap column chromatography, and Superdex 200 gel filtration
Ni-nitrilotriacetic acid-agarose affinity chromatography, gel filtration
Ni-NTA agarose column chromatography and Superdex 200 gel filtration
-
partial
Q Sepharose XL resin column chromatography, Q Sepharose HP resin column chromatography, and Sepharose S-200 gel filtration
-
recombinant protein using His-tag
the fusion protein was purified by amylose affinity chromatography
-
to homogenity
wild-type and recombinant enzyme to homogenity
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 (DE3)
-
expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)R3 Rosetta cells
expressed in Escherichia coli ER2566 cells
-
expression in Escherichia coli BL21
expression of His6-tagged and wild-type PPAT in Escherichia coli BL21(DE3)
-
expression of native gene in Escherichia coli BL21(DE3) not possible, expression of optimized gene in Escherichia coli BL21(DE3) as His-tag fusion protein
expression of recombinant MBP-PPAT was induced with 1 mM isopropylthio-beta-galactoside in Escherichia coli DH5alpha cells
-
His-tag, expressed in Escherichia coli
overexpression in Escherichia coli
overexpression in Escherichia coli JM101
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
R106A
-
pantothenate kinase (PanK) mutant
I4V/N76Y
-
the mutant is a homotetramer. Despite structural differences between wild type enzyme and IV4/N76Y, they have similar ligand-binding properties
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
medicine
-
PPAT is a target for antibacterial drug discovery
Show AA Sequence (10248 entries)
Longer loading times are possible. Please use the Sequence Search for a certain query.