Information on EC 2.7.1.33 - pantothenate kinase:
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EC NUMBERCOMMENTARY
2.7.1.33-

RECOMMENDED NAMEGeneOntology No.
pantothenate kinaseGO:0004594

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.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 mechanismStaphylococcus aureus-641398
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 kinaseEscherichia coliP0A6I3662251
ATP + (R)-pantothenate = ADP + (R)-4'-phosphopantothenate
show the reaction diagram		-Homo sapiens-662687

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
phospho group transfer----

PATHWAYKEGG LinkMetaCyc Link
phosphopantothenate biosynthesis I-PANTO-PWY
phosphopantothenate biosynthesis II-PWY-3961

SYSTEMATIC NAMEIUBMB Comments
ATP:(R)-pantothenate 4'-phosphotransferase-

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
BaPanKBacillus anthracisQ81VX4-672234
CoaAStaphylococcus aureus--662408, 677154, 686816
CoaAEscherichia coli--671767, 686816
CoaAPseudomonas aeruginosaQ9HWC1-677154
CoaAMycobacterium tuberculosis--686816
CoaXBacillus subtilis--662369
CoaXHelicobacter pylorip37564-662369
CoaXBacillus anthracis--687425
D-pantothenate kinase----
hPanK----
hPanK1----
hPANK2----
hPANK2Homo sapiens--686741
hPanK3----
hPanK4----
HpPanK-IIIHelicobacter pylori--685199
mPank----
mPank1----
mPanK2Mus musculus--686741
mPanK3----
MtCoaAMycobacterium tuberculosis--677979
PAK----
PanKMycobacterium tuberculosis--660631, 671053, 686816
PanKMus musculus--661331, 662406, 673027
PanKEscherichia coli--661331, 671053, 671767, 686816
PanKStaphylococcus aureus--661331, 686816
PanKEmericella nidulans--661331
PanKBacillus subtilis--662369
PanKHelicobacter pylorip37564-662369
PanKBacillus anthracisQ81VX4-672234
PanKPlasmodium falciparum--674852
PanKDrosophila sp.-the Drosophila genome encodes a single copy of PANK687036
PanKHomo sapiens--689010
PanKEnterococcus faecalisQ839J7-702284
PanK-IIIThermotoga maritima--674291
PanK1alphaHomo sapiensQ8TE04, Q9H999-687612
PanK2Homo sapiens--660712, 662455, 662687, 671347, 687016, 687943, 689128, 689334, 690019
PanK2Arabidopsis thaliana--676548
PanK2Homo sapiens-; 676884
PanK2Mus musculus--688176
PanK2Gorilla beringei--690187
PanK3Homo sapiensQ8TE04, Q9H999-687612
PanK4Rattus norvegicusQ923S8-675942
PanKBaBacillus anthracis--687425
pantothenate kinaseEscherichia coli, Mycobacterium tuberculosis--701469
pantothenate kinaseEnterococcus faecalisQ839J7-702284
pantothenate kinaseSaccharomyces cerevisiae--703325
pantothenate kinaseDrosophila melanogaster-5 splicing isoforms703958
pantothenate kinasePicrophilus torridusQ6L2I5-704326
pantothenate kinaseBacillus anthracis--706042
pantothenate kinase 2Homo sapiens--660712, 662455, 662687, 686741, 687016, 689128
pantothenate kinase 2Homo sapiens-; 676884
pantothenate kinase 2Mus musculus--686741, 688176
pantothenate kinase 4Rattus norvegicusQ923S8-675942
pantothenate kinase-2Homo sapiens--703958, 705271
pantothenic acid kinase----
rPanK4----
Rts protein ----
TmPanK-IIIThermotoga maritimaQ9WZY5-685199
type II pantothenate kinaseStaphylococcus aureusQ6G7I0-677154
type III pantothenate kinaseBacillus anthracis--672234, 687425
type III pantothenate kinaseThermotoga maritima--674291
type III pantothenate kinasePseudomonas aeruginosaQ9HWC1-677154
kinase, pantothenate (phosphorylating)----
additional informationBacillus subtilis-the enzyme forms a type III pantothenate kinase662369
additional informationHelicobacter pylorip37564the enzyme forms a type III pantothenate kinase662369

CAS REGISTRY NUMBERCOMMENTARY
9026-48-6-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Arabidopsis thalianaecotype Colombia-0676548--Manually annotated by BRENDA team
Bacillus anthracis-672234Q81VX4SwissProtManually annotated by BRENDA team
Bacillus anthracis-672234, 687425, 706042--Manually annotated by BRENDA team
Bacillus subtilisgene coaX662369--Manually annotated by BRENDA team
Brassica napus-641388--Manually annotated by BRENDA team
Corynebacterium ammoniagenes-641389--Manually annotated by BRENDA team
Drosophila melanogaster-703958--Manually annotated by BRENDA team
Drosophila melanogaster3 isoforms641401--Manually annotated by BRENDA team
Drosophila sp.-687036--Manually annotated by BRENDA team
Emericella nidulans-641402O93921SwissProtManually annotated by BRENDA team
Emericella nidulans-661331--Manually annotated by BRENDA team
Enterococcus faecalis-702284Q839J7UniProtManually annotated by BRENDA team
Escherichia coli-4406, 641396, 661331, 686816, 701469--Manually annotated by BRENDA team
Escherichia coli-641399, 671053P0A6I3UniprotManually annotated by BRENDA team
Escherichia coligene coaA662251P0A6I3UniprotManually annotated by BRENDA team
Escherichia coliK-12 strains UB 1005, SJ16, DV1641393--Manually annotated by BRENDA team
Escherichia coliK12 strain ts9671767--Manually annotated by BRENDA team
Gorilla beringei-690187--Manually annotated by BRENDA team
Helicobacter pylori-685199--Manually annotated by BRENDA team
Helicobacter pylorigene coaX662369p37564SwissProtManually annotated by BRENDA team
Homo sapiens-660726, 676884, 684227, 684736, 686546, 686741, 687016, 687943, 688202, 689010, 689108, 689128, 689193, 689334, 689335, 690019, 705271--Manually annotated by BRENDA team
Homo sapiens-671347, 676884, 689128, 703958Q9BZ23SwissProtManually annotated by BRENDA team
Homo sapiens-687612Q8TE04, Q9H999SwissProtManually annotated by BRENDA team
Homo sapiensmultiple genes, multiple enzyme forms662687--Manually annotated by BRENDA team
Homo sapienssplice variant pantothenate kinase 2, i.e. PanK2, contains mutation G521R, several isozymes e.g. iPanK2, spPanK2, mPanK2, overview662455--Manually annotated by BRENDA team
Homo sapiensthe 5' end of PANK2 gene, Hallervorden-Spatz syndrome, and a CpG island, complete sequence; enzyme form PANK2, 2 allelic variants660712Q9BZ23SwissProtManually annotated by BRENDA team
Lactobacillus plantarum-4406--Manually annotated by BRENDA team
Micrococcus luteus-4412--Manually annotated by BRENDA team
Morganella morganii-4406--Manually annotated by BRENDA team
Mus musculus-673027, 686741, 688176--Manually annotated by BRENDA team
Mus musculusisoforms mPanK1alpha, mPanK1beta641397, 641400Q8K4K6SwissProtManually annotated by BRENDA team
Mus musculusisozyme PanK1alpha661331--Manually annotated by BRENDA team
Mus musculusmale C57BL6/J mice, isozyme PanK3 and PanK1beta662406--Manually annotated by BRENDA team
Mycobacterium tuberculosis-677979, 701469P63810SwissProtManually annotated by BRENDA team
Mycobacterium tuberculosis-686816--Manually annotated by BRENDA team
Mycobacterium tuberculosisstrain H37Rv660631--Manually annotated by BRENDA team
Mycobacterium tuberculosisstrain H37Rv671053P63810SwissProtManually annotated by BRENDA team
no activity in Lactobacillus helveticus-4406--Manually annotated by BRENDA team
no activity in Neurospora crassa-4406--Manually annotated by BRENDA team
Orchesella cincta-688109--Manually annotated by BRENDA team
Picrophilus torridus-704326Q6L2I5UniProtManually annotated by BRENDA team
Plasmodium falciparum; strains 3D7 and FAF6674852--Manually annotated by BRENDA team
Plasmodium falciparumstrain 3D7660726--Manually annotated by BRENDA team
Pseudomonas aeruginosa-677154Q9HWC1UniprotManually annotated by BRENDA team
Rattus norvegicus-4406, 641394--Manually annotated by BRENDA team
Rattus norvegicus-675942Q923S8SwissProtManually annotated by BRENDA team
Rattus norvegicusmale Wistar641387--Manually annotated by BRENDA team
Rattus norvegicusmale Wistar; on normal or clofibrate enriched diet641390--Manually annotated by BRENDA team
Rattus norvegicusSprague-Dawley641391, 641392--Manually annotated by BRENDA team
Saccharomyces cerevisiae-4406, 703325--Manually annotated by BRENDA team
Spinacia oleraceaspinach641388--Manually annotated by BRENDA team
Staphylococcus aureus-641398, 661331, 686816--Manually annotated by BRENDA team
Staphylococcus aureus-677154Q6G7I0UniprotManually annotated by BRENDA team
Staphylococcus aureusstrain RN4220, gene coaA662408--Manually annotated by BRENDA team
Thermotoga maritima-674291--Manually annotated by BRENDA team
Thermotoga maritima-685199Q9WZY5UniprotManually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
malfunctionHomo sapiens-disease: pantothenate kinase-associated neurodegeneration703958
malfunctionHomo sapiens-pantothenate kinase-associated neurodegeneration, formerly known as Hallervorden-Spatz syndrome705271
additional informationDrosophila melanogaster-mitochondria-targeted human pantothenate kinase-2 is involved in pantothenate kinase-associated neurodegeneration703958

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Staphylococcus aureus--661331, 662408--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Staphylococcus aureusQ6G7I0-677154--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mus musculus--661331, 662406--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Escherichia coli--661331, 671053, 671767--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Homo sapiens--660726, 662687, 676884--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Emericella nidulans--661331--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Arabidopsis thaliana--676548--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Pseudomonas aeruginosaQ9HWC1-677154--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mycobacterium tuberculosisP63810-671053--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Plasmodium falciparum--660726, 674852--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Thermotoga maritima--674291--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Bacillus anthracisQ81VX4-672234--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Homo sapiensQ9BZ23-660712, 671347--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Helicobacter pylorip37564-662369--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicusQ923S8-675942--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Staphylococcus aureus-first step in coenzyme A biosynthesis661331, 662408--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Bacillus subtilis-first step in coenzyme A biosynthesis662369--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mus musculus, Escherichia coli-first step in coenzyme A biosynthesis661331--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Homo sapiens-first step in coenzyme A biosynthesis660726, 662455, 662687--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Emericella nidulans-first step in coenzyme A biosynthesis661331--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mycobacterium tuberculosis-first step in coenzyme A biosynthesis660631--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Plasmodium falciparum-first step in coenzyme A biosynthesis660726--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Helicobacter pylorip37564first step in coenzyme A biosynthesis662369--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mus musculus-first step in coenzyme A biosynthesis, regulatory function662406--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Escherichia coliP0A6I3first step in coenzyme A biosynthesis, the enzyme has a regulatory function in the pathway662251--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mycobacterium tuberculosis-i.e. vitamin B5660631--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Escherichia coliP0A6I3pantothenate 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, overview662251--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Bacillus subtilis-the enzyme is absolutely specific for ATP, no activity with CTP, GTP, UTP, or phosphoenolpyruvate as phosphoryl donors662369--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Homo sapiens-the phosphate binding loop of isozyme mPanK2 is the N-terminal motif DIGGT(S)XXK662455--?
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Bacillus anthracis-coaX is essential for growth of Bacillus anthracis687425--?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Lactobacillus plantarum--4406---
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Lactobacillus plantarum--4406-4406?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Staphylococcus aureus--641398--?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Escherichia coli--4406---
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Escherichia coli--4406-4406?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Escherichia coli--641396--?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus--4406, 641391---
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus--4406-4406?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus--641390-641390?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus--641391-641391?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus--641392-641392?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus--641394--?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Saccharomyces cerevisiae--4406---
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Saccharomyces cerevisiae--4406-4406?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Spinacia oleracea--641388---
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Spinacia oleracea--641388-641388?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Brassica napus--641388---
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Brassica napus--641388-641388?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Micrococcus luteus--4412--?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Morganella morganii--4406---
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Morganella morganii--4406-4406?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Corynebacterium ammoniagenes--641389-641389?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Mus musculusQ8K4K6-641397--?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Escherichia coli-poor phosphate donor: alpha,beta-methyleneadenosine 5'-triphosphate, transfers the gamma-phosphate of ATP to pantothenate641393-641393?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus-D-configuration of 2'-hydroxyl group in pantothenate molecule is essential for functional interaction with enzyme641387-641387?
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Escherichia coli-first and rate-controlling reaction of CoA-biosynthesis641393-641393-
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus-first and rate-controlling reaction of CoA-biosynthesis641387---
ATP + D-pantothenateADP + 4'-phosphopantothenate
show the reaction diagram		Homo sapiens--676884--?
ATP + D-pantothenateADP + 4'-phosphopantothenate
show the reaction diagram		Homo sapiensQ8TE04, Q9H999-687612--?
ATP + N-alkylpantothenamidesADP + ?
show the reaction diagram		Escherichia coliP0A6I3growth-inhibiting anti-metabolite, modeling into the active site structure662251--?
ATP + N-heptylpantothenamideADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram		Staphylococcus aureus--662408--?
ATP + N-heptylpantothenamideADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram		Escherichia coliP0A6I3-662251--?
ATP + N-heptylpantothenamideADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram		Staphylococcus aureus-substrate is converted to the inactive butyldethia-CoA analogue in the further downstream pathway leading to grwoth inhibition of the organism, overview662408--?
ATP + N-pentylpantothenamideADP + N-pentylpantothenamide 4-phosphate
show the reaction diagram		Staphylococcus aureus--662408--?
ATP + N-pentylpantothenamideADP + N-pentylpantothenamide 4-phosphate
show the reaction diagram		Escherichia coliP0A6I3-662251--?
ATP + pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Staphylococcus aureus, Escherichia coli--686816--?
ATP + pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Homo sapiens--686741--?
ATP + pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mycobacterium tuberculosis--686816--?
ATP + pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Escherichia coli-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 vivo686816--?
ATP + pantothenateADP + 4'-phosphopantothenate
show the reaction diagram		Mycobacterium tuberculosisP63810-677979--?
ATP + pantothenateADP + 4'-phosphopantothenate
show the reaction diagram		Homo sapiensQ8TE04, Q9H999pantothenate kinase catalyzes the first step in CoA biosynthesis687612--?
ATP + pantothenate?
show the reaction diagram		Helicobacter pylori--685199--?
ATP + pantothenateADP + (R)-4-phosphopantothenate
show the reaction diagram		Mus musculus--686741--?
ATP + pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Mycobacterium tuberculosis--686816--?
ATP + pantothenolADP + 4'-phosphopantothenol
show the reaction diagram		Mycobacterium tuberculosisP63810-677979--?
ATP + patothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Thermotoga maritimaQ9WZY5-685199--?
CTP + (R)-pantothenateCDP + (R)-4'-phosphopantothenate
show the reaction diagram		Helicobacter pylorip37564-662369--?
GTP + (R)-pantothenateGDP + (R)-4'-phosphopantothenate
show the reaction diagram		Helicobacter pylorip37564-662369--?
GTP + pantothenateGDP + D-4'-phosphopantothenate
show the reaction diagram		Corynebacterium ammoniagenes-phosphorylation at 28% the rate of ATP641389--?
GTP + pantothenateGDP + D-4'-phosphopantothenate
show the reaction diagram		Escherichia coli-phosphorylation at 20% the rate of ATP641393--?
pantetheine + ATPD-4'-phosphopantetheine + ADP
show the reaction diagram		Corynebacterium ammoniagenes--641389--?
panthenoylcysteine + ATPD-4'-phosphopanthenoylcysteine + ADP
show the reaction diagram		Corynebacterium ammoniagenes--641389--?
panthotenate + ATPphosphopantothenate + ADP
show the reaction diagram		Picrophilus torridusQ6L2I5relative activity with GTP: 81%, CTP: 68%, and UTP: 91.8%704326--?
pantothenate + ATP4'-phosphopantothenate + ADP
show the reaction diagram		Saccharomyces cerevisiae--703325--?
pantothenate + ATP4'-phosphopantothenate + ADP
show the reaction diagram		Bacillus anthracis--706042--?
pantothenate + ATPphosphopantothenate + ADP
show the reaction diagram		Escherichia coli, Mycobacterium tuberculosis--701469--?
pantothenate + ATPphosphopantothenate + ADP
show the reaction diagram		Enterococcus faecalisQ839J7-702284--?
pantothenate + CTP4'-phosphopantothenate + CDP
show the reaction diagram		Bacillus anthracis--706042--?
pantothenate + dATP4'-phosphopantothenate + dADP
show the reaction diagram		Bacillus anthracis--706042--?
pantothenate + dCTP4'-phosphopantothenate + dCDP
show the reaction diagram		Bacillus anthracis--706042--?
pantothenate + dGTP4'-phosphopantothenate + dGDP
show the reaction diagram		Bacillus anthracis--706042--?
pantothenate + dTTP4'-phosphopantothenate + dTDP
show the reaction diagram		Bacillus anthracis--706042--?
pantothenate + UTP4'-phosphopantothenate + UDP
show the reaction diagram		Bacillus anthracis--706042--?
pantothenyl alcohol + ATPD-4'-phosphopantothenyl alcohol + ADP
show the reaction diagram		Corynebacterium ammoniagenes--641389--?
UTP + pantothenateUDP + D-4'-phosphopantothenate
show the reaction diagram		Corynebacterium ammoniagenes-phosphorylation at 18% the rate of ATP641389--?
ITP + pantothenateIDP + D-4'-phosphopantothenate
show the reaction diagram		Corynebacterium ammoniagenes-phosphorylation at 46% the rate of ATP641389--?
additional information?-Homo sapiens-naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease662687---
additional information?-Homo sapiensQ9BZ23naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease660712---
additional information?-Bacillus subtilis-N-pentylpantothenate is no substrate662369---
additional information?-Helicobacter pylorip37564N-pentylpantothenate is no substrate, no activity with UTP or phosphoenolpyruvate as phosphoryl donors662369---
additional information?-Escherichia coliP0A6I3no acivity with hopantenate, formation of a pantothenate kinase-ADP-pantothenate ternary complex662251---
additional information?-Homo sapiens-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 verification689010---
additional information?-Orchesella cincta-pantothenate kinase is upregulated in the warming treatment688109---
additional information?-Bacillus anthracisQ81VX4type III PanK in the spore-forming Bacillus anthracis plays an essential role in the novel thiol/disulfide redox biology of this category A biodefense pathogen672234---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Homo sapiensQ9BZ23-660712--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Staphylococcus aureus-first step in coenzyme A biosynthesis661331, 662408--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Bacillus subtilis-first step in coenzyme A biosynthesis662369--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mus musculus, Escherichia coli-first step in coenzyme A biosynthesis661331--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Homo sapiens-first step in coenzyme A biosynthesis660726, 662455, 662687--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Emericella nidulans-first step in coenzyme A biosynthesis661331--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mycobacterium tuberculosis-first step in coenzyme A biosynthesis660631--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Plasmodium falciparum-first step in coenzyme A biosynthesis660726--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Helicobacter pylorip37564first step in coenzyme A biosynthesis662369--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Mus musculus-first step in coenzyme A biosynthesis, regulatory function662406--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Escherichia coliP0A6I3first step in coenzyme A biosynthesis, the enzyme has a regulatory function in the pathway662251--
ATP + (R)-pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Bacillus anthracis-coaX is essential for growth of Bacillus anthracis687425--
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Lactobacillus plantarum, Escherichia coli, Rattus norvegicus--4406--
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus--641391--
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Saccharomyces cerevisiae--4406--
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Spinacia oleracea, Brassica napus--641388--
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Morganella morganii--4406--
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Escherichia coli-first and rate-controlling reaction of CoA-biosynthesis641393-641393
ATP + D-pantothenateADP + D-4'-phosphopantothenate
show the reaction diagram		Rattus norvegicus-first and rate-controlling reaction of CoA-biosynthesis641387--
ATP + N-heptylpantothenamideADP + N-heptylpantothenamide 4-phosphate
show the reaction diagram		Staphylococcus aureus-substrate is converted to the inactive butyldethia-CoA analogue in the further downstream pathway leading to grwoth inhibition of the organism, overview662408--
ATP + pantothenateADP + (R)-4'-phosphopantothenate
show the reaction diagram		Escherichia coli-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 vivo686816--
ATP + pantothenateADP + 4'-phosphopantothenate
show the reaction diagram		Homo sapiensQ8TE04, Q9H999pantothenate kinase catalyzes the first step in CoA biosynthesis687612--
additional information?-Homo sapiens-naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease662687--
additional information?-Homo sapiensQ9BZ23naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease660712--
additional information?-Homo sapiens-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 verification689010--
additional information?-Orchesella cincta-pantothenate kinase is upregulated in the warming treatment688109--
additional information?-Bacillus anthracisQ81VX4type III PanK in the spore-forming Bacillus anthracis plays an essential role in the novel thiol/disulfide redox biology of this category A biodefense pathogen672234--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
ATPMycobacterium tuberculosis--660631, 671053 2D-image
ATPHomo sapiens--660712, 660726, 662455, 662687, 671347, 676884 2D-image
ATPPlasmodium falciparum--660726, 674852 2D-image
ATPMus musculus--661331, 662406 2D-image
ATPStaphylococcus aureus--661331, 662408, 677154 2D-image
ATPEscherichia coli--661331, 671053, 671767 2D-image
ATPEmericella nidulans--661331 2D-image
ATPEscherichia coliP0A6I3three-dimensional binding site structure, Arg243 is involved662251 2D-image
ATPBacillus subtilis-absolutely specific for662369 2D-image
ATPHelicobacter pylorip37564can partially be substituted by CTP or GTP662369 2D-image
ATPBacillus anthracisQ81VX4-672234 2D-image
ATPThermotoga maritima--674291 2D-image
ATPRattus norvegicusQ923S8-675942 2D-image
ATPArabidopsis thaliana--676548 2D-image
ATPPseudomonas aeruginosaQ9HWC1-677154 2D-image
CTPHelicobacter pylorip37564less active than ATP662369 2D-image
GTPHelicobacter pylorip37564less active than ATP662369 2D-image

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Co2+Corynebacterium ammoniagenes-activation, can replace Mg2+641389
K+Pseudomonas aeruginosaQ9HWC10.06-0.12 mM677154
K+Staphylococcus aureusQ6G7I00.06-0.12 mM677154
KClBacillus subtilis--662369
KClHelicobacter pylorip37564-662369
Mg2+Rattus norvegicus--4406, 641390, 641392
Mg2+Escherichia coli--4406, 641393, 661331
Mg2+Lactobacillus plantarum, Morganella morganii, Saccharomyces cerevisiae--4406
Mg2+Micrococcus luteus--4412
Mg2+Rattus norvegicus-requirement, active substrate: MgATP-complex641387
Mg2+Brassica napus, Spinacia oleracea-requirement, active substrate: MgATP-complex641388
Mg2+Corynebacterium ammoniagenes-Km-value: 1 mM; requirement, active substrate: MgATP-complex641389
Mg2+Rattus norvegicus-Km-value: 0.6 mM; requirement, active substrate: MgATP-complex641391
Mg2+Homo sapiens--660726, 662455
Mg2+Plasmodium falciparum--660726
Mg2+Mus musculus--661331, 662406
Mg2+Staphylococcus aureus--661331, 662408
Mg2+Emericella nidulans--661331
Mg2+Escherichia coliP0A6I3coordinated by the nucleotide beta- and gamma-phosphates and the side chains of Ser102 and Glu199, required for ATP but not for ADP binding662251
Mg2+Bacillus subtilis--662369
Mg2+Helicobacter pylorip37564-662369
Mg2+Pseudomonas aeruginosaQ9HWC1required677154
Mg2+Staphylococcus aureusQ6G7I0required677154
Mg2+Picrophilus torridusQ6L2I5activity with 1 mM (plus 2.5 mM ATP): 252 nmol/min/mg704326
Mn2+Corynebacterium ammoniagenes-activation, can replace Mg2+641389
NH4+Pseudomonas aeruginosaQ9HWC1induces a 5fold higher activation than either K+ or Rb+677154
NH4+Staphylococcus aureusQ6G7I0induces a 5fold higher activation than either K+ or Rb+677154
Ni2+Corynebacterium ammoniagenes-activation, can replace Mg2+ with about 50% efficiency641389
Rb+Pseudomonas aeruginosaQ9HWC1-677154
Rb+Staphylococcus aureusQ6G7I0-677154
Zn2+Corynebacterium ammoniagenes-activation, can replace Mg2+ with about 50% efficiency641389
Mn2+Picrophilus torridusQ6L2I5addition (1 mM) instead of Mg2+ accelerates activity 1.75fold704326
additional informationCorynebacterium ammoniagenes-no activation by Ca2+, Cd2+, Ba2+, Pb2+, Fe2+ or Cu2+641389
additional informationRattus norvegicus-nonspecific activation by anions in triethanolamine buffer, pH 7, mostly dicarboxylic acids, not citrate or diphosphate641391

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazideHomo sapiens, Plasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
(2R)-2,4-dihydroxy-3,3-dimethylbutanohydrazidePlasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
(2R)-2,4-dihydroxy-N-(2-hydroxyethyl)-3,3-dimethylbutanamidePlasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
(2R)-N-(2,3-dihydroxypropyl)-2,4-dihydroxy-3,3-dimethylbutanamidePlasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamideHomo sapiens, Plasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
(R)-3-azido-4,4-dimethyl-dihydro-furan-2-oneEscherichia coli, Staphylococcus aureus--661331 2D-image
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acidEmericella nidulans-80.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acidEscherichia coli-29.4% inhibition at 0.1 mM, purified enzyme661331 2D-image
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acidMus musculus-2.7% inhibition at 0.1 mM, cell extract661331 2D-image
(R)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acidStaphylococcus aureus-78.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
(R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acidEscherichia coli-11% inhibition at 0.1 mM, purified enzyme661331 2D-image
(R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acidMus musculus-13.1% inhibition at 0.1 mM, cell extract661331 2D-image
(R)-4-(2-azido-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acidEscherichia coli, Staphylococcus aureus--661331 2D-image
(S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acidEscherichia coli-12.5% inhibition at 0.1 mM, purified enzyme661331 2D-image
(S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acidStaphylococcus aureus-54.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
(S)-trifluoro-methanesulfonic acid 4,4-dimethyl-2-oxo-tetrahydro-furan-3-yl-esterEscherichia coli, Staphylococcus aureus--661331 2D-image
2'-KetopantetheineRattus norvegicus--641387 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramideEmericella nidulans-10.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramideEscherichia coli-76.4% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramideMus musculus-89.6% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-heptylcarbamoyl-ethyl)-butyramideStaphylococcus aureus-98.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramideEmericella nidulans-46.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramideEscherichia coli-71.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramideMus musculus-89.9% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-isobutylcarbamoyl-ethyl)-butyramideStaphylococcus aureus-97.1% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramidePlasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramideEmericella nidulans-12.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramideEscherichia coli-72.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramideMus musculus-81.4% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramideStaphylococcus aureus-98.8% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramideEmericella nidulans-59.5% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramideEscherichia coli-57.8% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramideMus musculus-80.9% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-phenethylcarbamoyl-ethyl)-butyramideStaphylococcus aureus-89.5% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramidePlasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramideEmericella nidulans-51.4% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramideEscherichia coli-82.5% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramideMus musculus-86.8% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramideStaphylococcus aureus-99.1% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramideEmericella nidulans-40.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramideEscherichia coli-71.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramideMus musculus-84.6% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[1-methyl-3-phenyl-propylcarbamoyl]-ethyl)-butyramideStaphylococcus aureus-86.4% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramideEmericella nidulans-35.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramideEscherichia coli-44.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramideMus musculus-70.5% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[2-(3,4-dimethoxy-phenyl)-ethylcarbamoyl]-ethyl)-butyramideStaphylococcus aureus-17.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramideEmericella nidulans-28.4% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramideEscherichia coli-33.4% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramideMus musculus-57.4% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-(2-[3,4,5-trimethoxy-benzylcarbamoyl]-ethyl)-butyramideStaphylococcus aureus-8.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramideEmericella nidulans-71.9% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramideEscherichia coli-3.0% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramideMus musculus-93.3% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2,6,6-trimethylbicyclo[3.1.1]hept-3-ylcarbamoyl)-ethyl]-butyramideStaphylococcus aureus-76.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramideEmericella nidulans-41.8% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramideEscherichia coli-28.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramideMus musculus-68.9% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethoxy-ethylcarbamoyl)-ethyl]-butyramideStaphylococcus aureus-95.1% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramideEmericella nidulans-61.0% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramideEscherichia coli-53.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramideMus musculus-82.9% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-ethylsulfanylethylcarbamoyl)-ethyl]-butyramideStaphylococcus aureus-97.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramideEmericella nidulans-49.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramideEscherichia coli-61.9% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramideMus musculus-85.0% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-methylsulfanylethylcarbamoyl)-ethyl]-butyramideStaphylococcus aureus-96.5% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramideEmericella nidulans-13.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramideEscherichia coli-10.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramideMus musculus-39.1% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(2-morpholin-4-yl-ethylcarbamoyl)-ethyl]-butyramideStaphylococcus aureus-4.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramideEmericella nidulans-92.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramideEscherichia coli-90.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramideMus musculus-98.9% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3,7-dimethylocta-2,6-dienylcarbamoyl)-ethyl]-butyramideStaphylococcus aureus-97.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramidePlasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramideEmericella nidulans-62.1% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramideEscherichia coli-32.3% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramideMus musculus-61.2% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramideStaphylococcus aureus-96.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramidePlasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramideEmericella nidulans-72.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramideEscherichia coli-54.3% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramideMus musculus-87.2% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramideStaphylococcus aureus-97.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEmericella nidulans-54.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEscherichia coli-55.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideMus musculus-82.2% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[2-(4-methoxy-benzylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideStaphylococcus aureus-53.9% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramideEmericella nidulans-15.9% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramideEscherichia coli-7.3% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramideMus musculus-73.0% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-3,3-dimethyl N-[3-(4-benzyl-piperazin-1-yl)-3-oxo-propyl]-butyramideStaphylococcus aureus-9.3% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEmericella nidulans-25.9% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEscherichia coli-3.4% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideMus musculus-56.7% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-N-[2-(2-hydroxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideStaphylococcus aureus-72.2% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEmericella nidulans-26.8% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEscherichia coli-28.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideMus musculus-67.6% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-N-[2-(2-methoxy-ethylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideStaphylococcus aureus-90.1% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEmericella nidulans-i.e. pantothenol, 36.7% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEscherichia coli-i.e. pantothenol, 11.5% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideMus musculus-i.e. pantothenol, 70.3% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-N-[2-(3-hydroxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideStaphylococcus aureus-i.e. pantothenol, 79.9% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramidePlasmodium falciparum-competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism660726 2D-image
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEmericella nidulans-52.9% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideEscherichia coli-38.6% inhibition at 0.1 mM, purified enzyme661331 2D-image
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideMus musculus-64.9% inhibition at 0.1 mM, cell extract661331 2D-image
2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramideStaphylococcus aureus-94.4% inhibition at 0.1 mM, purified enzyme661331 2D-image
4-(2,4-dihydroxy-3,3-dimethylbutylamido)butyric acidMus musculus-competitive inhibitor; competitive inhibitor, IC50: 0.05-0.15 mM673027 2D-image
5'-deoxy-5'-(4-(beta-D-galactopyranosyloxymethyl)-1,2,3-triazol-1-yl)adenosineBacillus anthracis-competitive inhibitor with respect to ATP706042-
acetoacetyl-CoAEscherichia coli--641393 2D-image
acetyl-CoABrassica napus, Spinacia oleracea-not641388 2D-image
acetyl-CoARattus norvegicus--641390, 641391, 641394 2D-image
acetyl-CoAEscherichia coli--641393 2D-image
acetyl-CoAMus musculus-strong641397 2D-image
acetyl-CoAEmericella nidulansO93921selective and strong, competitive to ATP641402 2D-image
acetyl-CoAMus musculus-feedback inhibition, regulatory function, isozyme PanK1beta and isozyme PanK3, strong inhibition of mutant chimera PanK1beta-3-1beta, slight inhibition of mutant chimera PanK3-1beta-3662406 2D-image
acetyl-CoAPlasmodium falciparum-effective inhibitor674852 2D-image
acetyl-CoAHomo sapiens-competitive inhibitor of purified PanK2 with respect to ATP; IC50: 60 nM, competitive inhibitor with respect to ATP676884 2D-image
acetyl-CoAHomo sapiens, Mus musculus--686741 2D-image
acetyl-CoAHomo sapiensQ8TE04, Q9H999a feedback inhibitor; a feedback inhibitor687612 2D-image
Acyl carrier proteinBrassica napus--641388 2D-image
Acyl carrier proteinSpinacia oleracea-PAK II: inhibition, PAK I: stimulation between 0.015-0.035 mM641388 2D-image
acyl-CoA-estersRattus norvegicus-long-chain acyl-CoAs less efficient than short-chain ester641390 2D-image
acyl-CoA-estersRattus norvegicus--641391 2D-image
acyl-CoA-estersMus musculus-long chain acyl CoA, feed-back inhibition, isoform PanK1alpha641400 2D-image
ADPCorynebacterium ammoniagenes-not641389 2D-image
ADPEscherichia coli--641393 2D-image
AlCl3Corynebacterium ammoniagenes-strong641389 2D-image
AMPEscherichia coli--641393 2D-image
Arachidonoyl-CoARattus norvegicus--641390 2D-image
ATPRattus norvegicus-free form641391 2D-image
Ba2+Corynebacterium ammoniagenes--641389 2D-image
citrateRattus norvegicus--641391 2D-image
CoARattus norvegicus-strong641387 2D-image
CoABrassica napus, Spinacia oleracea-not641388 2D-image
CoACorynebacterium ammoniagenes--641389 2D-image
CoARattus norvegicus--641390 2D-image
CoARattus norvegicus-not reversible by D-carnitine, acetyl-L-carnitine or other carnitine analogs; reversible by L-carnitine641391 2D-image
CoARattus norvegicus-feed-back inhibition; in vitro; reversible by L-carnitine641392 2D-image
CoAEscherichia coli-in vitro; in vivo; kinetics641393 2D-image
CoARattus norvegicus-inhibits isoform A stronger than isoform B641394 2D-image
CoAMus musculus-feed-back inhibition, isoform PanK1alpha641400 2D-image
CoAHomo sapiens-feedback inhibition, inhibition kinetics of recombinant isozyme mPanK2662455 2D-image
CoAEscherichia coli-feedback inhibitor671053 2D-image
CoAMycobacterium tuberculosisP63810feedback inhibitor671053 2D-image
CoAPlasmodium falciparum-IC50: 0.2 mM674852 2D-image
CoAMycobacterium tuberculosis--677979 2D-image
CoAEscherichia coli-competitive686816 2D-image
CoA estersHomo sapiens-feedback inhibition, inhibition kinetics of recombinant isozyme mPanK2662455 2D-image
coenzyme AEscherichia coliP0A6I3allosteric regulator, feedback inhibition662251 2D-image
coenzyme AMus musculus-feedback inhibition, regulatory function, isozyme PanK1beta, slight inhibition of isozyme PanK3662406 2D-image
coenzyme APlasmodium falciparum-feedback inhibition regulates pantothenol uptake. Furosemide reduces this inherent feedback inhibition by competing with coenzyme A for binding to pantothenate kinase, thereby increasing pantothenol uptake674852 2D-image
Cu2+Corynebacterium ammoniagenes-strong641389 2D-image
D-pantothenateCorynebacterium ammoniagenes-substrate inhibition, above 0.5 mM641389 2D-image
dephospho-CoARattus norvegicus--641387, 641390, 641391 2D-image
dephospho-CoACorynebacterium ammoniagenes--641389 2D-image
dephospho-CoAEscherichia coli-not641393 2D-image
diphosphateRattus norvegicus--641391 2D-image
EDTACorynebacterium ammoniagenes--641389 2D-image
Fe2+Corynebacterium ammoniagenes-strong641389 2D-image
HgCl2Corynebacterium ammoniagenes-strong641389 2D-image
L-PantothenateRattus norvegicus--641387 2D-image
malonyl-CoABrassica napus--641388 2D-image
malonyl-CoASpinacia oleracea-0.075 mM, complete inhibition of PAK I641388 2D-image
malonyl-CoARattus norvegicus--641390 2D-image
malonyl-CoAEscherichia coli--641393 2D-image
malonyl-CoAMus musculus-feedback inhibition, regulatory function, isozyme PanK3, slight inhibition of isozyme PanK1beta662406 2D-image
N-heptylpantothenamideEmericella nidulans--661331 2D-image
N-heptylpantothenamideEscherichia coliP0A6I3competitive to pantothenate662251 2D-image
N-heptylpantothenamideStaphylococcus aureus-IC50 is 0.0048 mM, potent growth inhibitory anti-metabolite662408 2D-image
N-pentylpantothenamideEmericella nidulans--661331 2D-image
N-pentylpantothenamideEscherichia coliP0A6I3competitive to pantothenate662251 2D-image
N-pentylpantothenamideStaphylococcus aureus-IC50 is 0.0035 mM, has antimicrobial activity against Staphylococcus aureus662408 2D-image
Na2HAsO4Corynebacterium ammoniagenes--641389 2D-image
NH4+Corynebacterium ammoniagenes--641389 2D-image
Octanoyl-CoARattus norvegicus--641390 2D-image
oleoyl-CoARattus norvegicus--641390 2D-image
palmitoyl-CoARattus norvegicus--641390, 641391 2D-image
palmitoyl-CoAEscherichia coli--641393 2D-image
palmitoyl-CoAMus musculus-feedback inhibition, regulatory function, isozyme PanK3, mutant chimera PanK1beta-3-1beta, slight inhibition of mutant chimera PanK3-1beta-3662406 2D-image
palmitoyl-CoAHomo sapiens-strong inhibitor676884 2D-image
pantetheineCorynebacterium ammoniagenes--641389 2D-image
pantetheine 4'-phosphateRattus norvegicus-strong641387 2D-image
pantetheine 4'-phosphateCorynebacterium ammoniagenes-weak641389 2D-image
pantetheine 4'-phosphateEscherichia coli-not641393 2D-image
pantothenamide, N-substitutedStaphylococcus aureus-IC50 about 0.0004-0.0016 mM641398-
pantothenic acid 4'-phosphateCorynebacterium ammoniagenes--641389 2D-image
pantothenolPlasmodium falciparum-competitive inhibition660726 2D-image
pantothenoylcysteine 4'-phosphateRattus norvegicus-strong641387 2D-image
pantothenoylcysteine 4'-phosphateCorynebacterium ammoniagenes-weak641389 2D-image
pantothenyl alcoholCorynebacterium ammoniagenes--641389 2D-image
Pb2+Corynebacterium ammoniagenes--641389 2D-image
propionyl-CoARattus norvegicus--641390 2D-image
succinyl-CoAEscherichia coli--641393 2D-image
malonyl-CoAPlasmodium falciparum-effective inhibitor674852 2D-image
additional informationSpinacia oleracea-not inhibitory: 3',5'-ADP; not inhibitory: CoASH, acetyl-CoA641388-
additional informationCorynebacterium ammoniagenes-no inhibition by 2,2'-dipyridyl, Ca2+, Cd2+, 3'-AMP, GTP, GDP, ITP, UTP; not inhibitory: 3',5'-ADP641389-
additional informationRattus norvegicus-not inhibitory: Mg2+, NADP+; not inhibitory: NAD+641391-
additional informationEscherichia coli-not inhibitory: 3',5'-ADP; not inhibitory: cAMP, NADH, NADPH, CoA:glutathione disulfide; not inhibitory: NAD+641393-
additional informationPlasmodium falciparum-in vivo antiplasmodial activities of the inhibitor molecules, overview660726-
additional informationEmericella nidulans-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, overview661331-
additional informationEscherichia coli-structural features required for enzyme inhibition, overview661331-
additional informationMus musculus-no inhibition by (S)-4-(2,4-dihydroxy-3,3-dimethyl-butyrylamino)-butyric acid, structural features required for enzyme inhibition, overview661331-
additional informationStaphylococcus aureus-no inhibition by (R)-4-(2-amino-4-hydroxy-3,3-dimethyl-butyrylamino)-butyric acid, structural features required for enzyme inhibition, overview661331-
additional informationEscherichia coliP0A6I3no inhibition by hopantenate662251-
additional informationBacillus subtilis-no inhibition by N-pentylpantothenamide, enzyme is not affected by CoA or acetyl-CoA662369-
additional informationHelicobacter pylorip37564no inhibition by N-pentylpantothenamide, enzyme is not affected by CoA or acetyl-CoA662369-
additional informationMus musculus-structural determinants for feedback inhibition662406-
additional informationStaphylococcus aureus-no feedback regulation by CoA or acetyl-CoA662408-
additional informationHomo sapiens-feedback inhibition by acyl-CoAs662687-
additional informationBacillus anthracisQ81VX4the enzyme is not subject to feedback inhibition by CoASH672234-
additional informationThermotoga maritima-not inhibited by CoA or its thioesters674291-
additional informationEscherichia coli-inhibition by CoA thioesters686816-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
Acyl carrier proteinSpinacia oleracea-PAK II: inhibition, PAK I: stimulation between 0.015-0.035 mM641388 2D-image
CoAMus musculus-stimulates641397 2D-image
palmitoylcarnitineHomo sapiens-activates; the enzymatic activity of PanK2 is stimulated to the highest level by 0.008 mM palmitoylcarnitine676884 2D-image
palmitoylcarnitineHomo sapiens, Mus musculus-activates686741 2D-image
dithiothreitolEscherichia coli-activation641393 2D-image
additional informationRattus norvegicus-no activation by L-carnitine641392-
additional informationBacillus subtilis-enzyme is not affected by CoA or acetyl-CoA662369-
additional informationHelicobacter pylorip37564enzyme is not affected by CoA or acetyl-CoA662369-
additional informationStaphylococcus aureus-no feedback regulation by CoA or acetyl-CoA662408-
additional informationHomo sapiens-carnitine and octanoylcarnitine do not have any effect on the PanK2 activity676884-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0057-(R)-pantothenateMus musculus-recombinant isozyme PanK1beta, pH 7.0, 37°C662406 2D-image
0.009-(R)-pantothenateHomo sapiens-recombinant isozyme iPanK2, pH 7.5, 37°C662455 2D-image
0.0095-(R)-pantothenateMus musculus-recombinant isozyme PanK3, pH 7.0, 37°C662406 2D-image
0.023-(R)-pantothenateStaphylococcus aureus-pH 7.5, 37°C, recombinant enzyme662408 2D-image
0.025-(R)-pantothenateHomo sapiens-recombinant isozyme mPanK2, pH 7.5, 37°C662455 2D-image
0.041-(R)-pantothenateEscherichia coliP0A6I3pH 7.5, 37°C, recombinant His-tagged enzyme662251 2D-image
0.043-(R)-pantothenateThermotoga maritima-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 50°C674291 2D-image
0.101-(R)-pantothenateHelicobacter pylorip37564pH 7.6, 25°C662369 2D-image
0.168-(R)-pantothenateBacillus subtilis-pH 7.6, 25°C662369 2D-image
0.027-ATPStaphylococcus aureus--686816 2D-image
0.034-ATPStaphylococcus aureus-pH 7.5, 37°C, recombinant enzyme662408 2D-image
0.035-ATPCorynebacterium ammoniagenes-pH 6.5, 37°C641389 2D-image
0.05-ATPMycobacterium tuberculosis-25°C, pH 7.8, determined by isothermal titration calorimetry677979 2D-image
0.064-ATPHomo sapiens-recombinant isozyme mPanK2, pH 7.5, 37°C662455 2D-image
0.068-ATPHomo sapiens-recombinant isozyme iPanK2, pH 7.5, 37°C662455 2D-image
0.087-ATPMus musculus-recombinant isozyme PanK1beta, pH 7.0, 37°C662406 2D-image
0.093-ATPStaphylococcus aureus-pH 7.5, 25°C641398 2D-image
0.099-ATPPicrophilus torridusQ6L2I5-704326 2D-image
0.112-ATPMus musculus-recombinant isozyme PanK3, pH 7.0, 37°C662406 2D-image
0.115-ATPEscherichia coli-Tris-HCl buffer, pH 8.0701469 2D-image
0.151-ATPMycobacterium tuberculosis-Tris-HCl buffer, pH8.0701469 2D-image
0.375-ATPMycobacterium tuberculosis-25°C, pH 7.8, determined from coupled assay677979 2D-image
0.406-ATPEscherichia coli-citrate buffer, pH 6.0701469 2D-image
0.51-ATPBacillus anthracis--706042 2D-image
0.616-ATPMycobacterium tuberculosis-citrate buffer, pH6.0701469 2D-image
3.05-ATPBacillus subtilis-pH 7.6, 25°C662369 2D-image
6.04-ATPThermotoga maritima-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 50°C674291 2D-image
9.59-ATPHelicobacter pylorip37564pH 7.6, 25°C662369 2D-image
1.759-CTPBacillus anthracis--706042 2D-image
0.138-dATPBacillus anthracis--706042 2D-image
0.839-dCTPBacillus anthracis--706042 2D-image
0.117-dGTPBacillus anthracis--706042 2D-image
0.723-dTTPBacillus anthracis--706042 2D-image
0.225-MgATP2-Escherichia coli-pH 7.4, 25°C641393 2D-image
0.6-MgATP2-Rattus norvegicus-pH 7.0, 37°C641391 2D-image
1-MgATP2-Rattus norvegicus-pH 6.1, 37°C641387 2D-image
0.008-N-heptylpantothenamideStaphylococcus aureus-pH 7.5, 37°C, recombinant enzyme662408 2D-image
0.124-N-heptylpantothenamideEscherichia coliP0A6I3pH 7.5, 37°C, recombinant His-tagged enzyme662251 2D-image
0.003-N-pentylpantothenamideStaphylococcus aureus-pH 7.5, 37°C, recombinant enzyme662408 2D-image
0.14-N-pentylpantothenamideEscherichia coliP0A6I3pH 7.5, 37°C, recombinant His-tagged enzyme662251 2D-image
0.009-pantothenateEscherichia coli--641393 2D-image
0.011-pantothenateRattus norvegicus-pH 6.1, 37°C641387 2D-image
0.016-pantothenateRattus norvegicus-pH 6.1, 37°C641390 2D-image
0.018-pantothenateRattus norvegicus-pH 7.0, 37°C641391 2D-image
0.027-pantothenateStaphylococcus aureus-pH 7.5, 25°C641398 2D-image
0.067-pantothenateCorynebacterium ammoniagenes-pH 6.5, 37°C641389 2D-image
0.093-pantothenateStaphylococcus aureus--686816 2D-image
0.1-pantothenateMycobacterium tuberculosis-25°C, pH 7.8, determined from coupled assay677979 2D-image
0.136-pantothenateEscherichia coli--686816 2D-image
0.18-pantothenateMycobacterium tuberculosis-25°C, pH 7.8, determined by isothermal titration calorimetry677979 2D-image
0.621-pantothenatePicrophilus torridusQ6L2I5-704326 2D-image
0.8-pantothenateSpinacia oleracea-isoform 2, 37°C, pH 8.0641388 2D-image
1.3-pantothenateSpinacia oleracea-isoform 1, 37°C, pH 8.0641388 2D-image
0.25-pantothenolMycobacterium tuberculosis-25°C, pH 7.8, determined by isothermal titration calorimetry677979 2D-image
0.28-pantothenolMycobacterium tuberculosis-25°C, pH 7.8, determined from coupled assay677979 2D-image
1.715-UTPBacillus anthracis--706042 2D-image
1-MgATP2-Corynebacterium ammoniagenes-pH 6.5, 37°C641389 2D-image
additional information-additional informationHomo sapiens-kinetics of recombinant isozyme mPanK2662455-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.29-(R)-pantothenateThermotoga maritima-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 50°C674291 2D-image
1.7-(R)-pantothenateStaphylococcus aureus-pH 7.5, 37°C, recombinant enzyme662408 2D-image
2.09-(R)-pantothenateHelicobacter pylorip37564pH 7.6, 25°C662369 2D-image
2.12-(R)-pantothenateBacillus subtilis-pH 7.6, 25°C662369 2D-image
0.052-ATPMycobacterium tuberculosis-citrate buffer, pH6.0701469 2D-image
0.071-ATPEscherichia coli-citrate buffer, pH 6.0701469 2D-image
0.411-ATPMycobacterium tuberculosis-Tris-HCl buffer, pH8.0701469 2D-image
0.62-ATPMycobacterium tuberculosis-25°C, pH 7.8, determined from coupled assay677979 2D-image
0.65-ATPMycobacterium tuberculosis-25°C, pH 7.8, determined by isothermal titration calorimetry677979 2D-image
0.718-ATPPicrophilus torridusQ6L2I5-704326 2D-image
1.14-ATPEscherichia coli-Tris-HCl buffer, pH 8.0701469 2D-image
1.5-ATPBacillus anthracis--706042 2D-image
1.6-ATPStaphylococcus aureus-pH 7.5, 37°C, recombinant enzyme662408 2D-image
2.09-ATPHelicobacter pylorip37564pH 7.6, 25°C662369 2D-image
2.12-ATPBacillus subtilis-pH 7.6, 25°C662369 2D-image
1.5-CTPBacillus anthracis--706042 2D-image
0.9-dATPBacillus anthracis--706042 2D-image
0.5-dCTPBacillus anthracis--706042 2D-image
0.8-dGTPBacillus anthracis--706042 2D-image
0.4-dTTPBacillus anthracis--706042 2D-image
0.425-N-heptylpantothenamideStaphylococcus aureus-pH 7.5, 37°C, recombinant enzyme662408 2D-image
0.15-N-pentylpantothenamideStaphylococcus aureus-pH 7.5, 37°C, recombinant enzyme662408 2D-image
0.61-pantothenateMycobacterium tuberculosis-25°C, pH 7.8, determined from coupled assay677979 2D-image
0.62-pantothenateMycobacterium tuberculosis-25°C, pH 7.8, determined by isothermal titration calorimetry677979 2D-image
0.818-pantothenatePicrophilus torridusQ6L2I5-704326 2D-image
0.38-pantothenolMycobacterium tuberculosis-25°C, pH 7.8, determined by isothermal titration calorimetry677979 2D-image
0.4-pantothenolMycobacterium tuberculosis-25°C, pH 7.8, determined from coupled assay677979 2D-image
1.7-UTPBacillus anthracis--706042 2D-image

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.08-ATPMycobacterium tuberculosis-citrate buffer, pH6.070146922040
0.17-ATPEscherichia coli-citrate buffer, pH 6.070146922040
2.72-ATPMycobacterium tuberculosis-Tris-HCl buffer, pH8.070146922040
2.9-ATPBacillus anthracis--70604222040
9.91-ATPEscherichia coli-Tris-HCl buffer, pH 8.070146922040
0.9-CTPBacillus anthracis--7060428829
6.6-dATPBacillus anthracis--7060429499
0.6-dCTPBacillus anthracis--7060429510
6.5-dGTPBacillus anthracis--7060429669
0.5-dTTPBacillus anthracis--70604210218
1-UTPBacillus anthracis--70604217783

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.138-(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazideHomo sapiens-37°C, versus pantothenate at 1 mM660726 2D-image
0.2-(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
0.013-(2R)-2,4-dihydroxy-3,3-dimethylbutanohydrazidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
0.0019-(2R)-2,4-dihydroxy-N-(2-hydroxyethyl)-3,3-dimethylbutanamidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
4-(2R)-N-(2,3-dihydroxypropyl)-2,4-dihydroxy-3,3-dimethylbutanamidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
0.082-(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
1-(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamideHomo sapiens-37°C, versus pantothenate at 1 mM660726 2D-image
0.162-2,4-dihydroxy-3,3-dimethyl N-(2-pentylcarbamoyl-ethyl)-butyramidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
0.112-2,4-dihydroxy-3,3-dimethyl N-(2-propylcarbamoylethyl)-butyramidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
0.111-2,4-dihydroxy-3,3-dimethyl N-[2-(3-ethoxy-propylcarbamoyl)-ethyl]-butyramidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
0.076-2,4-dihydroxy-3,3-dimethyl N-[2-(3-methylsulfanylpropylcarbamoyl)-ethyl]-butyramidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
0.109-2,4-dihydroxy-N-[2-(3-methoxy-propylcarbamoyl)-ethyl]-3,3-dimethyl-butyramidePlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image
0.164-5'-deoxy-5'-(4-(beta-D-galactopyranosyloxymethyl)-1,2,3-triazol-1-yl)adenosineBacillus anthracis--706042-
0.002-CoAMycobacterium tuberculosis--677979 2D-image
0.033-CoACorynebacterium ammoniagenes-reduced form, pH 6.5, 37°C641389 2D-image
0.067-CoACorynebacterium ammoniagenes-oxidized form, pH 6.5, 37°C641389 2D-image
0.037-pantetheine 4'-phosphateCorynebacterium ammoniagenes-pH 6.5, 37°C641389 2D-image
0.125-pantothenic acid 4'-phosphateCorynebacterium ammoniagenes-pH 6.5, 37°C641389 2D-image
0.129-pantothenolPlasmodium falciparum-37°C, versus pantothenate at 1 mM660726 2D-image

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.050.154-(2,4-dihydroxy-3,3-dimethylbutylamido)butyric acidMus musculus-competitive inhibitor, IC50: 0.05-0.15 mM673027 2D-image
6e-05-acetyl-CoAHomo sapiens-IC50: 60 nM, competitive inhibitor with respect to ATP676884 2D-image
6.25e-05-acetyl-CoAMus musculus--686741 2D-image
0.000125-acetyl-CoAHomo sapiens--686741 2D-image
0.2-CoAPlasmodium falciparum-IC50: 0.2 mM674852 2D-image
0.0048-N-heptylpantothenamideStaphylococcus aureus-IC50 is 0.0048 mM, potent growth inhibitory anti-metabolite662408 2D-image
0.0035-N-pentylpantothenamideStaphylococcus aureus-IC50 is 0.0035 mM, has antimicrobial activity against Staphylococcus aureus662408 2D-image
0.00040.0016pantothenamide, N-substitutedStaphylococcus aureus-IC50 about 0.0004-0.0016 mM641398-

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
0.0002421-Homo sapiens-0.045 mM pantothenate, 0.25 mM ATP (pH 7.0), 10 mM MgCl2, 0.1 M Tris/HCl (pH 7.5), at 37°C676884
0.0012-Rattus norvegicus-pH 6.1, 37°C641390
0.00171-Rattus norvegicus-pH 7.0, 37°C641391
0.0041-Rattus norvegicus-pH 6.1, 37°C641387
0.034-Corynebacterium ammoniagenes-pH 6.5, 37°C641389
0.152-Spinacia oleracea-isoform 1, 37°C, pH 8.0641388
0.36-Picrophilus torridusQ6L2I5purified recombinant protein704326
additional information-Micrococcus luteus--4412
additional information-Rattus norvegicus-specific activity in various tissues per mg wet weight641392
additional information-Staphylococcus aureus--662408

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
5-Picrophilus torridusQ6L2I5-704326
5.96.3Rattus norvegicus--641387
69Rattus norvegicus-broad, highest activity in 50 mM phosphate buffer641391
6.1-Rattus norvegicus--641390
6.57Corynebacterium ammoniagenes--641389
7-Mus musculus-assay at662406
7.5-Emericella nidulans, Escherichia coli, Mus musculus, Staphylococcus aureus-assay at661331
7.5-Escherichia coliP0A6I3assay at662251
7.5-Staphylococcus aureus-assay at662408
7.5-Homo sapiens-assay at662455
7.6-Bacillus subtilis-assay at662369
7.6-Helicobacter pylorip37564assay at662369
8-Spinacia oleracea-broad641388

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
4.56Picrophilus torridusQ6L2I5more than 70% of the maximum activity704326
69Spinacia oleracea--641388

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
25-Escherichia coli-assay at641393
25-Bacillus subtilis-assay at662369
25-Helicobacter pylorip37564assay at662369
3037Corynebacterium ammoniagenes--641389
37-Homo sapiens, Plasmodium falciparum-assay at660726
37-Emericella nidulans, Escherichia coli, Mus musculus, Staphylococcus aureus-assay at661331
37-Escherichia coliP0A6I3assay at662251
37-Mus musculus-assay at662406
37-Staphylococcus aureus-assay at662408
37-Homo sapiens-assay at662455
55-Picrophilus torridusQ6L2I5-704326

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
3042Escherichia coli--671767
5070Picrophilus torridusQ6L2I5more than 80% of the maximum activity704326

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
5.1-Rattus norvegicus-isoelectric focusing, isoform B641394
5.7-Rattus norvegicus-isoelectric focusing, isoform A641394

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
brainRattus norvegicus--641392Manually annotated by BRENDA team
brainHomo sapiens--660712, 662455Manually annotated by BRENDA team
brainHomo sapiens-subtissue distribution of several isoforms of PanK2, overview662687Manually annotated by BRENDA team
brainHomo sapiens, Mus musculus-expression of PanK2 is higher in human brain compared to mouse brain686741Manually annotated by BRENDA team
brainHomo sapiens-in most cases of pantothenate kinase-associated neurodegeneration, abnormalities are restricted to globus pallidus and substantia nigra689193Manually annotated by BRENDA team
brainGorilla beringei-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 mutation690187Manually annotated by BRENDA team
flowerArabidopsis thaliana--676548Manually annotated by BRENDA team
heartRattus norvegicus-ventricular muscle641391Manually annotated by BRENDA team
heartRattus norvegicus--641392Manually annotated by BRENDA team
heartMus musculus-mainly isoform mPanK1alpha641397Manually annotated by BRENDA team
HEK-293 cellHomo sapiens--676884Manually annotated by BRENDA team
HEK-293T cellMus musculus--673027Manually annotated by BRENDA team
Hep-G2 cellMus musculus--673027Manually annotated by BRENDA team
JURKAT cellHomo sapiens--660726Manually annotated by BRENDA team
kidneyRattus norvegicus--4406, 641392Manually annotated by BRENDA team
kidneyMus musculus-both isoforms641397Manually annotated by BRENDA team
leafSpinacia oleracea--641388Manually annotated by BRENDA team
leafArabidopsis thaliana--676548Manually annotated by BRENDA team
liverRattus norvegicus--4406, 641387, 641390, 641392, 641394Manually annotated by BRENDA team
liverMus musculus-mainly isoform mPanK1beta641397Manually annotated by BRENDA team
liverMus musculus--662406Manually annotated by BRENDA team
muscleRattus norvegicusQ923S8-675942Manually annotated by BRENDA team
neuronHomo sapiens--662687Manually annotated by BRENDA team
PC-12 cellMus musculus--673027Manually annotated by BRENDA team
rootArabidopsis thaliana--676548Manually annotated by BRENDA team
seedlingBrassica napus, Spinacia oleracea--641388Manually annotated by BRENDA team
stemArabidopsis thaliana--676548Manually annotated by BRENDA team
trophozoitePlasmodium falciparum--660726Manually annotated by BRENDA team
liverMus musculus-; chemical knockout of pantothenate kinase reveals the metabolic and genetic program responsible for hepatic coenzyme A homeostasis673027Manually annotated by BRENDA team
additional informationRattus norvegicus-distribution in different tissues641392Manually annotated by BRENDA team
additional informationHomo sapiens-naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease660712, 662687Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
chloroplastSpinacia oleracea--9507641388Manually annotated by BRENDA team
cytoplasmRattus norvegicusQ923S8-5737675942Manually annotated by BRENDA team
cytosolRattus norvegicus--58294406, 641387, 641390, 641392Manually annotated by BRENDA team
cytosolEscherichia coli--58294406, 641393Manually annotated by BRENDA team
cytosolLactobacillus plantarum, Morganella morganii, Saccharomyces cerevisiae--58294406Manually annotated by BRENDA team
cytosolMicrococcus luteus--58294412Manually annotated by BRENDA team
cytosolDrosophila melanogaster--5829641401Manually annotated by BRENDA team
cytosolHomo sapiens, Mus musculus--5829686741Manually annotated by BRENDA team
dendriteHomo sapiens--30425662687Manually annotated by BRENDA team
mitochondrionHomo sapiensQ9BZ23PANK2 contains a mitochondrial targeting signal5739660712Manually annotated by BRENDA team
mitochondrionHomo sapiens-several isoforms of brain PanK25739662687Manually annotated by BRENDA team
mitochondrionHomo sapiens--5739671347, 703958Manually annotated by BRENDA team
mitochondrionHomo sapiens-; 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-oxidation5739676884Manually annotated by BRENDA team
mitochondrionDrosophila melanogaster-one of the splicing isoforms localizes to mitochondria5739703958Manually annotated by BRENDA team
additional informationHomo sapiens-multiple subcellular distribution of multiple enzyme forms-662687Manually annotated by BRENDA team

PDBSCOPCATHORGANISM
3tqc, downloadSCOP (3tqc)CATH (3tqc)Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
1esm, downloadSCOP (1esm)CATH (1esm)Escherichia coli (strain K12)
1esn, downloadSCOP (1esn)CATH (1esn)Escherichia coli (strain K12)
1sq5, downloadSCOP (1sq5)CATH (1sq5)Escherichia coli (strain K12)
2i7n, downloadSCOP (2i7n)CATH (2i7n)Homo sapiens
2i7p, downloadSCOP (2i7p)CATH (2i7p)Homo sapiens
3mk6, downloadSCOP (3mk6)CATH (3mk6)Homo sapiens
3smp, downloadSCOP (3smp)CATH (3smp)Homo sapiens
3sms, downloadSCOP (3sms)CATH (3sms)Homo sapiens
3djc, downloadSCOP (3djc)CATH (3djc)Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
2ges, downloadSCOP (2ges)CATH (2ges)Mycobacterium tuberculosis
2get, downloadSCOP (2get)CATH (2get)Mycobacterium tuberculosis
2geu, downloadSCOP (2geu)CATH (2geu)Mycobacterium tuberculosis
2gev, downloadSCOP (2gev)CATH (2gev)Mycobacterium tuberculosis
2zs7, downloadSCOP (2zs7)CATH (2zs7)Mycobacterium tuberculosis
2zs8, downloadSCOP (2zs8)CATH (2zs8)Mycobacterium tuberculosis
2zs9, downloadSCOP (2zs9)CATH (2zs9)Mycobacterium tuberculosis
2zsa, downloadSCOP (2zsa)CATH (2zsa)Mycobacterium tuberculosis
2zsb, downloadSCOP (2zsb)CATH (2zsb)Mycobacterium tuberculosis
2zsd, downloadSCOP (2zsd)CATH (2zsd)Mycobacterium tuberculosis
2zse, downloadSCOP (2zse)CATH (2zse)Mycobacterium tuberculosis
2zsf, downloadSCOP (2zsf)CATH (2zsf)Mycobacterium tuberculosis
3aez, downloadSCOP (3aez)CATH (3aez)Mycobacterium tuberculosis
3af0, downloadSCOP (3af0)CATH (3af0)Mycobacterium tuberculosis
3af1, downloadSCOP (3af1)CATH (3af1)Mycobacterium tuberculosis
3af2, downloadSCOP (3af2)CATH (3af2)Mycobacterium tuberculosis
3af3, downloadSCOP (3af3)CATH (3af3)Mycobacterium tuberculosis
3af4, downloadSCOP (3af4)CATH (3af4)Mycobacterium tuberculosis
3avo, downloadSCOP (3avo)CATH (3avo)Mycobacterium tuberculosis
3avp, downloadSCOP (3avp)CATH (3avp)Mycobacterium tuberculosis
3avq, downloadSCOP (3avq)CATH (3avq)Mycobacterium tuberculosis
2f9t, downloadSCOP (2f9t)CATH (2f9t)Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
2f9w, downloadSCOP (2f9w)CATH (2f9w)Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
3bex, downloadSCOP (3bex)CATH (3bex)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
3bf1, downloadSCOP (3bf1)CATH (3bf1)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
3bf3, downloadSCOP (3bf3)CATH (3bf3)Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
36000-Escherichia coli-SDS-PAGE671767
36300-Escherichia coli-calculated from sequence of cDNA671767
45000-Corynebacterium ammoniagenes-gel filtration641389
48000-Homo sapiens-SDS-PAGE, mature protein671347
59000-Staphylococcus aureus-recombinant enzyme, gel filtration662408
99600-Arabidopsis thaliana-calculated from amino acid sequence676548

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
?Staphylococcus aureus-x * 29100, recombinant enzyme, six-His-tagged641398
?Drosophila melanogaster-x * 53000, SDS-PAGE, x * 56700, deduced from gene sequence641401
?Emericella nidulansO93921x * 46900, deduced from gene sequence641402
?Mycobacterium tuberculosis-x * 37500, recombinant enzyme, SDS-PAGE660631
?Homo sapiens-x * 48000, recombinant His/myc-tagged isozyme PanK2, SDS-PAGE, x * 63000, recombinant unprocessed PanK2, SDS-PAGE662687
?Picrophilus torridusQ6L2I5x * 33000 Da, SDS-PAGE704326
dimerEscherichia coli-crystal structure641396
dimerMus musculus-2 * 41100, isozyme Pank3, sequence calculation and gel filtration, 2 * 41600, isozyme Pank1beta, sequence calculation and gel filtration662406
dimerStaphylococcus aureus-2 * 29000, recombinant enzyme, SDS-PAGE662408
dimerHomo sapiens-molecular mass, 30.8-61.2 kDa, of diverse protein variants expressed from different plasmids in different systems, SDS-PAGE and gel filtration, overview662455
dimerThermotoga maritima-gel filtration, functional unit in solution674291
dimerPseudomonas aeruginosaQ9HWC1x-ray crystallography677154
dimerStaphylococcus aureusQ6G7I0x-ray crystallography677154
hexamerThermotoga maritima-X-ray crystallography, in the crystal form674291
homodimerEscherichia coli-2 * 36000, SDS-PAGE671053
monomerBacillus anthracisQ81VX4x-ray crystallography672234
additional informationEscherichia coliP0A6I3formation of a pantothenate kinase-ADP-pantothenate ternary complex, structure determination, pantothenate binding to the enzyme induces a significant conformational change in amino acids 243–263, which form a lid that folds over the open pantothenate binding groove662251

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
proteolytic modificationHomo sapiens-several isoforms of PanK2 are produced by sequential proteolytic cleavage, identification of cleavage sites for the mitochondrial processing peptidase, overview662687

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. 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 glycolBacillus anthracisQ81VX4672234
-Escherichia coli-641396, 686816
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 18°C, 1 week, X-ray diffraction structure determination and analysis at 2.2 A resolution, molecular modeling of N-alkylpantothenamides, growth-inhibitory anti-metabolitesEscherichia coliP0A6I3662251
sitting drop vapor diffusion method at 18°C, 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 18°C, homodimeric structures of the catalytic core of PanK3 in complex with acetyl-CoA. Crystallographic mapping of missense mutations associated with pantothenate kinase-associated neurodegeneration diseaseHomo sapiensQ8TE04, Q9H999687612
-Mycobacterium tuberculosis-686816, 701469
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 6.5Mycobacterium tuberculosisP63810671053
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 calculationsMycobacterium tuberculosis-660631
hanging drop vapour diffusion method using 28% (w/v) PEG 2000mM and 0.1M Bis-Tris (pH 6.5), at 18°CPseudomonas aeruginosaQ9HWC1677154
sitting drop vapour diffusion method using 28% (w/v) PEG 2 M and 0.1 M Bis-Tris (pH 6.5), at 18°CStaphylococcus aureusQ6G7I0677154
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 ADPThermotoga maritimaQ9WZY5685199
sitting drop vapour diffusion method with 15% polyethylene glycol 3350Thermotoga maritima-674291

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
6.5-Corynebacterium ammoniagenes-t1/2: 10 min at 30°C641389
7-Corynebacterium ammoniagenes-10 min stable at 30°C641389
7.5-Corynebacterium ammoniagenes-90% of activity retained after 10 min at 30°C641389
8-Corynebacterium ammoniagenes-80% of activity retained after 10 min at 30°C641389

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
30-Corynebacterium ammoniagenes-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 6.5641389
37-Corynebacterium ammoniagenes-10 min, 70% loss of activity641389
43-Corynebacterium ammoniagenes-10 min, inactivation641389
47-Escherichia coli-loses kinase activity at temperatures higher than 47°C671767

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
ATP and/or sucrose do not stabilizeCorynebacterium ammoniagenes-641389
ATP and/or sucrose stabilize during purificationRattus norvegicus-641387
considerably unstable independent of the degree of purityRattus norvegicus-641387
highly unstable upon purification, e.g. successive chromatographyRattus norvegicus-641391
thiol reducing agents stabilize enzyme in solutionRattus norvegicus-641391

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
4°C, 2 mg protein/ml in 0.01 M phosphate buffer, pH 7, inactivation within 4 daysCorynebacterium ammoniagenes-641389
-20°C, partially purified preparation, several monthsEscherichia coli-641393
-20°C, above 3 mg protein/ml, more than 1 weekRattus norvegicus-641387
-65°C, 3 mg partially purified protein/ml, at least 4 monthsRattus norvegicus-641391
4°C, above 3 mg protein/ml, 4 daysRattus norvegicus-641387
4°C, t1/2: 3 daysSpinacia oleracea-641388

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bacillus anthracis-706042
; Ni-NTA column chromatographyBacillus anthracisQ81VX4672234
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatographyBacillus subtilis-662369
-Corynebacterium ammoniagenes-641389
-Escherichia coli-701469
Ni-column chromatographyEscherichia coli-671767
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 chromatographyEscherichia coliP0A6I3662251
strain SJ16, partialEscherichia coli-641393
-Helicobacter pylori-685199
recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatographyHelicobacter pylorip37564662369
; Homo sapiensQ8TE04, Q9H999687612
His-tagged PanK2; HiTrap chelating HP column chromatography and Superdex 200 column gel filtrationHomo sapiens-676884
native enzyme partially by preparation of mitochondriaHomo sapiensQ9BZ23660712
recombinant His/myc-tagged isozyme PanK2 from mitochondria of QBI 293 cells by ion exchange and protein A affinity chromatography and gel filtrationHomo sapiens-662687
-Mycobacterium tuberculosis-686816, 701469
Ni-NTA metal affinity column chromatographyMycobacterium tuberculosisP63810671053
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatographyMycobacterium tuberculosis-660631
-Picrophilus torridusQ6L2I5704326
-Pseudomonas aeruginosaQ9HWC1677154
partialRattus norvegicus-4406
liver; partialSaccharomyces cerevisiae-4406
partial, presumably 2 isoformsSpinacia oleracea-641388
-Staphylococcus aureus-677154, 686816
recombinant enzyme, six-His-taggedStaphylococcus aureus-641398
recombinant His6-tagged from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtrationStaphylococcus aureus-662408
-Thermotoga maritimaQ9WZY5685199
nickel-nitrilotriacetic acid-agarose column chromatography and Resource Q column chromatographyThermotoga maritima-674291

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Bacillus anthracis-706042
; expressed in Escherichia coli strain C41(DE3)Bacillus anthracisQ81VX4672234
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)Bacillus subtilis-662369
-Drosophila melanogaster-641401, 703958
-Emericella nidulansO93921641402
gene coaA, expression in strain BL21(DE3)Escherichia coliP0A6I3662251
His-tag, expressed in Escherichia coli BL21 (DE3)Escherichia coli-701469
-Helicobacter pylori-685199
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)Helicobacter pylorip37564662369
-Homo sapiens-703958
; expressed in Escherichia coli BL21(DE3) cellsHomo sapiens-676884
expressed in Escherichia coli strain ts9Homo sapiens-671347
expression as a His-tagged fusion protein in Escherichia coli; expression as a His-tagged fusion protein in Escherichia coliHomo sapiensQ8TE04, Q9H999687612
expression of wild-type His/myc-tagged isozyme PanK2 and of mutant enzymes in mitochondria of QBI 293 cellsHomo sapiens-662687
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 enzymeHomo sapiensQ9BZ23660712
splice variant PanK2, expression of active PanK2 isozymes iPanK2, spPanK2, mPanK2 in HEK293T cells, in vitro transcription and translation of PanK2Homo sapiens-662455
-Mus musculus-641400, 673027, 686741
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 cellsMus musculus-662406
-Mycobacterium tuberculosis-677979, 686816, 701469
DNA and amino acid sequence determination and analysis, expression of the His-tagged in Escherichia coli strain BL21(DE3)Mycobacterium tuberculosis-660631
expressed in Escherichia coli BL21 (DE3) cellsMycobacterium tuberculosisP63810671053
expressed in Escherichia coliPicrophilus torridusQ6L2I5704326
-Pseudomonas aeruginosaQ9HWC1677154
expressed in Escherichia coliRattus norvegicusQ923S8675942
-Saccharomyces cerevisiae-703325
-Staphylococcus aureus-677154, 686816
gene coaA, expression of His6-tagged in Escherichia coli strain BL21(DE3)Staphylococcus aureus-662408
-Thermotoga maritimaQ9WZY5685199
expressed in Escherichia coli strain BL21(DE3)Thermotoga maritima-674291

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
F247VEscherichia coli-less than 50% of catalytic activity of wild type, feedback resistant641399
H177QEscherichia coli-less than 50% of catalytic activity of wild type, feedback resistant641399
L236FEscherichia coli-temperature-sensitive mutant, inactive above 39°C671767
R106AEscherichia coli-50% of catalytic activity of wild type, feedback resistant641399
R315CEscherichia coli-temperature-sensitive mutant, inactive above 39°C671767
S176LEscherichia coli-temperature-sensitive mutant, inactive above 39°C671767
A509VHomo sapiens-naturally occurring mutation, early onset in patients, 105% activity compared to the wild-type enzyme662455
E134GHomo sapiens-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 mutagenesis662687
G219VHomo sapiens-naturally occurring mutation, early and late onset in patients, 0.4% activity compared to the wild-type enzyme662455
G219VHomo sapiens-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 mutagenesis662687
G521RHomo sapiens-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 enzyme662455
G521RHomo sapiens-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 mutagenesis662687
G521RHomo sapiens-loss of enzyme activity671347
N404IHomo sapiens-naturally occurring mutation, early and late onset in patients, 83% activity compared to the wild-type enzyme662455
N500IHomo sapiens-naturally occurring mutation, early onset in patients, 3.9% activity compared to the wild-type enzyme662455
R264WHomo sapiens-naturally occurring mutation, early onset in patients, 58% activity compared to the wild-type enzyme662455
R286CHomo sapiens-naturally occurring mutation, early and late onset in patients, 176% activity compared to the wild-type enzyme662455
R532WHomo sapiens-naturally occurring mutation, early onset in patients, 95% activity compared to the wild-type enzyme662455
S351PHomo sapiens-naturally occurring mutation, early and late onset in patients, 78% activity compared to the wild-type enzyme662455
S471NHomo sapiens-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 mutagenesis662687
T234AHomo sapiens-naturally occurring mutation, early and late onset in patients, 112% activity compared to the wild-type enzyme662455
T234AHomo sapiens-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 mutagenesis662687
T327IHomo sapiens-naturally occurring mutation, early onset in patients, 91% activity compared to the wild-type enzyme662455
T528MHomo sapiens-naturally occurring mutation, early and late onset in patients, 146% activity compared to the wild-type enzyme662455
T528MHomo sapiens-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 mutagenesis662687
D101APseudomonas aeruginosaQ9HWC1reduced enzymatic activity677154
D121APseudomonas aeruginosaQ9HWC1reduced enzymatic activity677154
H156APseudomonas aeruginosaQ9HWC1slightly increased enzymatic activity677154
K13APseudomonas aeruginosaQ9HWC1reduced enzymatic activity677154
N9GPseudomonas aeruginosaQ9HWC1strongly reduced enzymatic activity677154
T157APseudomonas aeruginosaQ9HWC1reduced enzymatic activity677154
G351SSaccharomyces cerevisiae-temperature-sensitive phenotype703325
D6AStaphylococcus aureusQ6G7I0reduced enzymatic activity677154
E70AStaphylococcus aureusQ6G7I0reduced enzymatic activity677154
K13AStaphylococcus aureusQ6G7I0reduced enzymatic activity677154
L11AStaphylococcus aureusQ6G7I0reduced enzymatic activity677154
L263PStaphylococcus aureusQ6G7I0reduced enzymatic activity677154
T10AStaphylococcus aureusQ6G7I0reduced enzymatic activity677154
Y137AStaphylococcus aureusQ6G7I0reduced enzymatic activity677154
D105EThermotoga maritima-less than 6% activity of the wild type enzyme674291
D105NThermotoga maritima-less than 6% activity of the wild type enzyme674291
D125EThermotoga maritima-less than 6% activity of the wild type enzyme674291
D125NThermotoga maritima-less than 6% activity of the wild type enzyme674291
D6EThermotoga maritima-less than 6% activity of the wild type enzyme674291
D6NThermotoga maritima-less than 6% activity of the wild type enzyme674291
K224AHomo sapiens-site-directed mutagenesis, less than 0.2% activity compared to the wild-type enzyme662455
additional informationHomo sapiensQ9BZ23an allelic variant mislocates and thereby causes disease660712
additional informationHomo sapiens-several natural mutants with frame shifts show no activity, identification of mutants with mutations which introduce stop codons, overview662455
additional informationHomo sapiens-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 PanK2662687
additional informationHomo sapiens-two siblings with the adult-onset slowly progressive type of pantothenate kinase-associated neurodegeneration have the I346S mutation in pantothenate kinase-2705271
T528MHomo sapiens-no effect on PANK2 activity or stability671347
additional informationMus musculus-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, overview662406

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
synthesisEnterococcus faecalisQ839J7synthesis of (carboxyl-18O)phosphopantothenate702284
medicineHomo sapiens-neurodegeneration with brain iron accumulation is a heterogenous group of disorder. One group of patiens bears mutations in the gene encoding pantothenate kinase 2684227
medicineHomo sapiens-the cognitive deterioration in pantothenate kinase-associated neurodegeneration dystonia has been overemphasised and many of the apparent disabilities are more a consequence of the dystonia684736
medicineHomo sapiens-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 dystonia686546
medicineHomo sapiens-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 inheritance687016
medicineHomo sapiens-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 neurodegeneration687943
medicineHomo sapiens-pantothenate kinase-associated neurodegeneration is a neurodegenerative condition with a broad phenotypic spectrum688202
medicineHomo sapiens-patient with pantothenate kinase-associated neurodegeneration whose dystonia and freezing of gait respond dramatically to anticholinergic treatment689108
medicineHomo sapiens-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; 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 years689128
medicineHomo sapiens-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 reported689334
medicineHomo sapiens-pallidal stimulation for dystonia in pantothenate kinase associated neurodegeneration689335
medicineHomo sapiens-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 A690019
medicineMus musculus-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 disease688176

DISEASETITLE OF PUBLICATIONLINK TO PUBMED
AbetalipoproteinemiaCompound heterozygous PANK2 mutations confirm HARP and Hallervorden-Spatz syndromes are allelic. PubMed
Anemia, Sideroblastic[Genetics of hereditary iron overload] PubMed
AzoospermiaDeficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia. PubMed
AzoospermiaDeprivation of pantothenic acid elicits a movement disorder and azoospermia in a mouse model of pantothenate kinase-associated neurodegeneration. PubMed
AzoospermiaPantothenate kinase-associated neurodegeneration: altered mitochondria membrane potential and defective respiration in Pank2 knock-out mouse model. PubMed
Basal Ganglia DiseasesNeurodegeneration with brain iron accumulation. PubMed
Brain DiseasesPantothenate kinase-associated neurodegeneration in two Chinese children: identification of a novel PANK2 gene mutation. PubMed
Carcinoma, HepatocellularPantothenate kinase-2 (Pank2) silencing causes cell growth reduction, cell-specific ferroportin upregulation and iron deregulation. PubMed
Cerebellar AtaxiaPANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA) but mutations are rare in other types of adult neurodegenerative disease. PubMed
Deglutition DisordersDeficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia. PubMed
DysarthriaClinical heterogeneity of neurodegeneration with brain iron accumulation (Hallervorden-Spatz syndrome) and pantothenate kinase-associated neurodegeneration. PubMed
Dyskinesias[Tourettism, hemiballism and juvenile Parkinsonism: expanding the clinical spectrum of the neurodegeneration associated to pantothenate kinase deficiency (Hallervorden Spatz syndrome)] PubMed
DystoniaA novel PANK2 gene mutation with sudden-onset dystonia. PubMed
DystoniaCharacterization of the human PANK2 promoter. PubMed
DystoniaClinical heterogeneity of neurodegeneration with brain iron accumulation (Hallervorden-Spatz syndrome) and pantothenate kinase-associated neurodegeneration. PubMed
DystoniaFocal hand dystonia in a patient with PANK2 mutation. PubMed
DystoniaLow prevalence of PANK2 mutations in Brazilian patients with early onset generalised dystonia and basal ganglia abnormalities on MRI. PubMed
DystoniaPANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA) but mutations are rare in other types of adult neurodegenerative disease. PubMed
DystoniaPyruvate dehydrogenase E2 deficiency: A potentially treatable cause of episodic dystonia. PubMed
DystoniaRare causes of dystonia parkinsonism. PubMed
DystoniaUnraveling the Hallervorden-Spatz syndrome: pantothenate kinase-associated neurodegeneration is the name. PubMed
Dystonia[Anesthesia considerations for deep-brain stimulation in a patient with type-2 pantothenate kinase deficiency (Hallervorden-Spatz disease)] PubMed
Friedreich AtaxiaNeurodegeneration with brain iron accumulation - Clinical syndromes and neuroimaging. PubMed
Friedreich Ataxia[Genetics of hereditary iron overload] PubMed
Genetic Diseases, InbornIron toxicity as a potential factor in AMD. PubMed
GliomaPantothenate kinase-2 (Pank2) silencing causes cell growth reduction, cell-specific ferroportin upregulation and iron deregulation. PubMed
HepatoblastomaPPARalpha controls the intracellular coenzyme A concentration via regulation of PANK1alpha gene expression. PubMed
Hepatolenticular DegenerationRare causes of dystonia parkinsonism. PubMed
HypolipoproteinemiasCompound heterozygous PANK2 mutations confirm HARP and Hallervorden-Spatz syndromes are allelic. PubMed
InfectionPantothenic acid metabolism during avian malaria infection: pantothenate kinase activity in duck erythrocytes and in Plasmodium lophurae. PubMed
Infertility, MalePantothenate kinase-associated neurodegeneration: insights from a Drosophila model. PubMed
Intellectual DisabilityPANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA) but mutations are rare in other types of adult neurodegenerative disease. PubMed
Iron OverloadIron toxicity as a potential factor in AMD. PubMed
Iron Overload[Genetics of hereditary iron overload] PubMed
Learning DisordersPyruvate dehydrogenase E2 deficiency: A potentially treatable cause of episodic dystonia. PubMed
Macular DegenerationIron toxicity as a potential factor in AMD. PubMed
MalariaA class of pantothenic acid analogs inhibits Plasmodium falciparum pantothenate kinase and represses the proliferation of malaria parasites. PubMed
MalariaFeedback inhibition of pantothenate kinase regulates pantothenol uptake by the malaria parasite. PubMed
Malaria, AvianPantothenic acid metabolism during avian malaria infection: pantothenate kinase activity in duck erythrocytes and in Plasmodium lophurae. PubMed
Malaria, AvianTransport and metabolism of the essential vitamin pantothenic acid in human erythrocytes infected with the malaria parasite Plasmodium falciparum. PubMed
Movement DisordersDeprivation of pantothenic acid elicits a movement disorder and azoospermia in a mouse model of pantothenate kinase-associated neurodegeneration. PubMed
Movement DisordersHereditary parkinsonism: Parkinson disease look-alikes-An algorithm for clinicians to 'PARK' genes and beyond. PubMed
Movement DisordersPANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA) but mutations are rare in other types of adult neurodegenerative disease. PubMed
Movement DisordersPantothenate kinase-2 (Pank2) silencing causes cell growth reduction, cell-specific ferroportin upregulation and iron deregulation. PubMed
Movement DisordersSiblings with the adult-onset slowly progressive type of pantothenate kinase-associated neurodegeneration and a novel mutation, Ile346Ser, in PANK2: clinical features and (99m)Tc-ECD brain perfusion SPECT findings. PubMed
Movement DisordersThe 'eye of the tiger' sign in pure akinesia with gait freezing. PubMed
Nervous System DiseasesDeprivation of pantothenic acid elicits a movement disorder and azoospermia in a mouse model of pantothenate kinase-associated neurodegeneration. PubMed
Neuroaxonal DystrophiesIron Accumulation in Syndromes of Neurodegeneration with Brain Iron Accumulation 1 and 2 - causative or consequential? PubMed
Neuroaxonal DystrophiesNeurodegeneration with brain iron accumulation - Clinical syndromes and neuroimaging. PubMed
Neuroaxonal DystrophiesNeurodegeneration with brain iron accumulation. PubMed
Neuroaxonal DystrophiesWidespread Lewy body and tau accumulation in childhood and adult onset dystonia-parkinsonism cases with PLA2G6 mutations. PubMed
NeuroblastomaPantothenate kinase-2 (Pank2) silencing causes cell growth reduction, cell-specific ferroportin upregulation and iron deregulation. PubMed
Neurodegenerative DiseasesActivation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine. PubMed
Neurodegenerative DiseasesCoenzyme A: back in action. PubMed
Neurodegenerative DiseasesCofilin/Twinstar phosphorylation levels increase in response to impaired coenzyme a metabolism. PubMed
Neurodegenerative DiseasesEarly-onset neurodegeneration with brain iron accumulation due to PANK2 mutation. PubMed
Neurodegenerative DiseasesHereditary causes of disturbed iron homeostasis in the central nervous system. PubMed
Neurodegenerative DiseasesPANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA) but mutations are rare in other types of adult neurodegenerative disease. PubMed
Neurodegenerative DiseasesPantethine rescues a Drosophila model for pantothenate kinase-associated neurodegeneration. PubMed
Neurodegenerative DiseasesRare causes of hereditary iron overload. PubMed
Neurologic ManifestationsDeprivation of pantothenic acid elicits a movement disorder and azoospermia in a mouse model of pantothenate kinase-associated neurodegeneration. PubMed
pantothenate kinase deficiencyLocalization and regulation of mouse pantothenate kinase 2. PubMed
pantothenate kinase deficiencySkin fibroblasts from pantothenate kinase-associated neurodegeneration patients show altered cellular oxidative status and have defective iron-handling properties. PubMed
pantothenate kinase deficiency[Anesthesia considerations for deep-brain stimulation in a patient with type-2 pantothenate kinase deficiency (Hallervorden-Spatz disease)] PubMed
pantothenate kinase deficiency[Tourettism, hemiballism and juvenile Parkinsonism: expanding the clinical spectrum of the neurodegeneration associated to pantothenate kinase deficiency (Hallervorden Spatz syndrome)] PubMed
Pantothenate Kinase-Associated Neurodegeneration'Eye-of-the-Tiger' Sign and Classic Pantothenate Kinase Associated Neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationA novel 3-bp deletion in the PANK2 gene of Dutch patients with pantothenate kinase-associated neurodegeneration: evidence for a founder effect. PubMed
Pantothenate Kinase-Associated NeurodegenerationA novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. PubMed
Pantothenate Kinase-Associated NeurodegenerationAbsence of an orphan mitochondrial protein, c19orf12, causes a distinct clinical subtype of neurodegeneration with brain iron accumulation. PubMed
Pantothenate Kinase-Associated NeurodegenerationAn isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria. PubMed
Pantothenate Kinase-Associated NeurodegenerationAnticholinergic-responsive gait freezing in a patient with pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationAtypical Hallervorden-Spatz disease with preserved cognition and obtrusive obsessions and compulsions. PubMed
Pantothenate Kinase-Associated NeurodegenerationBiochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationCase report: MR spectroscopy in pantothenate kinase-2 associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationCharacterization of the human PANK2 promoter. PubMed
Pantothenate Kinase-Associated NeurodegenerationChildhood disorders of neurodegeneration with brain iron accumulation (NBIA). PubMed
Pantothenate Kinase-Associated NeurodegenerationClinical and genetic delineation of neurodegeneration with brain iron accumulation. PubMed
Pantothenate Kinase-Associated NeurodegenerationClinical heterogeneity of neurodegeneration with brain iron accumulation (Hallervorden-Spatz syndrome) and pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationConversion disorder as initial diagnosis in pantothenate kinase associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationDe novo CoA biosynthesis is required to maintain DNA integrity during development of the Drosophila nervous system. PubMed
Pantothenate Kinase-Associated NeurodegenerationDeep Brain Stimulation in Pantothenate Kinase Associated Neurodegeneration: challenges for the future. PubMed
Pantothenate Kinase-Associated NeurodegenerationEarly-onset neurodegeneration with brain iron accumulation due to PANK2 mutation. PubMed
Pantothenate Kinase-Associated NeurodegenerationEfficacy of botulinum toxin A treatment in a case of pantothenate kinase associated neurodegeneration (PKAN). PubMed
Pantothenate Kinase-Associated NeurodegenerationFirst cases in the Czech Republic of the Hallervorden-Spatz disease resulting from mutation in the pantothenate kinase 2 gene. PubMed
Pantothenate Kinase-Associated NeurodegenerationGene symbol: PANK2. Disease: Pantothenate kinase associated neurodegeneration (PKAN). PubMed,  PubMed
Pantothenate Kinase-Associated NeurodegenerationGene symbol: PANK2. Disease: pantothenate kinase-associated neurodegeneration (PKAN). PubMed,  PubMed,  PubMed,  PubMed,  PubMed,  PubMed,  PubMed,  PubMed,  PubMed,  PubMed,  PubMed
Pantothenate Kinase-Associated NeurodegenerationGenetic, clinical, and radiographic delineation of Hallervorden-Spatz syndrome. PubMed
Pantothenate Kinase-Associated NeurodegenerationHallervorden-Spatz syndrome. PubMed
Pantothenate Kinase-Associated NeurodegenerationHereditary causes of disturbed iron homeostasis in the central nervous system. PubMed
Pantothenate Kinase-Associated NeurodegenerationImpaired Coenzyme A metabolism affects histone and tubulin acetylation in Drosophila and human cell models of pantothenate kinase associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationInfluence of the Plant Extract Complex 'AdMax' on Global Gene Expression Levels in Cultured Human Fibroblasts. PubMed
Pantothenate Kinase-Associated NeurodegenerationIron Accumulation in Syndromes of Neurodegeneration with Brain Iron Accumulation 1 and 2 - causative or consequential? PubMed
Pantothenate Kinase-Associated NeurodegenerationIron toxicity as a potential factor in AMD. PubMed
Pantothenate Kinase-Associated NeurodegenerationMissense PANK2 mutation without 'Eye of the tiger' sign: MR findings in a large group of patients with pantothenate kinase-associated neurodegeneration (PKAN). PubMed
Pantothenate Kinase-Associated NeurodegenerationMitochondrial localization of human PANK2 and hypotheses of secondary iron accumulation in pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationNeuroacanthocytosis: new developments in a neglected group of dementing disorders. PubMed
Pantothenate Kinase-Associated NeurodegenerationNeurodegeneration with brain iron accumulation. PubMed,  PubMed
Pantothenate Kinase-Associated NeurodegenerationNeurodegeneration with brain iron accumulation: A cautionary tale. PubMed
Pantothenate Kinase-Associated NeurodegenerationNovel compound heterozygous mutations in the PANK2 gene in a Chinese patient with atypical pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationNovel histopathologic findings in molecularly-confirmed pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationNovel mutation in the PANK2 gene leads to pantothenate kinase-associated neurodegeneration in a Pakistani family. PubMed
Pantothenate Kinase-Associated NeurodegenerationNovel PANK2 gene mutations in korean patient with pantothenate kinase-associated neurodegeneration presenting unilateral dystonic tremor. PubMed
Pantothenate Kinase-Associated NeurodegenerationNovel PANK2 gene mutations in two Chinese siblings with atypical pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationPANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA) but mutations are rare in other types of adult neurodegenerative disease. PubMed
Pantothenate Kinase-Associated NeurodegenerationPANK2 mutation screening recommended to confirm diagnosis of pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantethine rescues a Drosophila model for pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase associated neurodegeneration (Hallervorden-Spatz syndrome). PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase-associated neurodegeneration (PKAN): molecular confirmation of a Turkish patient with a rare frameshift mutation in the coding region of the PANK2 gene. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase-associated neurodegeneration in Korea: recurrent R440P mutation in PANK2 and outcome of deep brain stimulation. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase-associated neurodegeneration in two Chinese children: identification of a novel PANK2 gene mutation. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase-associated neurodegeneration in two Taiwanese siblings: identification of a novel PANK2 gene mutation. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase-associated neurodegeneration initially presenting as postural tremor alone in a Japanese family with homozygous N245S substitutions in the pantothenate kinase gene. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase-associated neurodegeneration is not a synucleinopathy. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase-associated neurodegeneration: altered mitochondria membrane potential and defective respiration in Pank2 knock-out mouse model. PubMed
Pantothenate Kinase-Associated NeurodegenerationPantothenate kinase-associated neurodegeneration: novel mutations in the PANK2 gene in an Argentinean young woman. PubMed
Pantothenate Kinase-Associated NeurodegenerationPyruvate dehydrogenase E2 deficiency: A potentially treatable cause of episodic dystonia. PubMed
Pantothenate Kinase-Associated NeurodegenerationRare causes of hereditary iron overload. PubMed
Pantothenate Kinase-Associated NeurodegenerationSiblings with the adult-onset slowly progressive type of pantothenate kinase-associated neurodegeneration and a novel mutation, Ile346Ser, in PANK2: clinical features and (99m)Tc-ECD brain perfusion SPECT findings. PubMed
Pantothenate Kinase-Associated NeurodegenerationThe 'Eye-of-the-Tiger' Sign may be Absent in the Early Stages of Classic Pantothenate Kinase Associated Neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationThe diverse phenotype and genotype of pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated NeurodegenerationThe eye-of-the-tiger sign is not a reliable disease marker for Hallervorden-Spatz syndrome. PubMed
Pantothenate Kinase-Associated NeurodegenerationTranscranial sonography in pantothenate kinase-associated neurodegeneration. PubMed
Pantothenate Kinase-Associated Neurodegeneration[123I]FP-CIT SPECT findings in two patients with Hallervorden-Spatz disease with homozygous mutation in PANK2 gene. PubMed
Pantothenate Kinase-Associated Neurodegeneration[Clinical manifestations and detection of pantothenate kinase 2 gene mutation in a patient with Hallervorden-Spatz syndrome] PubMed
Pantothenate Kinase-Associated Neurodegeneration[Genetics of hereditary iron overload] PubMed
Pantothenate Kinase-Associated Neurodegeneration[Studies on PANK2 gene mutations in Chinese patients with Hallervorden-Spatz syndrome] PubMed
ParaplegiaRare causes of dystonia parkinsonism. PubMed
Parkinson DiseaseMutations in the pantothenate kinase gene PANK2 are not associated with Parkinson disease. PubMed
Parkinsonian DisordersA Novel PANK2 Mutation in a Patient with Atypical Pantothenate-Kinase-Associated Neurodegeneration Presenting with Adult-Onset Parkinsonism. PubMed
Parkinsonian DisordersNeurodegeneration with brain iron accumulation: clinical, radiographic and genetic heterogeneity and corresponding therapeutic options. PubMed
Parkinsonian DisordersPANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA) but mutations are rare in other types of adult neurodegenerative disease. PubMed
Parkinsonian DisordersRare causes of dystonia parkinsonism. PubMed
Parkinsonian DisordersYoung-onset parkinsonism in a Hong Kong Chinese man with adult-onset Hallervorden-Spatz syndrome. PubMed
Parkinsonian Disorders[Tourettism, hemiballism and juvenile Parkinsonism: expanding the clinical spectrum of the neurodegeneration associated to pantothenate kinase deficiency (Hallervorden Spatz syndrome)] PubMed
Protein Deficiency[Anesthesia considerations for deep-brain stimulation in a patient with type-2 pantothenate kinase deficiency (Hallervorden-Spatz disease)] PubMed
Retinal DegenerationDeficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia. PubMed
Retinal DegenerationIron toxicity as a potential factor in AMD. PubMed
Retinal DegenerationPantothenate kinase-associated neurodegeneration: altered mitochondria membrane potential and defective respiration in Pank2 knock-out mouse model. PubMed
Retinal TelangiectasisNovel mutation in PANK2 associated with retinal telangiectasis. PubMed
Retinitis PigmentosaCharacterization of the human PANK2 promoter. PubMed
Retinitis PigmentosaCompound heterozygous PANK2 mutations confirm HARP and Hallervorden-Spatz syndromes are allelic. PubMed
Retinitis PigmentosaPANK2 gene analysis confirms genetic heterogeneity in neurodegeneration with brain iron accumulation (NBIA) but mutations are rare in other types of adult neurodegenerative disease. PubMed
Retinitis PigmentosaUnraveling the Hallervorden-Spatz syndrome: pantothenate kinase-associated neurodegeneration is the name. PubMed
SiderosisIron toxicity as a potential factor in AMD. PubMed
Staphylococcal InfectionsInhibitors of pantothenate kinase: novel antibiotics for staphylococcal infections. PubMed
TremorA Novel PANK2 Mutation in a Patient with Atypical Pantothenate-Kinase-Associated Neurodegeneration Presenting with Adult-Onset Parkinsonism. PubMed
TremorNovel PANK2 gene mutations in korean patient with pantothenate kinase-associated neurodegeneration presenting unilateral dystonic tremor. PubMed
TremorPantothenate kinase-associated neurodegeneration initially presenting as postural tremor alone in a Japanese family with homozygous N245S substitutions in the pantothenate kinase gene. PubMed
TuberculosisEssentiality and functional analysis of type I and type III pantothenate kinases of Mycobacterium tuberculosis. PubMed
TuberculosisExpression, purification, crystallization and preliminary X-ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosis. PubMed
TuberculosisLocation and conformation of pantothenate and its derivatives in Mycobacterium tuberculosis pantothenate kinase: insights into enzyme action. PubMed
TuberculosisM. tuberculosis pantothenate kinase: dual substrate specificity and unusual changes in ligand locations. PubMed
TuberculosisMycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme action. PubMed
TuberculosisScreening, identification, and characterization of mechanistically diverse inhibitors of the Mycobacterium tuberculosis enzyme, pantothenate kinase (CoaA). PubMed
Whooping CoughCrystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria. PubMed

REF. AUTHORS TITLE JOURNAL VOL. PAGES YEAR ORGANISMLINK TO PUBMEDSOURCE
4406Brown, G.M.The metabolism of pantothenic acidJ. Biol. Chem.234370-3781959Escherichia coli, Lactobacillus plantarum, Morganella morganii, no activity in Lactobacillus helveticus, no activity in Neurospora crassa, Rattus norvegicus, Saccharomyces cerevisiae PubMed
4412Nishimura, N.; Kakimoto, T.; Chibata, I.Mechanism of coenzyme A biosynthesis by Sarcina luteaJ. Ferment. Technol.6195-991983Micrococcus luteus-
641387Abiko, Y.; Ashida, S.I.; Shimizu, M.Purification and properties of D-pantothenate kinase from rat liverBiochim. Biophys. Acta268364-3721972Rattus norvegicus PubMed
641388Falk, K.L.; Guerra, D.J.Coenzyme A biosynthesis in plants: partial purification and characterization of pantothenate kinase from spinachArch. Biochem. Biophys.301424-4301993Brassica napus, Spinacia oleracea PubMed
641389Shimizu, S.; Kubo, K.; Tani, Y.; Ogata, K.Purification and properties of pantothenate kinase from brevibacterium ammoniagenes IFO 12071Agric. Biol. Chem.372863-28701973Corynebacterium ammoniagenes-
641390Halvorsen, O.; Skrede, S.Regulation of the biosynthesis of CoA at the level of pantothenate kinaseEur. J. Biochem.124211-2151982Rattus norvegicus PubMed
641391Fisher, M.N.; Robishaw, J.D.; Neely, J.R.The properties and regulation of pantothenate kinase from rat heartJ. Biol. Chem.26015745-157511985Rattus norvegicus PubMed
641392Fisher, M.N.; Neely, J.R.Regulation of pantothenate kinase from various tissues of the ratFEBS Lett.190293-2961985Rattus norvegicus PubMed
641393Vallari, D.S.; Jackowski, S.; Rock, C.O.Regulation of pantothenate kinase by coenzyme A and its thioestersJ. Biol. Chem.2622468-24711987Escherichia coli PubMed
641394Halvorsen, O.; Tverdal, S.Multiple molecular forms of rat liver pantothenate kinaseScand. J. Clin. Lab. Invest.4667-701986Rattus norvegicus-
641396Yun, M.; Park, C.G.; Kim, J.Y.; Rock, C.O.; Jackowski, S.; Park, H.W.Structural basis for the feedback regulation of Escherichia coli pantothenate kinase by coenzyme AJ. Biol. Chem.27528093-280992000Escherichia coli PubMed
641397Rock, C.O.; Calder, R.B.; Karim, M.A.; Jackowski, S.Pantothenate kinase regulation of the intracellular concentration of coenzyme AJ. Biol. Chem.2751377-13832000Mus musculus PubMed
641398Choudhry, A.E.; Mandichak, T.L.; Broskey, J.P.; Egolf, R.W.; Kinsland, C.; Begley, T.P.; Seefeld, M.A.; Ku, T.W.; Brown, J.R.; Zalacain, M.; Ratnam, K.Inhibitors of pantothenate kinase: novel antibiotics for staphylococcal infectionsAntimicrob. Agents Chemother.472051-20552003Staphylococcus aureus PubMed
641399Rock, C.O.; Park, H.W.; Jackowski, S.Role of feedback regulation of pantothenate kinase (CoaA) in control of coenzyme A levels in Escherichia coliJ. Bacteriol.1853410-34152003Escherichia coli PubMed
641400Rock, C.O.; Karim, M.A.; Zhang, Y.M.; Jackowski, S.The murine pantothenate kinase (Pank1) gene encodes two differentially regulated pantothenate kinase isozymesGene29135-432002Mus musculus PubMed
641401Afshar, K.; Gonczy, P.; DiNardo, S.; Wasserman, S.A.Fumble encodes a pantothenate kinase homolog required for proper mitosis and meiosis in Drosophila melanogasterGenetics1571267-12762001Drosophila melanogaster PubMed
641402Calder, R.B.; Williams, R.S.; Ramaswamy, G.; Rock, C.O.; Campbell, E.; Unkles, S.E.; Kinghorn, J.R.; Jackowski, S.Cloning and characterization of a eukaryotic pantothenate kinase gene (panK) from Aspergillus nidulansJ. Biol. Chem.2742014-20201999Emericella nidulans PubMed
660631Das, S.; Kumar, P.; Bhor, V.; Surolia, A.; Vijayan, M.Expression, purification, crystallization and preliminary X-ray crystallographic analysis of pantothenate kinase from Mycobacterium tuberculosisActa Crystallogr. Sect. FF6165-672005Mycobacterium tuberculosis PubMed
660712Johnson, M.A.; Kuo, Y.M.; Westaway, S.K.; Parker, S.M.; Ching, K.H.; Gitschier, J.; Hayflick, S.J.Mitochondrial localization of human PANK2 and hypotheses of secondary iron accumulation in pantothenate kinase-associated neurodegenerationAnn. N.Y. Acad. Sci.1012282-2982004Homo sapiens PubMed
660726Spry, C.; Chai, C.L.; Kirk, K.; Saliba, K.J.A class of pantothenic acid analogs inhibits Plasmodium falciparum pantothenate kinase and represses the proliferation of malaria parasitesAntimicrob. Agents Chemother.494649-46572005Homo sapiens, Plasmodium falciparum PubMed
661331Virga, K.G.; Zhang, Y.M.; Leonardi, R.; Ivey, R.A.; Hevener, K.; Park, H.W.; Jackowski, S.; Rock, C.O.; Lee, R.E.Structure-activity relationships and enzyme inhibition of pantothenamide-type pantothenate kinase inhibitorsBioorg. Med. Chem.141007-10202006Emericella nidulans, Escherichia coli, Mus musculus, Staphylococcus aureus PubMed
662251Ivey, R.A.; Zhang, Y.M.; Virga, K.G.; Hevener, K.; Lee, R.E.; Rock, C.O.; Jackowski, S.; Park, H.W.The structure of the pantothenate kinase-ADP-pantothenate ternary complex reveals the relationship between the binding sites for substrate, allosteric regulator, and antimetabolitesJ. Biol. Chem.27935622-356292004Escherichia coli PubMed
662369Brand, L.A.; Strauss, E.Characterization of a new pantothenate kinase isoform from Helicobacter pyloriJ. Biol. Chem.28020185-201882005Bacillus subtilis, Helicobacter pylori PubMed
662406Zhang, Y.M.; Rock, C.O.; Jackowski, S.Feedback regulation of murine pantothenate kinase 3 by coenzyme A and coenzyme A thioestersJ. Biol. Chem.28032594-326012005Mus musculus PubMed
662408Leonardi, R.; Chohnan, S.; Zhang, Y.M.; Virga, K.G.; Lee, R.E.; Rock, C.O.; Jackowski, S.A pantothenate kinase from Staphylococcus aureus refractory to feedback regulation by coenzyme AJ. Biol. Chem.2803314-33222005Staphylococcus aureus PubMed
662455Zhang, Y.M.; Rock, C.O.; Jackowski, S.Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegenerationJ. Biol. Chem.281107-1142006Homo sapiens PubMed
662687Kotzbauer, P.T.; Truax, A.C.; Trojanowski, J.Q.; Lee, V.M.Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused by abnormal processing, stability, and catalytic activity of mutant pantothenate kinase 2J. Neurosci.25689-6982005Homo sapiens PubMed
671053Das, S.; Kumar, P.; Bhor, V.; Surolia, A.; Vijayan, M.Invariance and variability in bacterial PanK: a study based on the crystal structure of Mycobacterium tuberculosis PanKActa Crystallogr. Sect. D62628-6382006Escherichia coli, Mycobacterium tuberculosis PubMed
671347Hartig, M.B.; Hoertnagel, K.; Garavaglia, B.; Zorzi, G.; Kmiec, T.; Klopstock, T.; Rostasy, K.; Svetel, M.; Kostic, V.S.; Schuelke, M.; Botz, E.; Weindl, A.; Novakovic, I.; Nardocci, N.; Prokisch, H.; Meitinger, T.Genotypic and phenotypic spectrum of PANK2 mutations in patients with neurodegeneration with brain iron accumulationAnn. Neurol.59248-2562006Homo sapiens PubMed
671767Chen, X.; Shen, D.; Zhou, B.Analysis of the temperature-sensitive mutation of Escherichia coli pantothenate kinase reveals YbjN as a possible protein stabilizerBiochem. Biophys. Res. Commun.345834-8422006Escherichia coli PubMed
672234Nicely, N.I.; Parsonage, D.; Paige, C.; Newton, G.L.; Fahey, R.C.; Leonardi, R.; Jackowski, S.; Mallett, T.C.; Claiborne, A.Structure of the type III pantothenate kinase from Bacillus anthracis at 2.0 A resolution: implications for coenzyme A-dependent redox biologyBiochemistry463234-32452007Bacillus anthracis PubMed
673027Zhang, Y.M.; Chohnan, S.; Virga, K.G.; Stevens, R.D.; Ilkayeva, O.R.; Wenner, B.R.; Bain, J.R.; Newgard, C.B.; Lee, R.E.; Rock, C.O.; Jackowski, S.Chemical knockout of pantothenate kinase reveals the metabolic and genetic program responsible for hepatic coenzyme A homeostasisChem. Biol.14291-3022007Mus musculus PubMed
674291Yang, K.; Eyobo, Y.; Brand, L.A.; Martynowski, D.; Tomchick, D.; Strauss, E.; Zhang, H.Crystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteriaJ. Bacteriol.1885532-55402006Thermotoga maritima PubMed
674852Lehane, A.M.; Marchetti, R.V.; Spry, C.; van Schalkwyk, D.A.; Teng, R.; Kirk, K.; Saliba, K.J.Feedback inhibition of pantothenate kinase regulates pantothenol uptake by the malaria parasiteJ. Biol. Chem.28225395-254052007Plasmodium falciparum PubMed
675942Li, Y.; Chang, Y.; Zhang, L.; Feng, Q.; Liu, Z.; Zhang, Y.; Zuo, J.; Meng, Y.; Fang, F.High glucose upregulates pantothenate kinase 4 (PanK4) and thus affects M2-type pyruvate kinase (Pkm2)Mol. Cell. Biochem.277117-1252005Rattus norvegicus PubMed
676548Tilton, G.B.; Wedemeyer, W.J.; Browse, J.; Ohlrogge, J.Plant coenzyme A biosynthesis: characterization of two pantothenate kinases from ArabidopsisPlant Mol. Biol.61629-6422006Arabidopsis thaliana PubMed
676884Leonardi, R.; Rock, C.O.; Jackowski, S.; Zhang, Y.M.Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitineProc. Natl. Acad. Sci. USA1041494-14992007Homo sapiens PubMed
677154Hong, B.S.; Yun, M.K.; Zhang, Y.M.; Chohnan, S.; Rock, C.O.; White, S.W.; Jackowski, S.; Park, H.W.; Leonardi, R.Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic propertiesStructure141251-12612006Pseudomonas aeruginosa, Staphylococcus aureus PubMed
677979Kumar, P.; Chhibber, M.; Surolia, A.How pantothenol intervenes in coenzyme-A biosynthesis of Mycobacterium tuberculosisBiochem. Biophys. Res. Commun.361903-9092007Mycobacterium tuberculosis PubMed
684227Clement, F.; Devos, D.; Moreau, C.; Coubes, P.; Destee, A.; Defebvre, L.Neurodegeneration with brain iron accumulation: clinical, radiographic and genetic heterogeneity and corresponding therapeutic optionsActa Neurol. Belg.10726-312007Homo sapiens PubMed
684736Isaac, C.; Wright, I.; Bhattacharyya, D.; Baxter, P.; Rowe, J.Pallidal stimulation for pantothenate kinase-associated neurodegeneration dystoniaArch. Dis. Child.93239-2402008Homo sapiens PubMed
685199Yang, K.; Strauss, E.; Huerta, C.; Zhang, H.Structural basis for substrate binding and the catalytic mechanism of type III pantothenate kinaseBiochemistry471369-13802008Helicobacter pylori, Thermotoga maritima PubMed
686546Mikati, M.A.; Yehya, A.; Darwish, H.; Karam, P.; Comair, Y.Deep brain stimulation as a mode of treatment of early onset pantothenate kinase-associated neurodegenerationEur. J. Paediatr. Neurol.1361-642008Homo sapiens PubMed
686741Leonardi, R.; Zhang, Y.M.; Lykidis, A.; Rock, C.O.; Jackowski, S.Localization and regulation of mouse pantothenate kinase 2FEBS Lett.5814639-46442007Homo sapiens, Mus musculus PubMed
686816Spry, C.; Kirk, K.; Saliba, K.J.Coenzyme A biosynthesis: an antimicrobial drug targetFEMS Microbiol. Rev.3256-1062008Escherichia coli, Mycobacterium tuberculosis, Staphylococcus aureus PubMed
687016Chan, K.Y.; Lam, C.W.; Lee, L.P.; Tong, S.F.; Yuen, Y.P.Pantothenate kinase-associated neurodegeneration in two Chinese children: identification of a novel PANK2 gene mutationHong Kong Med. J.1470-732008Homo sapiens PubMed
687036Bosveld, F.; Rana, A.; van der Wouden, P.E.; Lemstra, W.; Ritsema, M.; Kampinga, H.H.; Sibon, O.C.De novo CoA biosynthesis is required to maintain DNA integrity during development of the Drosophila nervous systemHum. Mol. Genet.172058-20692008Drosophila sp. PubMed
687425Paige, C.; Reid, S.D.; Hanna, P.C.; Claiborne, A.The type III pantothenate kinase encoded by coaX is essential for growth of Bacillus anthracisJ. Bacteriol.1906271-62752008Bacillus anthracis PubMed
687612Hong, B.S.; Senisterra, G.; Rabeh, W.M.; Vedadi, M.; Leonardi, R.; Zhang, Y.M.; Rock, C.O.; Jackowski, S.; Park, H.W.Crystal structures of human pantothenate kinases. Insights into allosteric regulation and mutations linked to a neurodegeneration disorderJ. Biol. Chem.28227984-279932007Homo sapiens PubMed
687943Kazek, B.; Jamroz, E.; Gencik, M.; Jezela Stanek, A.; Marszal, E.; Wojaczynska-Stanek, K.A novel PANK2 gene mutation: clinical and molecular characteristics of patients short communicationJ. Child Neurol.221256-12592007Homo sapiens PubMed
688109Ellers, J.; Marien, J.; Driessen, G.; van Straalen, N.M.Temperature-induced gene expression associated with different thermal reaction norms for growth rateJ. Exp. Zool. B Mol. Dev. Evol.310137-1472008Orchesella cincta PubMed
688176Kuo, Y.M.; Hayflick, S.J.; Gitschier, J.Deprivation of pantothenic acid elicits a movement disorder and azoospermia in a mouse model of pantothenate kinase-associated neurodegenerationJ. Inherit. Metab. Dis.30310-3172007Mus musculus PubMed
688202Freeman, K.; Gregory, A.; Turner, A.; Blasco, P.; Hogarth, P.; Hayflick, S.Intellectual and adaptive behaviour functioning in pantothenate kinase-associated neurodegenerationJ. Intellect. Disabil. Res.51417-4262007Homo sapiens PubMed
689010Wilfred, B.R.; Wang, W.X.; Nelson, P.T.Energizing miRNA research: a review of the role of miRNAs in lipid metabolism, with a prediction that miR-103/107 regulates human metabolic pathwaysMol. Genet. Metab.91209-2172007Homo sapiens PubMed
689108Lyoo, C.H.; Prokisch, H.; Meitinger, T.; Lee, S.Y.; Kim, d.o..H.; Lee, M.S.Anticholinergic-responsive gait freezing in a patient with pantothenate kinase-associated neurodegenerationMov. Disord.23283-2842008Homo sapiens PubMed
689128Schneider, S.A.; Walker, R.H.; Bhatia, K.P.The Huntingtons disease-like syndromes: what to consider in patients with a negative Huntingtons disease gene testNat. Clin. Pract. Neurol.3517-5252007Homo sapiens PubMed
689193McNeill, A.; Birchall, D.; Hayflick, S.J.; Gregory, A.; Schenk, J.F.; Zimmerman, E.A.; Shang, H.; Miyajima, H.; Chinnery, P.F.T2* and FSE MRI distinguishes four subtypes of neurodegeneration with brain iron accumulationNeurology701614-16192008Homo sapiens PubMed
689334Saleheen, D.; Ali, T.; Aly, Z.; Khealani, B.; Frossard, P.M.Novel mutation in the PANK2 gene leads to pantothenate kinase-associated neurodegeneration in a Pakistani familyPediatr. Neurol.37296-2982007Homo sapiens PubMed
689335Shields, D.C.; Sharma, N.; Gale, J.T.; Eskandar, E.N.Pallidal stimulation for dystonia in pantothenate kinase-associated neurodegenerationPediatr. Neurol.37442-4452007Homo sapiens PubMed
690019Wong, R.W.; Richa, D.C.; Hahn, P.; Green, W.R.; Dunaief, J.L.Iron toxicity as a potential factor in AMDRetina (Philadelphia, Pa.)27997-10032007Homo sapiens PubMed
690187Marquez, M.; Serafin, A.; Fernandez-Bellon, H.; Serrat, S.; Ferrer-Admetlla, A.; Bertranpetit, J.; Ferrer, I.; Pumarola, M.Neuropathologic findings in an aged albino gorillaVet. Pathol.45531-5372008Gorilla beringei PubMed
701469Chetnani, B.; Das, S.; Kumar, P.; Surolia, A.; Vijayan, M.Mycobacterium tuberculosis pantothenate kinase: possible changes in location of ligands during enzyme actionActa Crystallogr. Sect. D65312-3252009Escherichia coli, Mycobacterium tuberculosis PubMed
702284Yao, J.; Patrone, J.D.; Dotson, G.D.Characterization and kinetics of phosphopantothenoylcysteine synthetase from Enterococcus faecalisBiochemistry482799-28062009Enterococcus faecalis PubMed
703325Olzhausen, J.; Schuebbe, S.; Schueller, H.J.Genetic analysis of coenzyme A biosynthesis in the yeast Saccharomyces cerevisiae: identification of a conditional mutation in the pantothenate kinase gene CAB1Curr. Genet.55163-1732009Saccharomyces cerevisiae PubMed
703958Wu, Z.; Li, C.; Lv, S.; Zhou, B.Pantothenate kinase-associated neurodegeneration: insights from a Drosophila modelHum. Mol. Genet.183659-36722009Drosophila melanogaster, Homo sapiens PubMed
704326Takagi, M.; Tamaki, H.; Miyamoto, Y.; Leonardi, R.; Hanada, S.; Jackowski, S.; Chohnan, S.Pantothenate kinase from the thermoacidophilic archaeon Picrophilus torridusJ. Bacteriol.192233-2412010Picrophilus torridus PubMed
705271Doi, H.; Koyano, S.; Miyatake, S.; Matsumoto, N.; Kameda, T.; Tomita, A.; Miyaji, Y.; Suzuki, Y.; Sawaishi, Y.; Kuroiwa, Y.Siblings with the adult-onset slowly progressive type of pantothenate kinase-associated neurodegeneration and a novel mutation, Ile346Ser, in PANK2: Clinical features and (99m)Tc-ECD brain perfusion SPECT findingsJ. Neurol. Sci.290172-1762009Homo sapiens PubMed
706042Rowan, A.S.; Nicely, N.I.; Cochrane, N.; Wlassoff, W.A.; Claiborne, A.; Hamilton, C.J.Nucleoside triphosphate mimicry: a sugar triazolyl nucleoside as an ATP-competitive inhibitor of B. anthracis pantothenate kinaseOrg. Biomol. Chem.74029-40362009Bacillus anthracis PubMed

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