Information on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase

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

EC NUMBER
COMMENTARY
2.7.7.3
-
RECOMMENDED NAME
GeneOntology No.
pantetheine-phosphate adenylyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
ATP + pantetheine 4'-phosphate = diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adenosyl group transfer
-
-
nucleotidyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
coenzyme A biosynthesis
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3'-dephospho-CoA pyrophosphorylase
-
-
-
-
4'-phosphopantetheine adenylyltransferase
-
-
dephospho-CoA pyrophosphorylase
-
-
-
-
dephospho-coenzyme A pyrophosphorylase
-
-
-
-
pantetheine phosphate adenylyltransferase
-
-
-
-
phosphopantetheine adenylyltransferase
-
-
phosphopantetheine adenylyltransferase
Q3JW91
-
phosphopantetheine adenylyltransferase
-
-
phosphopantetheine adenylyltransferase
-
-
phosphopantetheine adenylyltransferase
-
-
phosphopantetheine adenylyltransferase
O26010
-
phosphopantetheine adenylyltransferase
-
-
phosphopantetheine adenylyltransferase
P0A530
-
phosphopantetheine adenylyltransferase
P63819
-
PPAT
-
-
-
-
PPAT
O26010
-
Enterococcus faecalis PPAT
-
-
additional information
-
bifunctional enzyme catalyzing the last two steps of coenzyme A biosynthesis
additional information
Mycobacterium tuberculosis Rv2965c
-
bifunctional enzyme catalyzing the last two steps of coenzyme A biosynthesis
-
additional information
-
with EC 2.7.1.24 part of a bifunctional enzyme with EC 2.7.1.24
CAS REGISTRY NUMBER
COMMENTARY
9026-99-7
-
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-, Q3JW91
the enzyme catalyzes the fourth of five steps in the coenzyme A biosynthetic pathway
metabolism
-
the enzyme catalyzes the penultimate step in the coenzyme A biosynthetic pathway
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
-
coenzyme A biosynthetic pathway
-
-
r
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
show the reaction diagram
-
important enzyme in CoA biosynthesis
-
-
r
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
P63819, -
-
-
-
r
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
-
-
-
-
-
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
P0A6I6
-
-
-
r
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
Q13057
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
-
-
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
-
-
-
-
-
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
Q8MIR4
-
-
-
r
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
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
-
-
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
-
?
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
-
-
-
-
-
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
-
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
Q9UYT0
-
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-, P0A530
-
-
-
r
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
-, Q3JW91
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-, O26010
-
-
-
?
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
no substrates are GTP, ITP, UTP, or CTP
-
-
-
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
no substrate is 4'-pantothenoyl-L-cysteine
-
-
-
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
involved in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
involved in coenzyme A biosynthesis
-
-
-
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
involved in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
Q9UYT0
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
Mycobacterium tuberculosis Rv2965c
-
-, rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
diphosphate + 3'-dephospho-CoA
ATP + pantetheine 4'-phosphate
show the reaction diagram
-
-
-
-
r
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
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
show the reaction diagram
-
coenzyme A biosynthetic pathway
-
-
r
4'-phosphopantetheine + ATP
3'-dephospho-CoA + diphosphate
show the reaction diagram
-
important enzyme in CoA biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
-
-
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
-
-
-
-
-
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
-
-
-
-
-
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
-
-
-
-
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
-
involved in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
involved in coenzyme A biosynthesis
-
-
-
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
involved in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
Q9UYT0
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
Mycobacterium tuberculosis Rv2965c
-
rate-limiting penultimate step in coenzyme A biosynthesis
-
-
r
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 ACCESSION NO.
COMMENTARY
LITERATURE
Mg2+
-
requirement, 2 mM
Mg2+
-
required for activity
Mg2+
-
the enzyme contains a catalytic Mg2+ ion
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3'-Dephospho-CoA
-
-
adenosine-5'-[(alpha,beta)-methyleno]triphosphate
-
-
-
coenzyme A
-, O26010
feedback inhibition
deoxycholate
-
inactivation at 0.2%, activation at 0.01%
dephospho-CoA
-
-
pantetheine
-
potent inhibitor
phosphopantetheine
-
-
PTX040334
-
IC50: 0.03 mM
PTX040334
-
no inhibition
PTX042695
-
IC50: 0.000006 mM
PTX042695
-
no inhibition
diphosphate
-
-
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
cysteine
-
activation, in vitro
cysteine
-
requirement
deoxycholate
-
stimulation at 0.01%, inactivation at 0.2%
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0067
-
3'-Dephospho-CoA
-
apparent value, at 25C in 50 mM Tris (pH 8.0)
0.007
-
3'-Dephospho-CoA
-
-
0.007
-
3'-Dephospho-CoA
-
25C, pH 8
0.0147
-
3'-Dephospho-CoA
Q8MIR4
25C, pH 8
0.1157
-
ATP
-
apparent value, at 25C in 75 mM HEPES (pH 7.0)
0.3
-
ATP
-
30C, pH 8.5, cytosol
1
-
ATP
-
37C, pH 8
0.017
-
dephospho-CoA
-
; reverse reaction
0.022
-
diphosphate
-
-
0.022
-
diphosphate
-
25C, pH 8
0.23
-
diphosphate
-
; reverse reaction
0.272
-
diphosphate
Q8MIR4
25C, pH 8
0.22
-
Mg-ATP
-
forward reaction
0.015
-
pantetheine 4'-phosphate
-
30C, pH 8.5
0.0377
-
pantetheine 4'-phosphate
-
apparent value, at 25C in 75 mM HEPES (pH 7.0)
0.14
-
pantetheine 4'-phosphate
-
37C, pH 8
0.19
-
pantetheine 4'-phosphate
-
pH 8
0.0047
-
phosphopantetheine
-
; forward reaction
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000917
-
3'-Dephospho-CoA
-
25C, pH 8
4.808
-
3'-Dephospho-CoA
-
at 25C in 50 mM Tris (pH 8.0)
4.547
-
ATP
-
at 25C in 75 mM HEPES (pH 7.0)
4.853
-
pantetheine 4'-phosphate
-
at 25C in 75 mM HEPES (pH 7.0)
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.388
-
adenosine-5'-[(alpha,beta)-methyleno]triphosphate
-
at 25C in 75 mM HEPES (pH 7.0)
-
0.011
-
CoA
-
Substrate: dephospho-CoA, Cosubstrate: diphosphate (1.6 mM)
0.014
-
CoA
-
Substrate: phosphopantetheine, Cosubstrate: ATP (300 microM)
0.07
-
CoA
-
Substrate: ATP, Cosubstrate: phosphopantetheine (300 microM)
0.117
-
CoA
-
Substrate: Pyrophosphate, Cosubstrate: dephospho-CoA (300 microM)
0.121
-
dephospho-CoA
-
Substrate: phosphopantetheine, Cosubstrate: ATP (3.0 mM)
0.192
-
dephospho-CoA
-
Substrate: ATP, Cosubstrate: phosphopantetheine (300 microM)
0.12
-
diphosphate
-
Substrate: ATP, Cosubstrate: phosphopantetheine (300 microM)
0.0084
-
phosphopantetheine
-
Substrate: dephospho-CoA, Cosubstrate: diphosphate (1.6 mM)
0.131
-
phosphopantetheine
-
Substrate: diphosphate, Cosubstrate: dephospho-CoA (500 microM)
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
PTX040334
-
IC50: 0.03 mM
0.000006
-
PTX042695
-
IC50: 0.000006 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.07
-
Q9UYT0
reverse reaction using the purified His-tag fusion protein
7.61
-
-
-
9.1
-
-
recombinant enzyme
22.3
-
-
wild-type enzyme
300
-
-
diphosphate
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
37
-
-
assay at
41
-
-
assay at
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.75
-
-
chromatofocusing technique with a PBE 94 column and Polybuffer 74
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
normal and Plasmodium lophurae-infected
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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)
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
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
19990
-
Q9UYT0
MALDI-TOF mass spectrometry of His-tag fusion protein
20000
-
-
gel filtration
20000
-
Q9UYT0
SDS-PAGE of His-tag fusion protein
62000
-
Q8MIR4
gel filtration
67000
-
-
analytical ultracentrifugation
71000
-
-
gel filtration
108000
-
-
gel filtration
108000
-
-
ultracentrifugation
115000
-
-
gel filtration
118000
-
-
gel filtration
120000
-
-
dynamic light-scattering analysis
128600
-
-, O26010
analytical ultracentrifugation
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
alpha2, 2 * 57000, SDS-PAGE
dimer
-
alpha2, 2 * 61000, SDS-PAGE, subunit structure
hexamer
-
crystallization studies
hexamer
-
alpha6, 6 * 17800, SDS-PAGE
hexamer
-
6 * 17800
hexamer
-
6 * 17700, crystal structure analysis, analytical ultracentrifugation data of the native enzyme suggests an equilibrium of two trimers and one hexamer in solution
hexamer
-
crystal structure analysis hexamer is composed of two identical trimers, ligand binding was found to alter the protein structure
hexamer
-
x-ray crystallography
homohexamer
-
the calculated monomer weight including the C-terminal tag is 19741 Da
homohexamer
-
6*17800, the dyad axis of the hexamer divides the protein into two asymmetrical trimers; taken from literature, 6*17800Da
homohexamer
P63819, -
crystal structure analysis
homohexamer
-, Q3JW91
x-ray crystallography
homohexamer
-, O26010
6 * 19701, MALDI-TOF mass spectrometry; 6 * 20000, SDS-PAGE
homohexamer
-
x-ray crystallography
homohexamer
-
x-ray crystallography
monomer
Q8MIR4
1 * 62000, gel filtration
monomer
-
1 * 20000, gel filtration
monomer
Q9UYT0
1 * 20000, SDS-PAGE of His-tag fusion protein, circular dichroism, and 2D NMR experiments, 1 * 19992, MALDI-TOF mass spectrometry
trimer
-
alpha3, 3 * 35400, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-, Q3JW91
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
-, O26010
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
P63819, -
oil batch method
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
2 min, inactivation at 46C
6.7
-
-
t1/2: 2 min at 46C
10
-
-
2 min, 10% loss of activity at 46C
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
LITERATURE
-20C, 0.5 mg protein/ml, at least 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the fusion protein was purified by amylose affinity chromatography
-
His Trap column chromatography, and Superdex 200 gel filtration
-, Q3JW91
copurification as hexamer with 0.5 equivalents of CoA tightly bound per PPAT monomer
-
wild-type and recombinant enzyme to homogenity
-
Co2 + affinity column chromatography
-, O26010
Ni-NTA agarose column chromatography and Superdex 200 gel filtration
-
Q Sepharose XL resin column chromatography, Q Sepharose HP resin column chromatography, and Sepharose S-200 gel filtration
-
recombinant protein using His-tag
Q9UYT0
to homogenity
-
Ni-nitrilotriacetic acid-agarose affinity chromatography, gel filtration
P63819, -
partial
-
to homogenity
Q8MIR4
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression of recombinant MBP-PPAT was induced with 1 mM isopropylthio-beta-galactoside in Escherichia coli DH5alpha cells
-
expressed in Escherichia coli BL21(DE3)R3 Rosetta cells
-, Q3JW91
expression of His6-tagged and wild-type PPAT in Escherichia coli BL21(DE3)
-
overexpression in Escherichia coli JM101
-
expressed in Escherichia coli BL21(DE3) cells
-, O26010
overexpression in Escherichia coli
-
expression in Escherichia coli BL21
Q13057
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli ER2566 cells
-
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
Q9UYT0
overexpression in Escherichia coli
-
His-tag, expressed in Escherichia coli
P63819, -
expressed in Escherichia coli BL21 (DE3)
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
PPAT is a target for antibacterial drug discovery
drug development
-
potential target for antibiotic drugs
drug development
Mycobacterium tuberculosis Rv2965c
-
potential target for antibiotic drugs
-