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Information on EC 2.7.7.3 - pantetheine-phosphate adenylyltransferase and Organism(s) Helicobacter pylori and UniProt Accession O26010

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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:
Helicobacter pylori
UNIPROT: O26010
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The taxonomic range for the selected organisms is: Helicobacter pylori
The enzyme appears in selected viruses and cellular organisms
Synonyms
phosphopantetheine adenylyltransferase, 4'-phosphopantetheine adenylyltransferase, pantetheine phosphate adenylyltransferase, pantetheine-phosphate adenylyltransferase, dephospho-coa pyrophosphorylase, enterococcus faecalis ppat, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphopantetheine adenylyltransferase
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3'-dephospho-CoA pyrophosphorylase
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-
-
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dephospho-CoA pyrophosphorylase
-
-
-
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dephospho-coenzyme A pyrophosphorylase
-
-
-
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pantetheine phosphate adenylyltransferase
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-
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phosphopantetheine adenylyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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-
-
-
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
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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
ATP + pantetheine 4'-phosphate
diphosphate + 3'-dephospho-CoA
show the reaction diagram
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
coenzyme A
feedback inhibition
D-amethopterin
a mixed-type inhibitor of HpPPAT activity, that simultaneously occupies the HpPPAT 4'-phosphopantetheine- and ATP-binding sites, the compound can serve as a lead compound in drug development, steady-state kinetic inhibition assay. Model of HpPPAT complexed with D-amethopterin, overview
additional information
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.2674
D-amethopterin
pH 7.9, 25°C, recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
enzyme inactivation effectively prevents bacterial viability
metabolism
the enzyme catalyzes the penultimate step in coenzyme A biosynthesis
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
128600
analytical ultracentrifugation
19701
6 * 19701, MALDI-TOF mass spectrometry
20000
6 * 20000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homohexamer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.1 M Tris–HCl, 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
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mutant enzyme I4V/N76Y
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I4V/N76Y
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the mutant is a homotetramer. Despite structural differences between wild type enzyme and IV4/N76Y, they have similar ligand-binding properties
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Co2 + affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
recombinant expression in Escherichia coli strain BL21(DE3)
overexpression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development
the enzyme is an attractive target for antibacterial drug development against Helicobacter pylori
medicine
the enzyme is a therapeutical target in treatment of Helicobacter induced gastritis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eom, S.J.; Ahn, H.J.; Kim, H.W.; Baek, S.H.; Suh, S.W.
Crystallization and preliminary X-ray crystallographic studies of phosphopantetheine adenylyltransferase from Helicobacter pylori
Acta Crystallogr. Sect. D
59
561-562
2003
Helicobacter pylori
Manually annotated by BRENDA team
Cheng, C.S.; Chen, C.H.; Luo, Y.C.; Chen, W.T.; Chang, S.Y.; Lyu, P.C.; Kao, M.C.; Yin, H.S.
Crystal structure and biophysical characterisation of Helicobacter pylori phosphopantetheine adenylyltransferase
Biochem. Biophys. Res. Commun.
408
356-361
2011
Helicobacter pylori (O26010), Helicobacter pylori
Manually annotated by BRENDA team
Cheng, C.S.; Chen, W.T.; Chen, Y.W.; Chen, C.H.; Luo, Y.C.; Lyu, P.C.; Yin, H.S.
Substitution of asparagine 76 by a tyrosine residue induces domain swapping in Helicobacter pylori phosphopantetheine adenylyltransferase
J. Biomol. Struct. Dyn.
30
488-502
2012
Helicobacter pylori
Manually annotated by BRENDA team
Cheng, C.S.; Jia, K.F.; Chen, T.; Chang, S.Y.; Lin, M.S.; Yin, H.S.
Experimentally validated novel inhibitors of Helicobacter pylori phosphopantetheine adenylyltransferase discovered by virtual high-throughput screening
PLoS ONE
8
e74271
2013
Helicobacter pylori (O26010), Helicobacter pylori
Manually annotated by BRENDA team