Information on EC 2.7.1.33 - pantothenate kinase

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

EC NUMBER
COMMENTARY
2.7.1.33
-
RECOMMENDED NAME
GeneOntology No.
pantothenate kinase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
show the reaction diagram
bi bi mechanism
-
ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
show the reaction diagram
active site structure, mechanism, pantothenate binding site structure, the reaction proceeds by a concerted mechanism that involves a dissociative transition state, although the negative charge neutralization of the gamma-phosphate by Arg243, Lys101, and Mg2+ coupled with hydrogen bonding of the C1 of pantothenate to Asp127 suggests different interpretations of the phosphoryl transfer mechanism of pantothenate kinase
P0A6I3
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme A biosynthesis II (mammalian)
-
-
coenzyme A metabolism
-
-
Metabolic pathways
-
-
Pantothenate and CoA biosynthesis
-
-
phosphopantothenate biosynthesis I
-
-
phosphopantothenate biosynthesis II
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-pantothenate 4'-phosphotransferase
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D-pantothenate kinase
-
-
-
-
hPanK
-
-
-
-
hPanK1
-
-
-
-
hPANK2
-
-
-
-
hPanK3
-
-
-
-
hPanK4
-
-
-
-
kinase, pantothenate (phosphorylating)
-
-
-
-
mPank
-
-
-
-
mPank1
-
-
-
-
mPanK3
-
-
-
-
PAK
-
-
-
-
pantothenic acid kinase
-
-
-
-
rPanK4
-
-
-
-
Rts protein
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9026-48-6
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ecotype Colombia-0
-
-
Manually annotated by BRENDA team
gene coaX
-
-
Manually annotated by BRENDA team
gene coaA
Uniprot
Manually annotated by BRENDA team
K-12 strains UB 1005, SJ16, DV1
-
-
Manually annotated by BRENDA team
K12 strain ts9
-
-
Manually annotated by BRENDA team
gene coaX
SwissProt
Manually annotated by BRENDA team
isoform PanK3
SwissProt
Manually annotated by BRENDA team
multiple genes, multiple enzyme forms
-
-
Manually annotated by BRENDA team
splice variant pantothenate kinase 2, i.e. PanK2, contains mutation G521R, several isozymes e.g. iPanK2, spPanK2, mPanK2, overview
-
-
Manually annotated by BRENDA team
the 5' end of PANK2 gene, Hallervorden-Spatz syndrome, and a CpG island, complete sequence; enzyme form PANK2, 2 allelic variants
SwissProt
Manually annotated by BRENDA team
isoforms mPanK1alpha, mPanK1beta
SwissProt
Manually annotated by BRENDA team
isozyme PanK1alpha
-
-
Manually annotated by BRENDA team
male C57BL6/J mice, isozyme PanK3 and PanK1beta
-
-
Manually annotated by BRENDA team
strain H37Rv
SwissProt
Manually annotated by BRENDA team
Mycobacterium tuberculosis H37Rv (ATCC 27294)
-
-
-
Manually annotated by BRENDA team
no activity in Lactobacillus helveticus
-
-
-
Manually annotated by BRENDA team
no activity in Neurospora crassa
-
-
-
Manually annotated by BRENDA team
; strains 3D7 and FAF6
-
-
Manually annotated by BRENDA team
strain 3D7
-
-
Manually annotated by BRENDA team
male Wistar
-
-
Manually annotated by BRENDA team
male Wistar; on normal or clofibrate enriched diet
-
-
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
strain RN4220, gene coaA
-
-
Manually annotated by BRENDA team
Staphylococcus aureus RN4220
strain RN4220, gene coaA
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
disease: pantothenate kinase-associated neurodegeneration
malfunction
-
pantothenate kinase-associated neurodegeneration, formerly known as Hallervorden-Spatz syndrome
malfunction
-
flies carrying a fumble loss-of-function allele have a 3fold increase in total zinc levels per dry weight when compared to control strains, but no change in total iron, copper or manganese levels
malfunction
-
the elimination of PanK1 reduces hepatic CoA levels. Pank1-deficient mice become hypoglycemic during a fast due to impaired gluconeogenesis
physiological function
-
CoaA is essential for survival of Mycobacterium tuberculosis. The coax gene is unable to complement the loss of gene coaA. CoaX lacks pantothenate kinase activity in vitro and is not required for survival in macrophages and mice
physiological function
-
pantothenate kinase 1 is required to support the metabolic transition from the fed to the fasted state
physiological function
Mycobacterium tuberculosis H37Rv (ATCC 27294)
-
CoaA is essential for survival of Mycobacterium tuberculosis. The coax gene is unable to complement the loss of gene coaA. CoaX lacks pantothenate kinase activity in vitro and is not required for survival in macrophages and mice
-
metabolism
-
pantothenate kinase catalyzes the rate-controlling step in coenzyme A biosynthesis
additional information
-
mitochondria-targeted human pantothenate kinase-2 is involved in pantothenate kinase-associated neurodegeneration
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
show the reaction diagram
Q5JHF1
the enzyme is involved in coenzyme A biosynthesis in the archaea
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Q6G7I0
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Q9H999
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Q9HWC1
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
P9WPA7
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Q81VX4
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Q9BZ23
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
p37564
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Q923S8
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
D2K764
-
-
-
ir
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
p37564
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis, regulatory function
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
P0A6I3
first step in coenzyme A biosynthesis, the enzyme has a regulatory function in the pathway
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
i.e. vitamin B5
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
P0A6I3
pantothenate binding site structure involving residues E249, Y262, F247, F259, Y258, and F244, located at the distal end of a large surface groove, induced fit binding mechanism, overview
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
the enzyme is absolutely specific for ATP, no activity with CTP, GTP, UTP, or phosphoenolpyruvate as phosphoryl donors
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
the phosphate binding loop of isozyme mPanK2 is the N-terminal motif DIGGT(S)XXK
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
coaX is essential for growth of Bacillus anthracis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Mycobacterium tuberculosis H37Rv (ATCC 27294)
-
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis, i.e. vitamin B5
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
D2K764
-
-
-
ir
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Staphylococcus aureus RN4220
-
first step in coenzyme A biosynthesis
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
Q8K4K6
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
poor phosphate donor: alpha,beta-methyleneadenosine 5'-triphosphate, transfers the gamma-phosphate of ATP to pantothenate
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
D-configuration of 2'-hydroxyl group in pantothenate molecule is essential for functional interaction with enzyme
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
first and rate-controlling reaction of CoA-biosynthesis
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
first and rate-controlling reaction of CoA-biosynthesis
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
?
ATP + D-pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + D-pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
Q8TE04, Q9H999
-
-
-
?
ATP + N-alkylpantothenamides
ADP + ?
show the reaction diagram
P0A6I3
growth-inhibiting anti-metabolite, modeling into the active site structure
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram
P0A6I3
-
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram
-
substrate is converted to the inactive butyldethia-CoA analogue in the further downstream pathway leading to grwoth inhibition of the organism, overview
-
-
?
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram
Staphylococcus aureus RN4220
-
substrate is converted to the inactive butyldethia-CoA analogue in the further downstream pathway leading to grwoth inhibition of the organism, overview
-
-
?
ATP + N-nonylpantothenamide
ADP + N-nonylpantothenamide 4-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-pentylpantothenamide
ADP + N-pentylpantothenamide 4-phosphate
show the reaction diagram
-
-
-
-
?
ATP + N-pentylpantothenamide
ADP + N-pentylpantothenamide 4-phosphate
show the reaction diagram
P0A6I3
-
-
-
?
ATP + N-pentylpantothenamide
ADP + N-pentylpantothenamide 4-phosphate
show the reaction diagram
Staphylococcus aureus RN4220
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Q9WZY5
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step of the pathway from pantothenate to CoA. The activity of this protein is tightly regulated by CoA feedback inhibition, both in vitro and in vivo
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
P9WPA7
-
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
Q8TE04, Q9H999
pantothenate kinase catalyzes the first step in CoA biosynthesis
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
P9WPA7
-
-
-
?
ATP + pantothenate
?
show the reaction diagram
-
-
-
-
?
ATP + pantothenate
ADP + (R)-4-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + pantothenol
ADP + 4'-phosphopantothenol
show the reaction diagram
P9WPA7
-
-
-
?
CTP + (R)-pantothenate
CDP + (R)-4'-phosphopantothenate
show the reaction diagram
p37564
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
GTP + (R)-pantothenate
GDP + (R)-4'-phosphopantothenate
show the reaction diagram
p37564
-
-
-
?
GTP + pantothenate
GDP + D-4'-phosphopantothenate
show the reaction diagram
-
phosphorylation at 28% the rate of ATP
-
-
?
GTP + pantothenate
GDP + D-4'-phosphopantothenate
show the reaction diagram
-
phosphorylation at 20% the rate of ATP
-
-
?
pantetheine + ATP
D-4'-phosphopantetheine + ADP
show the reaction diagram
-
-
-
-
?
panthenoylcysteine + ATP
D-4'-phosphopanthenoylcysteine + ADP
show the reaction diagram
-
-
-
-
?
pantothenate + ATP
phosphopantothenate + ADP
show the reaction diagram
-
-
-
-
?
pantothenate + ATP
phosphopantothenate + ADP
show the reaction diagram
Q839J7
-
-
-
?
pantothenate + ATP
phosphopantothenate + ADP
show the reaction diagram
Q6L2I5
relative activity with GTP: 81%, CTP: 68%, and UTP: 91.8%
-
-
?
pantothenate + ATP
4'-phosphopantothenate + ADP
show the reaction diagram
-
-
-
-
?
pantothenate + ATP
4'-phosphopantothenate + ADP
show the reaction diagram
-
-
-
-
?
pantothenate + CTP
4'-phosphopantothenate + CDP
show the reaction diagram
-
-
-
-
?
pantothenate + dATP
4'-phosphopantothenate + dADP
show the reaction diagram
-
-
-
-
?
pantothenate + dCTP
4'-phosphopantothenate + dCDP
show the reaction diagram
-
-
-
-
?
pantothenate + dGTP
4'-phosphopantothenate + dGDP
show the reaction diagram
-
-
-
-
?
pantothenate + dTTP
4'-phosphopantothenate + dTDP
show the reaction diagram
-
-
-
-
?
pantothenate + UTP
4'-phosphopantothenate + UDP
show the reaction diagram
-
-
-
-
?
pantothenyl alcohol + ATP
D-4'-phosphopantothenyl alcohol + ADP
show the reaction diagram
-
-
-
-
?
UTP + pantothenate
UDP + D-4'-phosphopantothenate
show the reaction diagram
-
phosphorylation at 18% the rate of ATP
-
-
?
ITP + pantothenate
IDP + D-4'-phosphopantothenate
show the reaction diagram
-
phosphorylation at 46% the rate of ATP
-
-
?
additional information
?
-
-
naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease
-
-
-
additional information
?
-
Q9BZ23
naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease
-
-
-
additional information
?
-
-
N-pentylpantothenate is no substrate
-
-
-
additional information
?
-
p37564
N-pentylpantothenate is no substrate, no activity with UTP or phosphoenolpyruvate as phosphoryl donors
-
-
-
additional information
?
-
P0A6I3
no acivity with hopantenate, formation of a pantothenate kinase-ADP-pantothenate ternary complex
-
-
-
additional information
?
-
-
miRNAs, which exist in vertebrate genomes within introns of the pantothenate kinase genes, are predicted by bioinformatics to affect multiple mRNA targets in pathways that involve cellular acetyl-CoA and lipid levels. Significantly, PANK enzymes also affect these pathways, so the miRNA and host gene may act synergistically. These predictions require experimental verification
-
-
-
additional information
?
-
-
pantothenate kinase is upregulated in the warming treatment
-
-
-
additional information
?
-
Q81VX4
type III PanK in the spore-forming Bacillus anthracis plays an essential role in the novel thiol/disulfide redox biology of this category A biodefense pathogen
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (R)-4-phosphopantoate + beta-alanine
AMP + diphosphate + (R)-4'-phosphopantothenate
show the reaction diagram
Q5JHF1
the enzyme is involved in coenzyme A biosynthesis in the archaea
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Q9BZ23
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
p37564
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis, regulatory function
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
P0A6I3
first step in coenzyme A biosynthesis, the enzyme has a regulatory function in the pathway
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
coaX is essential for growth of Bacillus anthracis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step in coenzyme A biosynthesis
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
Staphylococcus aureus RN4220
-
first step in coenzyme A biosynthesis
-
-
?
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
first and rate-controlling reaction of CoA-biosynthesis
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
-
first and rate-controlling reaction of CoA-biosynthesis
-
-
-
ATP + D-pantothenate
ADP + D-4'-phosphopantothenate
show the reaction diagram
Rattus norvegicus Sprague-Dawley
-
-
-
-
-
ATP + N-heptylpantothenamide
ADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram
Staphylococcus aureus, Staphylococcus aureus RN4220
-
substrate is converted to the inactive butyldethia-CoA analogue in the further downstream pathway leading to grwoth inhibition of the organism, overview
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
first step of the pathway from pantothenate to CoA. The activity of this protein is tightly regulated by CoA feedback inhibition, both in vitro and in vivo
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
Q8TE04, Q9H999
pantothenate kinase catalyzes the first step in CoA biosynthesis
-
-
?
additional information
?
-
-
naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease
-
-
-
additional information
?
-
Q9BZ23
naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease
-
-
-
additional information
?
-
-
miRNAs, which exist in vertebrate genomes within introns of the pantothenate kinase genes, are predicted by bioinformatics to affect multiple mRNA targets in pathways that involve cellular acetyl-CoA and lipid levels. Significantly, PANK enzymes also affect these pathways, so the miRNA and host gene may act synergistically. These predictions require experimental verification
-
-
-
additional information
?
-
-
pantothenate kinase is upregulated in the warming treatment
-
-
-
additional information
?
-
Q81VX4
type III PanK in the spore-forming Bacillus anthracis plays an essential role in the novel thiol/disulfide redox biology of this category A biodefense pathogen
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ATP
P0A6I3
three-dimensional binding site structure, Arg243 is involved
ATP
-
absolutely specific for
ATP
p37564
can partially be substituted by CTP or GTP
ATP
Q81VX4
-
ATP
Q923S8
-
CTP
p37564
less active than ATP
GTP
p37564
less active than ATP
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
-
activation, can replace Mg2+
K+
Q9HWC1
0.06-0.12 mM
K+
Q6G7I0
0.06-0.12 mM
Mg2+
-
requirement, active substrate: MgATP-complex
Mg2+
-
requirement, active substrate: MgATP-complex
Mg2+
-
Km-value: 1 mM; requirement, active substrate: MgATP-complex
Mg2+
-
Km-value: 0.6 mM; requirement, active substrate: MgATP-complex
Mg2+
P0A6I3
coordinated by the nucleotide beta- and gamma-phosphates and the side chains of Ser102 and Glu199, required for ATP but not for ADP binding
Mg2+
p37564
-
Mg2+
Q9HWC1
required
Mg2+
Q6G7I0
required
Mg2+
Q6L2I5
activity with 1 mM (plus 2.5 mM ATP): 252 nmol/min/mg
Mn2+
-
activation, can replace Mg2+
NH4+
Q9HWC1
induces a 5fold higher activation than either K+ or Rb+
NH4+
Q6G7I0
induces a 5fold higher activation than either K+ or Rb+
Ni2+
-
activation, can replace Mg2+ with about 50% efficiency
Zn2+
-
activation, can replace Mg2+ with about 50% efficiency
Mn2+
Q6L2I5
addition (1 mM) instead of Mg2+ accelerates activity 1.75fold
additional information
-
no activation by Ca2+, Cd2+, Ba2+, Pb2+, Fe2+ or Cu2+
additional information
-
nonspecific activation by anions in triethanolamine buffer, pH 7, mostly dicarboxylic acids, not citrate or diphosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-2,4-dihydroxy-3,3-dimethylbutanohydrazide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-2,4-dihydroxy-N-(2-hydroxyethyl)-3,3-dimethylbutanamide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-N-(2,3-dihydroxypropyl)-2,4-dihydroxy-3,3-dimethylbutanamide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(R)-3-azido-4,4-dimethyl-dihydro-furan-2-one
-
-
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
80.6% inhibition at 0.1 mM, purified enzyme
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
29.4% inhibition at 0.1 mM, purified enzyme
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
2.7% inhibition at 0.1 mM, cell extract
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
78.7% inhibition at 0.1 mM, purified enzyme
(R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
11% inhibition at 0.1 mM, purified enzyme
(R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
13.1% inhibition at 0.1 mM, cell extract
(R)-4-(2-azido-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
-
(S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
12.5% inhibition at 0.1 mM, purified enzyme
(S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid
-
54.6% inhibition at 0.1 mM, purified enzyme
(S)-trifluoro-methanesulfonic acid 4,4-dimethyl-2-oxo-tetrahydro-furan-3-yl-ester
-
-
1,4-dioxa-8-azaspiro[4.5]dec-8-yl[2-[(3-fluorophenyl)sulfanyl]pyridin-4-yl]methanone
-
mixed non-competitive inhibition
1,4-phenylene-bis(1,2-ethanediyl)bis-isothiourea dihydrobromide
Q9H999
-
-
2'-Ketopantetheine
-
-
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
-
10.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
-
76.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
-
89.6% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramide
-
98.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
-
46.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
-
71.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
-
89.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramide
-
97.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
12.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
72.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
81.4% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
98.8% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
-
59.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
-
57.8% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
-
80.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramide
-
89.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
51.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
82.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
86.8% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
99.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
-
40.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
-
71.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
-
84.6% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramide
-
86.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
-
35.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
-
44.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
-
70.5% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramide
-
17.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
-
28.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
-
33.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
-
57.4% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramide
-
8.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
-
71.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
-
3.0% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
-
93.3% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramide
-
76.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
-
41.8% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
-
28.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
-
68.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramide
-
95.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
61.0% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
53.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
82.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
97.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
49.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
61.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
85.0% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramide
-
96.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
-
13.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
-
10.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
-
39.1% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramide
-
4.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
-
92.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
-
90.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
-
98.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramide
-
97.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
62.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
32.3% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
61.2% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
96.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
72.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
54.3% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
87.2% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
97.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
54.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
55.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
82.2% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
53.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
-
15.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
-
7.3% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
-
73.0% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramide
-
9.3% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
25.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
3.4% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
56.7% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
72.2% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
26.8% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
28.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
67.6% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
90.1% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
i.e. pantothenol, 36.7% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
i.e. pantothenol, 11.5% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
i.e. pantothenol, 70.3% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
i.e. pantothenol, 79.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
52.9% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
38.6% inhibition at 0.1 mM, purified enzyme
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
64.9% inhibition at 0.1 mM, cell extract
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
94.4% inhibition at 0.1 mM, purified enzyme
2-[2-(1-benzoylpiperidin-4-yl)-5-methyl-1,3-thiazol-4-yl]-N-(4-methylphenyl)acetamide
-
uncompetitive inhibition
4-(2,4-dihydroxy-3,3-dimethylbutylamido)butyric acid
-
competitive inhibitor; competitive inhibitor, IC50: 0.05-0.15 mM
4-phosphopantoate
Q5JHF1
substrate inhibition
5'-deoxy-5'-(4-(beta-D-galactopyranosyloxymethyl)-1,2,3-triazol-1-yl)adenosine
-
competitive inhibitor with respect to ATP
acetoacetyl-CoA
-
-
acetyl-CoA
-
-
acetyl-CoA
-
strong
acetyl-CoA
O93921
selective and strong, competitive to ATP
acetyl-CoA
-
feedback inhibition, regulatory function, isozyme PanK1beta and isozyme PanK3, strong inhibition of mutant chimera PanK1beta-3-1beta, slight inhibition of mutant chimera PanK3-1beta-3
acetyl-CoA
-
effective inhibitor
acetyl-CoA
-
competitive inhibitor of purified PanK2 with respect to ATP; IC50: 60 nM, competitive inhibitor with respect to ATP
acetyl-CoA
Q8TE04, Q9H999
a feedback inhibitor; a feedback inhibitor
acetyl-CoA
Q9H999
complete inhibition of isoform PanK3 at 0.008 mM
Acyl carrier protein
-
-
Acyl carrier protein
-
PAK II: inhibition, PAK I: stimulation between 0.015-0.035 mM
acyl-CoA-esters
-
long-chain acyl-CoAs less efficient than short-chain ester
acyl-CoA-esters
-
-
acyl-CoA-esters
-
long chain acyl CoA, feed-back inhibition, isoform PanK1alpha
ADP
Q9H999
competitive inhibitor of isoform PanK3 with respect to ATP1 and a mixed-type inhibitor with respect to pantothenate
Arachidonoyl-CoA
-
-
ATP
-
free form
ATP
Q5JHF1
substrate inhibition
chloranil
Q9H999
-
CoA
-
strong
CoA
-
not reversible by D-carnitine, acetyl-L-carnitine or other carnitine analogs; reversible by L-carnitine
CoA
-
feed-back inhibition; in vitro; reversible by L-carnitine
CoA
-
in vitro; in vivo; kinetics
CoA
-
inhibits isoform A stronger than isoform B
CoA
-
feed-back inhibition, isoform PanK1alpha
CoA
-
feedback inhibition, inhibition kinetics of recombinant isozyme mPanK2
CoA
-
feedback inhibitor
CoA
P9WPA7
feedback inhibitor
CoA
-
IC50: 0.2 mM
CoA
-
competitive
CoA esters
-
feedback inhibition, inhibition kinetics of recombinant isozyme mPanK2
coenzyme A
P0A6I3
allosteric regulator, feedback inhibition
coenzyme A
-
feedback inhibition, regulatory function, isozyme PanK1beta, slight inhibition of isozyme PanK3
coenzyme A
-
feedback inhibition regulates pantothenol uptake. Furosemide reduces this inherent feedback inhibition by competing with coenzyme A for binding to pantothenate kinase, thereby increasing pantothenol uptake
D-pantothenate
-
substrate inhibition, above 0.5 mM
dehydroisoandrosterone
Q9H999
about 30% residual activity at 0.1 mM (isoform PanK3)
Dehydroisoandrosterone sulfate
Q9H999
; about 8% residual activity at 0.1 mM (isoform PanK3)
dephospho-CoA
-
not
diphosphate
-
-
ephedrine hydrochloride
Q9H999
-
-
estradiol
Q9H999
about 80% residual activity at 0.1 mM (isoform PanK3)
Estradiol sulfate
Q9H999
about 90% residual activity at 0.1 mM (isoform PanK3)
Estrone sulfate
Q9H999
about 50% residual activity at 0.1 mM (isoform PanK3)
Fusidic acid
Q9H999
-
glipizide
Q9H999
-
-
glyburide
Q9H999
-
GW5074
Q9H999
-
Hexachlorophene
Q9H999
-
L-Pantothenate
-
-
malonyl-CoA
-
-
malonyl-CoA
-
0.075 mM, complete inhibition of PAK I
malonyl-CoA
-
-
malonyl-CoA
-
-
malonyl-CoA
-
feedback inhibition, regulatory function, isozyme PanK3, slight inhibition of isozyme PanK1beta
malonyl-CoA
-
effective inhibitor
N-heptylpantothenamide
-
-
N-heptylpantothenamide
P0A6I3
competitive to pantothenate
N-heptylpantothenamide
-
IC50 is 0.0048 mM, potent growth inhibitory anti-metabolite
N-pentylpantothenamide
-
-
N-pentylpantothenamide
P0A6I3
competitive to pantothenate
N-pentylpantothenamide
-
IC50 is 0.0035 mM, has antimicrobial activity against Staphylococcus aureus
N-[1-(5-[[2-(4-chlorophenoxy)ethyl]sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl)ethyl]naphthalene-1-carboxamide
-
competitive inhibition
Octanoyl-CoA
-
-
oleoyl-CoA
-
-
palmitoyl-CoA
-
-
palmitoyl-CoA
-
-
palmitoyl-CoA
-
feedback inhibition, regulatory function, isozyme PanK3, mutant chimera PanK1beta-3-1beta, slight inhibition of mutant chimera PanK3-1beta-3
palmitoyl-CoA
-
strong inhibitor
pantetheine 4'-phosphate
-
strong
pantetheine 4'-phosphate
-
weak
pantetheine 4'-phosphate
-
not
pantothenamide, N-substituted
-
IC50 about 0.0004-0.0016 mM
-
pantothenic acid 4'-phosphate
-
-
pantothenol
-
competitive inhibition
pantothenoylcysteine 4'-phosphate
-
strong
pantothenoylcysteine 4'-phosphate
-
weak
pantothenyl alcohol
-
-
pioglitazone hydrochloride
Q9H999
-
-
pregnenolobe
Q9H999
about 92% residual activity at 0.1 mM (isoform PanK3)
-
pregnenolone sulfate
Q9H999
; about 10% residual activity at 0.1 mM (isoform PanK3)
propionyl-CoA
-
-
Psi-rhodomyrtoxin
Q9H999
-
-
Reactive Blue
Q9H999
-
-
Ro 41-0960
Q9H999
-
rosiglitazone
Q9H999
-
succinyl-CoA
-
-
tamoxifen
Q9H999
-
tolfenamic acid
Q9H999
-
tyrphostin AG 528
Q9H999
-
-
tyrphostin AG 808
Q9H999
-
-
WIN 62577
Q9H999
-
-
[2-[(3-chlorophenyl)sulfanyl]pyridin-4-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
-
mixed non-competitive inhibition
[2-[(3-chlorophenyl)sulfanyl]quinolin-4-yl](piperidin-1-yl)methanone
-
mixed non-competitive inhibition
[[2-[[4-(6-methylpyridin-2-yl)piperazin-1-yl]methyl]-4'-(trifluoromethoxy)biphenyl-4-yl]oxy]acetic acid
-
mixed non-competitive inhibition
MCC-555
Q9H999
MCC-555 inhibits all three isoforms with a rank order of PanK3 > PanK2 > PanK1b; MCC-555 inhibits all three isoforms with a rank order of PanK3 > PanK2 > PanK1b
-
additional information
-
not inhibitory: 3',5'-ADP; not inhibitory: CoASH, acetyl-CoA
-
additional information
-
no inhibition by 2,2'-dipyridyl, Ca2+, Cd2+, 3'-AMP, GTP, GDP, ITP, UTP; not inhibitory: 3',5'-ADP
-
additional information
-
not inhibitory: Mg2+, NADP+; not inhibitory: NAD+
-
additional information
-
not inhibitory: 3',5'-ADP; not inhibitory: cAMP, NADH, NADPH, CoA:glutathione disulfide; not inhibitory: NAD+
-
additional information
-
in vivo antiplasmodial activities of the inhibitor molecules, overview
-
additional information
-
no inhibition by (R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid and (S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid, structural features required for enzyme inhibition, overview
-
additional information
-
structural features required for enzyme inhibition, overview
-
additional information
-
no inhibition by (S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid, structural features required for enzyme inhibition, overview
-
additional information
-
no inhibition by (R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid, structural features required for enzyme inhibition, overview
-
additional information
P0A6I3
no inhibition by hopantenate
-
additional information
-
no inhibition by N-pentylpantothenamide, enzyme is not affected by CoA or acetyl-CoA
-
additional information
p37564
no inhibition by N-pentylpantothenamide, enzyme is not affected by CoA or acetyl-CoA
-
additional information
-
structural determinants for feedback inhibition
-
additional information
-
no feedback regulation by CoA or acetyl-CoA
-
additional information
-
feedback inhibition by acyl-CoAs
-
additional information
Q81VX4
the enzyme is not subject to feedback inhibition by CoASH
-
additional information
-
not inhibited by CoA or its thioesters
-
additional information
-
inhibition by CoA thioesters
-
additional information
Q9H999
isoform PanK3 is not inhibited by estrone
-
additional information
Q5JHF1
feedback inhibition by CoA/acetyl-CoA and product inhibition by 4'-phosphopantothenate are not observed
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Acyl carrier protein
-
PAK II: inhibition, PAK I: stimulation between 0.015-0.035 mM
cholesterol
Q9H999
about 125% activity at 0.1 mM
CoA
-
stimulates
dithiothreitol
-
activation
O-oleoylcarnitine
Q9H999
140% activation at 0.1 mM
-
O-palmitoylcarnitine
Q9H999
120% activation at 0.1 mM
oleoylethanolamide
Q9H999
120% activation at 0.1 mM
palmitoylcarnitine
-
activates; the enzymatic activity of PanK2 is stimulated to the highest level by 0.008 mM palmitoylcarnitine
palmitoylcarnitine
-
activates
tamoxifen
Q9H999
140% activation at 0.1 mM
glyburide
Q9H999
; isoform PanK1b is activated by glyburide
additional information
-
no activation by L-carnitine
-
additional information
-
enzyme is not affected by CoA or acetyl-CoA
-
additional information
p37564
enzyme is not affected by CoA or acetyl-CoA
-
additional information
-
no feedback regulation by CoA or acetyl-CoA
-
additional information
-
carnitine and octanoylcarnitine do not have any effect on the PanK2 activity
-
additional information
Q9H999
isoform PanK3 is not activated by 1,4-naphthoquinone and phenylmercuric acid
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0057
(R)-pantothenate
-
recombinant isozyme PanK1beta, pH 7.0, 37C
0.009
(R)-pantothenate
-
recombinant isozyme iPanK2, pH 7.5, 37C
0.0095
(R)-pantothenate
-
recombinant isozyme PanK3, pH 7.0, 37C
0.014
(R)-pantothenate
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.023
(R)-pantothenate
-
pH 7.5, 37C, recombinant enzyme
0.025
(R)-pantothenate
-
recombinant isozyme mPanK2, pH 7.5, 37C
0.041
(R)-pantothenate
P0A6I3
pH 7.5, 37C, recombinant His-tagged enzyme
0.043
(R)-pantothenate
-
in 100 mM HEPES, pH 7.6, 20 mM KCl, 10 mM MgCl2, 2 mM phosphoenolpyruvate, 0.3 mM NADH, 5 units of lactate dehydrogenase, 2.5 units of pyruvate kinase, and 0.00027 mM of the PanK-III protein, at 50C
0.101
(R)-pantothenate
p37564
pH 7.6, 25C
0.168
(R)-pantothenate
-
pH 7.6, 25C
0.034
ATP
-
pH 7.5, 37C, recombinant enzyme
0.035
ATP
-
pH 6.5, 37C
0.05
ATP
-
25C, pH 7.8, determined by isothermal titration calorimetry
0.064
ATP
-
recombinant isozyme mPanK2, pH 7.5, 37C
0.068
ATP
-
recombinant isozyme iPanK2, pH 7.5, 37C
0.087
ATP
-
recombinant isozyme PanK1beta, pH 7.0, 37C
0.093
ATP
-
pH 7.5, 25C
0.099
ATP
Q6L2I5
-
0.112
ATP
-
recombinant isozyme PanK3, pH 7.0, 37C
0.115
ATP
-
Tris-HCl buffer, pH 8.0
0.151
ATP
-
Tris-HCl buffer, pH8.0
0.311
ATP
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.375
ATP
-
25C, pH 7.8, determined from coupled assay
0.406
ATP
-
citrate buffer, pH 6.0
0.51
ATP
-
-
0.616
ATP
-
citrate buffer, pH6.0
0.616
ATP
-
in citrate buffer, pH 6.5, temperature not specified in the publication
3.05
ATP
-
pH 7.6, 25C
6.04
ATP
-
in 100 mM HEPES, pH 7.6, 20 mM KCl, 10 mM MgCl2, 2 mM phosphoenolpyruvate, 0.3 mM NADH, 5 units of lactate dehydrogenase, 2.5 units of pyruvate kinase, and 0.00027 mM of the PanK-III protein, at 50C
9.59
ATP
p37564
pH 7.6, 25C
1.759
CTP
-
-
0.138
dATP
-
-
0.839
dCTP
-
-
0.117
dGTP
-
-
0.723
dTTP
-
-
668
GTP
-
in citrate buffer, pH 6.5, temperature not specified in the publication
0.225
MgATP2-
-
pH 7.4, 25C
0.6
MgATP2-
-
pH 7.0, 37C
1
MgATP2-
-
pH 6.1, 37C
0.008
N-heptylpantothenamide
-
pH 7.5, 37C, recombinant enzyme
0.124
N-heptylpantothenamide
P0A6I3
pH 7.5, 37C, recombinant His-tagged enzyme
0.003
N-pentylpantothenamide
-
pH 7.5, 37C, recombinant enzyme
0.14
N-pentylpantothenamide
P0A6I3
pH 7.5, 37C, recombinant His-tagged enzyme
0.009
pantothenate
-
-
0.011
pantothenate
-
pH 6.1, 37C
0.016
pantothenate
-
pH 6.1, 37C
0.018
pantothenate
-
pH 7.0, 37C
0.027
pantothenate
-
pH 7.5, 25C
0.067
pantothenate
-
pH 6.5, 37C
0.093
pantothenate
-
-
0.1
pantothenate
-
25C, pH 7.8, determined from coupled assay
0.136
pantothenate
-
-
0.18
pantothenate
-
25C, pH 7.8, determined by isothermal titration calorimetry
0.621
pantothenate
Q6L2I5
-
0.8
pantothenate
-
isoform 2, 37C, pH 8.0
1.3
pantothenate
-
isoform 1, 37C, pH 8.0
0.25
pantothenol
-
25C, pH 7.8, determined by isothermal titration calorimetry
0.28
pantothenol
-
25C, pH 7.8, determined from coupled assay
1.715
UTP
-
-
1
MgATP2-
-
pH 6.5, 37C
additional information
additional information
-
kinetics of recombinant isozyme mPanK2
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.29
(R)-pantothenate
-
in 100 mM HEPES, pH 7.6, 20 mM KCl, 10 mM MgCl2, 2 mM phosphoenolpyruvate, 0.3 mM NADH, 5 units of lactate dehydrogenase, 2.5 units of pyruvate kinase, and 0.00027 mM of the PanK-III protein, at 50C
1.7
(R)-pantothenate
-
pH 7.5, 37C, recombinant enzyme
2.09
(R)-pantothenate
p37564
pH 7.6, 25C
2.12
(R)-pantothenate
-
pH 7.6, 25C
0.052
ATP
-
citrate buffer, pH6.0
0.052
ATP
-
in citrate buffer, pH 6.5, temperature not specified in the publication
0.071
ATP
-
citrate buffer, pH 6.0
0.411
ATP
-
Tris-HCl buffer, pH8.0
0.62
ATP
-
25C, pH 7.8, determined from coupled assay
0.65
ATP
-
25C, pH 7.8, determined by isothermal titration calorimetry
0.718
ATP
Q6L2I5
-
1.14
ATP
-
Tris-HCl buffer, pH 8.0
1.6
ATP
-
pH 7.5, 37C, recombinant enzyme
2.09
ATP
p37564
pH 7.6, 25C
2.12
ATP
-
pH 7.6, 25C
0.9
dATP
-
-
0.5
dCTP
-
-
0.8
dGTP
-
-
0.4
dTTP
-
-
0.064
GTP
-
in citrate buffer, pH 6.5, temperature not specified in the publication
0.425
N-heptylpantothenamide
-
pH 7.5, 37C, recombinant enzyme
0.15
N-pentylpantothenamide
-
pH 7.5, 37C, recombinant enzyme
0.61
pantothenate
-
25C, pH 7.8, determined from coupled assay
0.62
pantothenate
-
25C, pH 7.8, determined by isothermal titration calorimetry
0.818
pantothenate
Q6L2I5
-
0.38
pantothenol
-
25C, pH 7.8, determined by isothermal titration calorimetry
0.4
pantothenol
-
25C, pH 7.8, determined from coupled assay
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
ATP
-
citrate buffer, pH6.0
4
0.084
ATP
-
in citrate buffer, pH 6.5, temperature not specified in the publication
4
0.17
ATP
-
citrate buffer, pH 6.0
4
2.72
ATP
-
Tris-HCl buffer, pH8.0
4
2.9
ATP
-
-
4
9.91
ATP
-
Tris-HCl buffer, pH 8.0
4
0.9
CTP
-
-
60
6.6
dATP
-
-
140
0.6
dCTP
-
-
179
6.5
dGTP
-
-
219
0.5
dTTP
-
-
145
0.095
GTP
-
in citrate buffer, pH 6.5, temperature not specified in the publication
37
1
UTP
-
-
65
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.138
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazide
-
37C, versus pantothenate at 1 mM
0.2
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazide
-
37C, versus pantothenate at 1 mM
0.013
(2R)-2,4-dihydroxy-3,3-dimethylbutanohydrazide
-
37C, versus pantothenate at 1 mM
0.0019
(2R)-2,4-dihydroxy-N-(2-hydroxyethyl)-3,3-dimethylbutanamide
-
37C, versus pantothenate at 1 mM
4
(2R)-N-(2,3-dihydroxypropyl)-2,4-dihydroxy-3,3-dimethylbutanamide
-
37C, versus pantothenate at 1 mM
0.082
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamide
-
37C, versus pantothenate at 1 mM
1
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamide
-
37C, versus pantothenate at 1 mM
0.162
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramide
-
37C, versus pantothenate at 1 mM
0.112
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramide
-
37C, versus pantothenate at 1 mM
0.111
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramide
-
37C, versus pantothenate at 1 mM
0.076
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramide
-
37C, versus pantothenate at 1 mM
0.109
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramide
-
37C, versus pantothenate at 1 mM
0.164
5'-deoxy-5'-(4-(beta-D-galactopyranosyloxymethyl)-1,2,3-triazol-1-yl)adenosine
-
-
0.033
CoA
-
reduced form, pH 6.5, 37C
0.067
CoA
-
oxidized form, pH 6.5, 37C
0.037
pantetheine 4'-phosphate
-
pH 6.5, 37C
0.125
pantothenic acid 4'-phosphate
-
pH 6.5, 37C
0.129
pantothenol
-
37C, versus pantothenate at 1 mM
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0084
1,4-dioxa-8-azaspiro[4.5]dec-8-yl[2-[(3-fluorophenyl)sulfanyl]pyridin-4-yl]methanone
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25C
0.0004
1,4-phenylene-bis(1,2-ethanediyl)bis-isothiourea dihydrobromide
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.00257
2-[2-(1-benzoylpiperidin-4-yl)-5-methyl-1,3-thiazol-4-yl]-N-(4-methylphenyl)acetamide
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25C
0.05 - 0.15
4-(2,4-dihydroxy-3,3-dimethylbutylamido)butyric acid
-
competitive inhibitor, IC50: 0.05-0.15 mM
0.00006
acetyl-CoA
-
IC50: 60 nM, competitive inhibitor with respect to ATP
0.0000625
acetyl-CoA
-
-
0.000125
acetyl-CoA
-
-
0.0059
chloranil
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.2
CoA
-
IC50: 0.2 mM
0.0035
Dehydroisoandrosterone sulfate
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.0016
ephedrine hydrochloride
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.0001
Fusidic acid
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.0052
glipizide
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.0068
glyburide
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.0092
GW5074
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.0088
Hexachlorophene
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.0048
N-heptylpantothenamide
-
IC50 is 0.0048 mM, potent growth inhibitory anti-metabolite
0.0035
N-pentylpantothenamide
-
IC50 is 0.0035 mM, has antimicrobial activity against Staphylococcus aureus
0.00007
N-[1-(5-[[2-(4-chlorophenoxy)ethyl]sulfanyl]-4-methyl-4H-1,2,4-triazol-3-yl)ethyl]naphthalene-1-carboxamide
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25C
0.0004 - 0.0016
pantothenamide, N-substituted
-
IC50 about 0.0004-0.0016 mM
-
0.001
pioglitazone hydrochloride
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.0025
pregnenolone sulfate
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.0016
Psi-rhodomyrtoxin
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.0013
Reactive Blue
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.0039
Ro 41-0960
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.0017
rosiglitazone
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.0092
tolfenamic acid
Q9H999
isoform PanK3, at pH 7.5 and 37C
0.003
tyrphostin AG 528
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.009
tyrphostin AG 808
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.0007
WIN 62577
Q9H999
isoform PanK3, at pH 7.5 and 37C
-
0.00024
[2-[(3-chlorophenyl)sulfanyl]pyridin-4-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25C
0.00042
[2-[(3-chlorophenyl)sulfanyl]pyridin-4-yl][4-(hydroxymethyl)piperidin-1-yl]methanone
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25C
0.00087
[2-[(3-chlorophenyl)sulfanyl]quinolin-4-yl](piperidin-1-yl)methanone
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25C
0.00082
[[2-[[4-(6-methylpyridin-2-yl)piperazin-1-yl]methyl]-4'-(trifluoromethoxy)biphenyl-4-yl]oxy]acetic acid
-
in 50 mM PIPES-NaOH (pH 7.0), 25 mM KCl, 20 mM MgCl, at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0002421
-
0.045 mM pantothenate, 0.25 mM ATP (pH 7.0), 10 mM MgCl2, 0.1 M Tris/HCl (pH 7.5), at 37C
0.0012
-
pH 6.1, 37C
0.00171
-
pH 7.0, 37C
0.0041
-
pH 6.1, 37C
0.034
-
pH 6.5, 37C
0.152
-
isoform 1, 37C, pH 8.0
0.36
Q6L2I5
purified recombinant protein
additional information
-
-
additional information
-
specific activity in various tissues per mg wet weight
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.9 - 6.3
-
-
6 - 9
-
broad, highest activity in 50 mM phosphate buffer
7
-
assay at
7.5
-
assay at
7.6
-
assay at
7.6
p37564
assay at
8
Q5JHF1
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 6
Q6L2I5
more than 70% of the maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
-
assay at
25
-
assay at
25
p37564
assay at
37
P0A6I3
assay at
37
-
assay at
37
-
assay at
75
Q5JHF1
assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15
D2K764
the enzyme has no activity at temperatures below 15C
30 - 42
-
-
50 - 70
Q6L2I5
more than 80% of the maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.1
-
isoelectric focusing, isoform B
5.7
-
isoelectric focusing, isoform A
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
subtissue distribution of several isoforms of PanK2, overview
Manually annotated by BRENDA team
-
expression of PanK2 is higher in human brain compared to mouse brain
Manually annotated by BRENDA team
-
in most cases of pantothenate kinase-associated neurodegeneration, abnormalities are restricted to globus pallidus and substantia nigra
Manually annotated by BRENDA team
-
of a 40 years old gorilla, suffering during the last 2 years of life from progressive tetraparesis, nystagmus, and dyskinesia of the arms, hands and neck, with accompanying abnormal behavior. Sequencing of the PANK2 gene fails to detect any mutation
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
ventricular muscle
Manually annotated by BRENDA team
-
mainly isoform mPanK1alpha
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
ventricular muscle
-
Manually annotated by BRENDA team
-
both isoforms
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
-
mainly isoform mPanK1beta
Manually annotated by BRENDA team
-
chemical knockout of pantothenate kinase reveals the metabolic and genetic program responsible for hepatic coenzyme A homeostasis
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
additional information
-
distribution in different tissues
Manually annotated by BRENDA team
additional information
-
naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease
Manually annotated by BRENDA team
additional information
Rattus norvegicus Sprague-Dawley
-
distribution in different tissues
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Rattus norvegicus Sprague-Dawley
-
-
-
Manually annotated by BRENDA team
Q9BZ23
PANK2 contains a mitochondrial targeting signal
Manually annotated by BRENDA team
-
several isoforms of brain PanK2
Manually annotated by BRENDA team
-
PanK2 is located in the mitochondria to sense the levels of palmitoylcarnitine and up-regulate CoA biosynthesis in response to an increased mitochondrial demand for the cofactor to support beta-oxidation
Manually annotated by BRENDA team
-
one of the splicing isoforms localizes to mitochondria
Manually annotated by BRENDA team
additional information
-
multiple subcellular distribution of multiple enzyme forms
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Klebsiella pneumoniae (strain 342)
Klebsiella pneumoniae (strain 342)
Klebsiella pneumoniae (strain 342)
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
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)
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)
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)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MSSA476)
Staphylococcus aureus (strain MW2)
Staphylococcus aureus (strain MW2)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
-
SDS-PAGE
671767
36300
-
calculated from sequence of cDNA
671767
45000
-
gel filtration
641389
48000
-
SDS-PAGE, mature protein
671347
59000
-
recombinant enzyme, gel filtration
662408
99600
-
calculated from amino acid sequence
676548
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 29100, recombinant enzyme, six-His-tagged
?
O93921
x * 46900, deduced from gene sequence
?
-
x * 53000, SDS-PAGE, x * 56700, deduced from gene sequence
?
D2K764
x * 36800, SDS-PAGE, x * 52000, recombinant enzyme, SDS-PAGE
?
-
x * 52000, recombinant enzyme, SDS-PAGE
?
-
x * 37500, recombinant enzyme, SDS-PAGE
?
-
x * 48000, recombinant His/myc-tagged isozyme PanK2, SDS-PAGE, x * 63000, recombinant unprocessed PanK2, SDS-PAGE
?
Q6L2I5
x * 33000 Da, SDS-PAGE
?
-
x * 37500, recombinant enzyme, SDS-PAGE
-
?
-
x * 36800, SDS-PAGE, x * 52000, recombinant enzyme, SDS-PAGE
-
dimer
-
crystal structure
dimer
Q6G7I0
x-ray crystallography
dimer
Q9HWC1
x-ray crystallography
dimer
-
2 * 29000, recombinant enzyme, SDS-PAGE
dimer
-
2 * 41100, isozyme Pank3, sequence calculation and gel filtration, 2 * 41600, isozyme Pank1beta, sequence calculation and gel filtration
dimer
-
molecular mass, 30.8-61.2 kDa, of diverse protein variants expressed from different plasmids in different systems, SDS-PAGE and gel filtration, overview
dimer
-
gel filtration, functional unit in solution
dimer
Staphylococcus aureus RN4220
-
2 * 29000, recombinant enzyme, SDS-PAGE
-
hexamer
-
X-ray crystallography, in the crystal form
homodimer
-
2 * 36000, SDS-PAGE
monomer
Q81VX4
x-ray crystallography
additional information
P0A6I3
formation of a pantothenate kinase-ADP-pantothenate ternary complex, structure determination, pantothenate binding to the enzyme induces a significant conformational change in amino acids 243263, which form a lid that folds over the open pantothenate binding groove
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
-
several isoforms of PanK2 are produced by sequential proteolytic cleavage, identification of cleavage sites for the mitochondrial processing peptidase, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting-drop method. The crystal structure of Bacillus anthracis PanK is solved using multiwavelength anomalous dispersion data and refined at a resolution of 2.0 A; sitting drop vapour diffusion method using 24-26% ethylene glycol
Q81VX4
purified recombinant enzyme in a ternary complex with ADP and pantothenate, hanging drop vapour diffusion method, 30 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 1 mM DTT, 1 mM EDTA, incubated overnight with 30 mM ADP, 30 mM pantothenate, and 30 mM magnesium nitrate, mixing in equal volumes with reservoir solution containing 11% PEG 3350, 0.2 M sodium citrate, pH 8.2, at 18C, 1 week, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular modeling of N-alkylpantothenamides, growth-inhibitory anti-metabolites
P0A6I3
sitting drop vapor diffusion method at 18C, homodimeric structures of the catalytic core of PanK1alpha in complex with acetyl-CoA. Crystallographic mapping of missense mutations associated with pantothenate kinase-associated neurodegeneration disease; sitting drop vapor diffusion method at 18C, homodimeric structures of the catalytic core of PanK3 in complex with acetyl-CoA. Crystallographic mapping of missense mutations associated with pantothenate kinase-associated neurodegeneration disease
Q8TE04, Q9H999
bound to oantothenate, pantothenol or N-nonylpantothenamide, using 1.4-1.8 M trisodium citrate, 0.05-0.1 M sodium acetate and 10% (v/v) glycerol at pH 6.5
-
complexes of the enzyme with guanosine-5'-[(beta,gamma)-methyleno]triphosphate and pantothenate, GDP and phosphopantothenate, GDP, GDP and pantothenate, 5'-adenylyl (beta,gamma-methylene)diphosphonate, and guanosine-5'-[(beta,gamma)-methyleno]triphosphate, hanging drop vapor diffusion method, using 1.4-1.8 M trisodium citrate, 0.05-0.1 M sodium acetate, and 10% (v/v) glycerol at pH 6.5
-
hanging drop vapour diffusion method using 10-15% (w/v) PEG 8000, 0.05-0.1 M NaOAc and 0.05 M NaCl dissolved in 0.1 M sodium cacodylate buffer pH 6.5
P9WPA7
purified recombinant His-tagged enzyme, hanging drop vapour diffusion method, 0.003 ml protein solution containing 6 mg/ml protein, 0.1 M Tris-HCl, pH 8.0, 0.15 M NaCl, 5% v/v glycerol and 0.001 M 2-mercaptoethanol, mixed 0.001 ml of precipitant solution containing 10-15% w/v PEG 8000, 0.05-0.1 M NaOAc, 0.05 NaCl, and 0.1 M cacodylate, pH 6.5, room temperature, equilibration against 0.4 ml precipitant solution, 3-7 days, 2 different crystal forms, X-ray diffraction structure determination and analysis at 2.5 A and 2.9 A resolution, respectively, molecular replacement calculations
-
hanging drop vapour diffusion method using 28% (w/v) PEG 2000 mM and 0.1M Bis-Tris (pH 6.5), at 18C
Q9HWC1
sitting drop vapour diffusion method using 28% (w/v) PEG 2 M and 0.1 M Bis-Tris (pH 6.5), at 18C
Q6G7I0
hanging drop vapor-diffusion method, crystal structures of PanK-III in complex with pantothenate, phosphopantothenate as well as a ternary complex structure of PanK-III with pantothenate and ADP
Q9WZY5
sitting drop vapour diffusion method with 15% polyethylene glycol 3350
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
-
t1/2: 10 min at 30C
641389
7
-
10 min stable at 30C
641389
7.5
-
90% of activity retained after 10 min at 30C
641389
8
-
80% of activity retained after 10 min at 30C
641389
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
10% to 20% loss of activity within 10 min at pH 7.5 to 8, 10 min stable at pH 7, t1/2: 10 min at pH 6.5
641389
37
-
10 min, 70% loss of activity
641389
43
-
10 min, inactivation
641389
47
-
loses kinase activity at temperatures higher than 47C
671767
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
ATP and/or sucrose do not stabilize
-
ATP and/or sucrose stabilize during purification
-
considerably unstable independent of the degree of purity
-
highly unstable upon purification, e.g. successive chromatography
-
thiol reducing agents stabilize enzyme in solution
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, 2 mg protein/ml in 0.01 M phosphate buffer, pH 7, inactivation within 4 days
-
-20C, partially purified preparation, several months
-
-20C, above 3 mg protein/ml, more than 1 week
-
-65C, 3 mg partially purified protein/ml, at least 4 months
-
4C, above 3 mg protein/ml, 4 days
-
4C, t1/2: 3 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; Ni-NTA column chromatography
Q81VX4
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
Ni-column chromatography
-
recombinant enzyme from strain BL21(DE3) by ion exchange and hydrophobic interaction chromatography, and gel filtration, recombinant His-tagged enzyme from strain BL21(DE3) by nickel affinity chromatography
P0A6I3
strain SJ16, partial
-
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
p37564
;
Q8TE04, Q9H999
His-tagged PanK2; HiTrap chelating HP column chromatography and Superdex 200 column gel filtration
-
native enzyme partially by preparation of mitochondria
Q9BZ23
recombinant His/myc-tagged isozyme PanK2 from mitochondria of QBI 293 cells by ion exchange and protein A affinity chromatography and gel filtration
-
Ni-NTA column chromatography
-
Ni-NTA column chromatography and Superdex pg 200 gel filtration
-
Ni-NTA metal affinity column chromatography
P9WPA7
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
liver; partial
-
partial, presumably 2 isoforms
-
recombinant enzyme, six-His-tagged
-
recombinant His6-tagged from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
immobilized Co2+-affinity chromatography
D2K764
nickel-nitrilotriacetic acid-agarose column chromatography and Resource Q column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; expressed in Escherichia coli strain C41(DE3)
Q81VX4
gene coaX, gene cluster analysis, DNA and amino acid sequence determination and analysis, overexpression of N-terminally His6-tagged in Escherichia coli strain BL21(DE3)
-
gene coaA, expression in strain BL21(DE3)
P0A6I3
His-tag, expressed in Escherichia coli BL21 (DE3)
-
gene coaX, gene cluster analysis, DNA and amino acid sequence determination and analysis, overexpression of N-terminally His6-tagged in Escherichia coli strain BL21(DE3)
p37564
; expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain ts9
-
expression as a His-tagged fusion protein in Escherichia coli; expression as a His-tagged fusion protein in Escherichia coli
Q8TE04, Q9H999
expression of wild-type His/myc-tagged isozyme PanK2 and of mutant enzymes in mitochondria of QBI 293 cells
-
PANK2, 2 translational strat sites, CAG and CUG initiation codons, expression of PANK2 as EGFP-tagged protein in HeLa cell mitochondria, and in COS-7 cells as His/myc-tagged enzyme
Q9BZ23
splice variant PanK2, expression of active PanK2 isozymes iPanK2, spPanK2, mPanK2 in HEK293T cells, in vitro transcription and translation of PanK2
-
; expression in HEK-293T cells
-
DNA and amino acid sequence determination and analysis of isozymes PanK3 and PanK1beta, overexpression of wild-type isozymes PanK3 and PanK1beta and chimeric mutants thereof in HEK293T cells
-
DNA and amino acid sequence determination and analysis, expression of the His-tagged in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21 (DE3) cells
P9WPA7
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli DV62 and BL21(DE3) cells
-
expressed in Escherichia coli
Q6L2I5
expressed in Escherichia coli
Q923S8
gene coaA, expression of His6-tagged in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli BL21(DE3) cells
D2K764
the TK2141 gene encoding PoK, with a His6-Tag on its N-terminus, is overexpressed in Thermococcus kodakarensis
Q5JHF1
expressed in Escherichia coli strain BL21(DE3)
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F247V
-
less than 50% of catalytic activity of wild type, feedback resistant
H177Q
-
less than 50% of catalytic activity of wild type, feedback resistant
L236F
-
temperature-sensitive mutant, inactive above 39C
R106A
-
50% of catalytic activity of wild type, feedback resistant
R315C
-
temperature-sensitive mutant, inactive above 39C
S176L
-
temperature-sensitive mutant, inactive above 39C
A267F
Q9H999
catalytically inactive
A269F
Q9H999
catalytically inactive
A509V
-
naturally occurring mutation, early onset in patients, 105% activity compared to the wild-type enzyme
E134G
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
G219V
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
G219V
-
naturally occurring mutation, early and late onset in patients, 0.4% activity compared to the wild-type enzyme
G521R
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
G521R
-
the splice variant PanK2 naturally contains mutation which is associated with neurodegenerative disease in brain, early and late onset in patients, less than 0.2% activity compared to the wild-type enzyme
G521R
-
loss of enzyme activity
N404I
-
naturally occurring mutation, early and late onset in patients, 83% activity compared to the wild-type enzyme
N500I
-
naturally occurring mutation, early onset in patients, 3.9% activity compared to the wild-type enzyme
R207A
Q9H999
catalytically inactive
R264W
-
naturally occurring mutation, early onset in patients, 58% activity compared to the wild-type enzyme
R286C
-
naturally occurring mutation, early and late onset in patients, 176% activity compared to the wild-type enzyme
R532W
-
naturally occurring mutation, early onset in patients, 95% activity compared to the wild-type enzyme
S195V
Q9H999
the mutant is insensitive to acetyl-CoA and has a KM defect for pantothenate
S351P
-
naturally occurring mutation, early and late onset in patients, 78% activity compared to the wild-type enzyme
S471N
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
T234A
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
T234A
-
naturally occurring mutation, early and late onset in patients, 112% activity compared to the wild-type enzyme
T327I
-
naturally occurring mutation, early onset in patients, 91% activity compared to the wild-type enzyme
T528M
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
T528M
-
naturally occurring mutation, early and late onset in patients, 146% activity compared to the wild-type enzyme
D101A
Q9HWC1
reduced enzymatic activity
D121A
Q9HWC1
reduced enzymatic activity
H156A
Q9HWC1
slightly increased enzymatic activity
K13A
Q9HWC1
reduced enzymatic activity
N9G
Q9HWC1
strongly reduced enzymatic activity
T157A
Q9HWC1
reduced enzymatic activity
G351S
-
temperature-sensitive phenotype
D6A
Q6G7I0
reduced enzymatic activity
E70A
Q6G7I0
reduced enzymatic activity
K13A
Q6G7I0
reduced enzymatic activity
L11A
Q6G7I0
reduced enzymatic activity
L263P
Q6G7I0
reduced enzymatic activity
T10A
Q6G7I0
reduced enzymatic activity
Y137A
Q6G7I0
reduced enzymatic activity
D105E
-
less than 6% activity of the wild type enzyme
D105N
-
less than 6% activity of the wild type enzyme
D125E
-
less than 6% activity of the wild type enzyme
D125N
-
less than 6% activity of the wild type enzyme
D6E
-
less than 6% activity of the wild type enzyme
D6N
-
less than 6% activity of the wild type enzyme
K224A
-
site-directed mutagenesis, less than 0.2% activity compared to the wild-type enzyme
additional information
Q9BZ23
an allelic variant mislocates and thereby causes disease
additional information
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identification of naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease, identification of other disease related point mutations which lead to reduced enzyme activity, mutations alter processing, stability, and catalytic activity of the mutant PanK2
additional information
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several natural mutants with frame shifts show no activity, identification of mutants with mutations which introduce stop codons, overview
additional information
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two siblings with the adult-onset slowly progressive type of pantothenate kinase-associated neurodegeneration have the I346S mutation in pantothenate kinase-2
T528M
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no effect on PANK2 activity or stability
additional information
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construction of chimeric mutant enzymes PanK1beta-3-1beta and PanK3-1beta-3 by combination of isozymes PanK3 and PanK1beta, mutant show different sensitivity to feedback inhibitors compared to the wild-type isozymes, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
Q839J7
synthesis of (carboxyl-18O)phosphopantothenate
medicine
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a young girl with early onset pantothenate kinase-associated neurodegeneration whose initial clinical manifestation is ataxia at the age of 2.5 years and refractory severe dystonia resulting in essentially complete loss of motor control. She has a mutation in PANK2 gene consisting of an amino acid change of alanine to valine in exon 5 (A382V). After Globus Pallidus deep brain stimulation at the age of 11 years, the patient regains useful motor function and speech with a marked decrease in the severity of the dystonia
medicine
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neurodegeneration with brain iron accumulation is a heterogenous group of disorder. One group of patiens bears mutations in the gene encoding pantothenate kinase 2
medicine
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pallidal stimulation for dystonia in pantothenate kinase associated neurodegeneration
medicine
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pantothenate kinase associated neurodegeneration is an autosomal recessive disorder characterized by dystonia, parkinsonism, and iron accumulation in the brain. Many patients have a mutation in the gene encoding pantothenate kinase 2 which is a key regulator enzyme in the biosynthesis of coenzyme A
medicine
-
pantothenate kinase-associated neurodegeneration (formerly Hallervorden-Spatz syndrome), the most prevalent form of neurodegeneration with brain iron accumulation, is a rare degenerative brain disease characterised by predominantly extrapyramidal dysfunction resulting from mutations in the PANK2 (pantothenate kinase 2) gene. A novel missense mutation (P354L) in exon 4 of the PANK2 gene is identified in an adolescent with classic pantothenate kinase-associated neurodegeneration. DNA-based diagnosis of pantothenate kinase-associated neurodegeneration plays a key role in determination, and can make the diagnosis more simply, directly, and economically because it obviates the need for unnecessary biochemical tests. Once pantothenate kinase-associated neurodegeneration-like symptoms are identified, mutation analysis and target screening for the family of the proband can provide efficient and accurate evidence of pantothenate kinase-associated neurodegeneration inheritance
medicine
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pantothenate kinase-associated neurodegeneration is a neurodegenerative condition with a broad phenotypic spectrum
medicine
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pantothenate kinase-associated neurodegeneration is a progressive neurodegenerative disorder with autosomal recessive inheritance. The major symptoms of PKAN include the onset before the age of 20 years, progressive pyramidal and extrapyramidal signs, retinitis pigmentosa, optic atrophy, dementia, and iron depositions in the globus pallidus. Identification of mutations of PANK2 gene in patients with proven molecular diagnosis of pantothenate kinase-associated neurodegeneration
medicine
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pantothenate kinase-associated neurodegeneration is an autosomal-recessive disorder associated with the accumulation of iron in the basal ganglia. The disease presents with dystonia, rigidity, and gait impairment, leading to restriction of activities and loss of ambulation. The disorder is caused by defective iron metabolism associated with mutations in the PANK2 gene, which codes for the pantothenate kinase enzyme. A mutation screen conducted in two siblings to establish a molecular diagnosis of the disease and a genetic test for the family is reported
medicine
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pantothenate-kinase-associated neurodegeneration (PKAN) is caused by mutations of the pantothenate kinase (PANK2) on chromosome 20p13. PKAN is characterized clinically by extrapyramidal symptoms (in 98% of cases), in particular, generalized dystonia with oromandibular involvement, and parkinsonism-spasticity (25%), behavioral changes followed by dementia (29%), and pigmentary retinal degeneration. The mean age at onset is between 3 and 4 years, pantothenate-kinase-associated neurodegeneration is caused by mutations of the pantothenate kinase gene. Pantothenate-kinase-associated neurodegeneration is characterized clinically by extrapyramidal symptoms (in 98% of cases), in particular, generalized dystonia with oromandibular involvement, and parkinsonism-spasticity (25%), behavioral changes followed by dementia (29%), and pigmentary retinal degeneration. The mean age at onset is between 3 and 4 years
medicine
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patient with pantothenate kinase-associated neurodegeneration whose dystonia and freezing of gait respond dramatically to anticholinergic treatment
medicine
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the cognitive deterioration in pantothenate kinase-associated neurodegeneration dystonia has been overemphasised and many of the apparent disabilities are more a consequence of the dystonia
medicine
-
pantothenic acid deprivation provides a useful phenocopy for pantothenate kinase associated neurodegeneration (formerly called Hallervorden-Spatz syndrome) and allows us to test pharmacological and other interventional strategies in the treatment of this devastating disease
medicine
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the enzyme is a suitable target for therapeutic intervention in metabolic disorders that feature hyperglycemia and hypertriglyceridemia