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Information on EC 2.7.1.33 - pantothenate kinase and Organism(s) Homo sapiens and UniProt Accession Q9BZ23

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Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
pank2, pantothenate kinase, pantothenate kinase 2, pank1, pank3, pank4, pank-iii, pfpank1, pantothenate kinase-2, type ii pantothenate kinase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pantothenate kinase 2
-
pantothenate kinase-2
-
D-pantothenate kinase
-
-
-
-
hPanK
-
-
-
-
hPanK1
hPANK2
hPanK3
hPanK4
-
-
-
-
HsPANK4
-
-
kinase, pantothenate (phosphorylating)
-
-
-
-
mPank
-
-
-
-
mPank1
-
-
-
-
mPanK3
-
-
-
-
PAK
-
-
-
-
PanK1alpha
-
PanK1b
-
isoform
PanK2
PanK3
PanK4
-
-
pantothenate kinase 1
-
pantothenate kinase 2
-
-
pantothenate kinase 3
-
pantothenate kinase-2
-
-
pantothenic acid kinase
-
-
-
-
rPanK4
-
-
-
-
Rts protein
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:(R)-pantothenate 4'-phosphotransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9026-48-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
ATP + D-pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
ATP + D-pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
-
-
-
?
ATP + pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
-
-
-
-
?
ATP + pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
pantothenate kinase catalyzes the first step in CoA biosynthesis
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
ATP + (R)-pantothenate
ADP + (R)-4'-phosphopantothenate
show the reaction diagram
ATP + pantothenate
ADP + 4'-phosphopantothenate
show the reaction diagram
pantothenate kinase catalyzes the first step in CoA biosynthesis
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetyl-CoA
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamide
-
competitive, pantothenic acid analogue with 2,4-dihydroxy-3,3-dimethylbutyramide core of pantothenate, inhibition mechanism
1,4-phenylene-bis(1,2-ethanediyl)bis-isothiourea dihydrobromide
-
acetyl-CoA
ADP
competitive inhibitor of isoform PanK3 with respect to ATP1 and a mixed-type inhibitor with respect to pantothenate
chloranil
-
CoA
-
feedback inhibition, inhibition kinetics of recombinant isozyme mPanK2
CoA esters
-
feedback inhibition, inhibition kinetics of recombinant isozyme mPanK2
dehydroisoandrosterone
about 30% residual activity at 0.1 mM (isoform PanK3)
Dehydroisoandrosterone sulfate
ephedrine hydrochloride
-
estradiol
about 80% residual activity at 0.1 mM (isoform PanK3)
Estradiol sulfate
about 90% residual activity at 0.1 mM (isoform PanK3)
Estrone sulfate
about 50% residual activity at 0.1 mM (isoform PanK3)
Fusidic acid
-
glipizide
-
glyburide
-
Hexachlorophene
-
MCC-555
MCC-555 inhibits all three isoforms with a rank order of PanK3 > PanK2 > PanK1b
palmitoyl-CoA
strong inhibitor
pioglitazone hydrochloride
-
pregnenolone sulfate
Psi-rhodomyrtoxin
-
Reactive blue 2
-
Ro 41-0960
-
rosiglitazone
-
tamoxifen
-
tolfenamic acid
-
tyrphostin AG 528
-
tyrphostin AG 808
-
WIN 62577
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
palmitoylcarnitine
activates
cholesterol
about 125% activity at 0.1 mM
glyburide
O-oleoylcarnitine
140% activation at 0.1 mM
O-palmitoylcarnitine
120% activation at 0.1 mM
oleoylethanolamide
120% activation at 0.1 mM
palmitoylcarnitine
tamoxifen
140% activation at 0.1 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.009 - 0.833
(R)-pantothenate
0.0031 - 0.311
ATP
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.138
(2R)-2,4-dihydroxy-3,3-dimethyl-N'-phenylbutanohydrazide
-
37°C, versus pantothenate at 1 mM
1
(2R)-N-allyl-2,4-dihydroxy-3,3-dimethylbutanamide
-
37°C, versus pantothenate at 1 mM
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0004
1,4-phenylene-bis(1,2-ethanediyl)bis-isothiourea dihydrobromide
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.00006 - 0.000125
acetyl-CoA
0.0059
chloranil
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0035
Dehydroisoandrosterone sulfate
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0016
ephedrine hydrochloride
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0001
Fusidic acid
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0052
glipizide
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0068
glyburide
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0092
GW5074
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0088
Hexachlorophene
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.001
pioglitazone hydrochloride
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0025
pregnenolone sulfate
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0016
Psi-rhodomyrtoxin
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0013
Reactive blue 2
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0039
Ro 41-0960
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0017
rosiglitazone
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0092
tolfenamic acid
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.003
tyrphostin AG 528
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.009
tyrphostin AG 808
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
0.0007
WIN 62577
Homo sapiens
isoform PanK3, at pH 7.5 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0002421
0.045 mM pantothenate, 0.25 mM ATP (pH 7.0), 10 mM MgCl2, 0.1 M Tris/HCl (pH 7.5), at 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
disease: pantothenate kinase-associated neurodegeneration
physiological function
allosteric regulation of mammalian pantothenate kinase. Pantothenate kinase is the master regulator of CoA biosynthesis and is feedback-inhibited by acetyl-CoA
evolution
malfunction
metabolism
pantothenate kinase catalyzes the rate-controlling step in coenzyme A biosynthesis
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PANK2_HUMAN
570
0
62681
Swiss-Prot
Mitochondrion (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
48000
SDS-PAGE, mature protein
48000
-
x * 48000, recombinant His/myc-tagged isozyme PanK2, SDS-PAGE, x * 63000, recombinant unprocessed PanK2, SDS-PAGE
63000
-
x * 48000, recombinant His/myc-tagged isozyme PanK2, SDS-PAGE, x * 63000, recombinant unprocessed PanK2, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 48000, recombinant His/myc-tagged isozyme PanK2, SDS-PAGE, x * 63000, recombinant unprocessed PanK2, SDS-PAGE
dimer
-
molecular mass, 30.8-61.2 kDa, of diverse protein variants expressed from different plasmids in different systems, SDS-PAGE and gel filtration, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
several isoforms of PanK2 are produced by sequential proteolytic cleavage, identification of cleavage sites for the mitochondrial processing peptidase, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop 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 disease
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G521R
loss of enzyme activity
T528M
no effect on PANK2 activity or stability
A267F
catalytically inactive
A269F
catalytically inactive
A509V
-
naturally occurring mutation, early onset in patients, 105% activity compared to the wild-type enzyme
E134G
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
E138V
G19V
site-directed mutagenesis, PANK3(G19V) cannot bind ATP, and biochemical analyses of an engineered PANK3/PANK3(G19V) heterodimer confirmed that the two active sites are functionally coupled. Analysis of PANK3/PANK3(G19V) heterodimers, overview
G219V
G521R
K224A
-
site-directed mutagenesis, less than 0.2% activity compared to the wild-type enzyme
N404I
-
naturally occurring mutation, early and late onset in patients, 83% activity compared to the wild-type enzyme
N500I
-
naturally occurring mutation, early onset in patients, 3.9% activity compared to the wild-type enzyme
R207A
catalytically inactive
R207W
R264W
-
naturally occurring mutation, early onset in patients, 58% activity compared to the wild-type enzyme
R286C
-
naturally occurring mutation, early and late onset in patients, 176% activity compared to the wild-type enzyme
R532W
-
naturally occurring mutation, early onset in patients, 95% activity compared to the wild-type enzyme
S195V
the mutant is insensitive to acetyl-CoA and has a KM defect for pantothenate
S351P
-
naturally occurring mutation, early and late onset in patients, 78% activity compared to the wild-type enzyme
S471N
-
naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
T234A
T327I
-
naturally occurring mutation, early onset in patients, 91% activity compared to the wild-type enzyme
T528M
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged PanK2
native enzyme partially by preparation of mitochondria
HiTrap chelating HP column chromatography and Superdex 200 column gel filtration
recombinant His/myc-tagged isozyme PanK2 from mitochondria of QBI 293 cells by ion exchange and protein A affinity chromatography and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain ts9
PANK2, 2 translational strat sites, CAG and CUG initiation codons, expression of PANK2 as EGFP-tagged protein in HeLa cell mitochondria, and in COS-7 cells as His/myc-tagged enzyme
expressed in Escherichia coli BL21(DE3) cells
expression as a His-tagged fusion protein in Escherichia coli
expression of wild-type His/myc-tagged isozyme PanK2 and of mutant enzymes in mitochondria of QBI 293 cells
-
gene PANK1, PANK1alpha and PANK1beta are splice variants of the PANK1 gene
gene PANK3, sequence comparisons and phylogenetic analysis
gene PANK4, sequence comparisons and phylogenetic analysis
splice variant PanK2, expression of active PanK2 isozymes iPanK2, spPanK2, mPanK2 in HEK293T cells, in vitro transcription and translation of PanK2
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
pantothenate-kinase-associated neurodegeneration (PKAN) is caused by mutations of the pantothenate kinase (PANK2) on chromosome 20p13. PKAN is characterized clinically by extrapyramidal symptoms (in 98% of cases), in particular, generalized dystonia with oromandibular involvement, and parkinsonism-spasticity (25%), behavioral changes followed by dementia (29%), and pigmentary retinal degeneration. The mean age at onset is between 3 and 4 years
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, 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 neurodegeneration
Ann. N. Y. Acad. Sci.
1012
282-298
2004
Homo sapiens (Q9BZ23), Homo sapiens
Manually annotated by BRENDA team
Spry, 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 parasites
Antimicrob. Agents Chemother.
49
4649-4657
2005
Homo sapiens, Plasmodium falciparum
Manually annotated by BRENDA team
Zhang, Y.M.; Rock, C.O.; Jackowski, S.
Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration
J. Biol. Chem.
281
107-114
2006
Homo sapiens
Manually annotated by BRENDA team
Kotzbauer, 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 2
J. Neurosci.
25
689-698
2005
Homo sapiens
Manually annotated by BRENDA team
Hartig, 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 accumulation
Ann. Neurol.
59
248-256
2006
Homo sapiens (Q9BZ23), Homo sapiens
Manually annotated by BRENDA team
Leonardi, R.; Rock, C.O.; Jackowski, S.; Zhang, Y.M.
Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine
Proc. Natl. Acad. Sci. USA
104
1494-1499
2007
Homo sapiens, Homo sapiens (Q9BZ23)
Manually annotated by BRENDA team
Clement, F.; Devos, D.; Moreau, C.; Coubes, P.; Destee, A.; Defebvre, L.
Neurodegeneration with brain iron accumulation: clinical, radiographic and genetic heterogeneity and corresponding therapeutic options
Acta Neurol. Belg.
107
26-31
2007
Homo sapiens
Manually annotated by BRENDA team
Isaac, C.; Wright, I.; Bhattacharyya, D.; Baxter, P.; Rowe, J.
Pallidal stimulation for pantothenate kinase-associated neurodegeneration dystonia
Arch. Dis. Child.
93
239-240
2008
Homo sapiens
Manually annotated by BRENDA team
Mikati, M.A.; Yehya, A.; Darwish, H.; Karam, P.; Comair, Y.
Deep brain stimulation as a mode of treatment of early onset pantothenate kinase-associated neurodegeneration
Eur. J. Paediatr. Neurol.
13
61-64
2008
Homo sapiens
Manually annotated by BRENDA team
Leonardi, R.; Zhang, Y.M.; Lykidis, A.; Rock, C.O.; Jackowski, S.
Localization and regulation of mouse pantothenate kinase 2
FEBS Lett.
581
4639-4644
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Chan, 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 mutation
Hong Kong Med. J.
14
70-73
2008
Homo sapiens
Manually annotated by BRENDA team
Hong, 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 disorder
J. Biol. Chem.
282
27984-27993
2007
Homo sapiens (Q8TE04), Homo sapiens (Q9H999), Homo sapiens
Manually annotated by BRENDA team
Kazek, 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 communication
J. Child Neurol.
22
1256-1259
2007
Homo sapiens
Manually annotated by BRENDA team
Freeman, K.; Gregory, A.; Turner, A.; Blasco, P.; Hogarth, P.; Hayflick, S.
Intellectual and adaptive behaviour functioning in pantothenate kinase-associated neurodegeneration
J. Intellect. Disabil. Res.
51
417-426
2007
Homo sapiens
Manually annotated by BRENDA team
Wilfred, 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 pathways
Mol. Genet. Metab.
91
209-217
2007
Homo sapiens
Manually annotated by BRENDA team
Lyoo, 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 neurodegeneration
Mov. Disord.
23
283-284
2008
Homo sapiens
Manually annotated by BRENDA team
Schneider, S.A.; Walker, R.H.; Bhatia, K.P.
The Huntingtons disease-like syndromes: what to consider in patients with a negative Huntingtons disease gene test
Nat. Clin. Pract. Neurol.
3
517-525
2007
Homo sapiens, Homo sapiens (Q9BZ23)
Manually annotated by BRENDA team
McNeill, 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 accumulation
Neurology
70
1614-1619
2008
Homo sapiens
Manually annotated by BRENDA team
Saleheen, 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 family
Pediatr. Neurol.
37
296-298
2007
Homo sapiens
Manually annotated by BRENDA team
Shields, D.C.; Sharma, N.; Gale, J.T.; Eskandar, E.N.
Pallidal stimulation for dystonia in pantothenate kinase-associated neurodegeneration
Pediatr. Neurol.
37
442-445
2007
Homo sapiens
Manually annotated by BRENDA team
Wong, R.W.; Richa, D.C.; Hahn, P.; Green, W.R.; Dunaief, J.L.
Iron toxicity as a potential factor in AMD
Retina (Philadelphia, Pa. )
27
997-1003
2007
Homo sapiens
Manually annotated by BRENDA team
Wu, Z.; Li, C.; Lv, S.; Zhou, B.
Pantothenate kinase-associated neurodegeneration: insights from a Drosophila model
Hum. Mol. Genet.
18
3659-3672
2009
Drosophila melanogaster, Homo sapiens (Q9BZ23), Homo sapiens
Manually annotated by BRENDA team
Doi, 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 findings
J. Neurol. Sci.
290
172-176
2009
Homo sapiens
Manually annotated by BRENDA team
Leonardi, R.; Zhang, Y.M.; Yun, M.K.; Zhou, R.; Zeng, F.Y.; Lin, W.; Cui, J.; Chen, T.; Rock, C.O.; White, S.W.; Jackowski, S.
Modulation of pantothenate kinase 3 activity by small molecules that interact with the substrate/allosteric regulatory domain
Chem. Biol.
17
892-902
2010
Homo sapiens, Homo sapiens (Q9H999)
Manually annotated by BRENDA team
Subramanian, C.; Yun, M.K.; Yao, J.; Sharma, L.K.; Lee, R.E.; White, S.W.; Jackowski, S.; Rock, C.O.
Allosteric regulation of mammalian pantothenate kinase
J. Biol. Chem.
291
22302-22314
2016
Mus musculus, Mus musculus (Q8K4K6), Mus musculus (Q8R2W9), Homo sapiens (Q8TE04), Homo sapiens (Q9BZ23), Homo sapiens (Q9H999), Homo sapiens
Manually annotated by BRENDA team
Yao, J.; Subramanian, C.; Rock, C.O.; Jackowski, S.
Human pantothenate kinase 4 is a pseudo-pantothenate kinase
Protein Sci.
28
1031-1047
2019
Homo sapiens, Homo sapiens (Q9H999)
Manually annotated by BRENDA team