2.7.1.33: pantothenate kinase
This is an abbreviated version!
For detailed information about pantothenate kinase, go to the full flat file.
Word Map on EC 2.7.1.33
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2.7.1.33
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neurodegeneration
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kinase-associated
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panks
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sign
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dystonia
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ganglia
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hallervorden-spatz
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extrapyramidal
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parkinsonism
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eye-of-the-tiger
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pla2g6
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phosphopantothenate
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dysarthria
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tiger
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neuroaxonal
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phosphopantetheine
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hypointensity
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medicine
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4'-phosphopantothenate
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pigmentary
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pantothenamide
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bradykinesia
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synthesis
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atp13a2
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4'-phosphopantetheine
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pantethine
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drug development
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neuroferritinopathy
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choreoathetosis
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phosphopantothenoylcysteine
- 2.7.1.33
- neurodegeneration
-
kinase-associated
-
panks
- sign
- dystonia
- ganglia
- hallervorden-spatz
-
extrapyramidal
- parkinsonism
-
eye-of-the-tiger
- pla2g6
- phosphopantothenate
- dysarthria
- tiger
-
neuroaxonal
- phosphopantetheine
-
hypointensity
- medicine
- 4'-phosphopantothenate
-
pigmentary
- pantothenamide
-
bradykinesia
- synthesis
-
atp13a2
- 4'-phosphopantetheine
- pantethine
- drug development
-
neuroferritinopathy
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choreoathetosis
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phosphopantothenoylcysteine
Reaction
Synonyms
4-phosphopantoate, BaPanK, Cab1, Cab1p, CoaA, coaW, CoaX, D-pantothenate kinase, EhPAnK, fumble, hPanK, hPanK1, hPANK2, hPanK3, hPanK4, HpPanK-III, HsPANK3, HsPANK4, kinase, pantothenate (phosphorylating), More, mPank, mPank1, mPanK2, mPanK3, MtCoaA, MtPanK, PAK, PanK, PanK-III, PanK1, PanK1alpha, PanK1b, PanK2, PanK3, PanK4, PanKBa, pantothenate kinase, pantothenate kinase 1, pantothenate kinase 2, pantothenate kinase 3, pantothenate kinase 4, pantothenate kinase-2, pantothenic acid kinase, PfPanK, Pfpank1, PoK, rPanK4, Rts protein
ECTree
2.7.1.33 pantothenate kinaseAdvanced search results
results (
results (Engineering
Engineering on EC 2.7.1.33 - pantothenate kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F247V
less than 50% of catalytic activity of wild type, feedback resistant
H177Q
less than 50% of catalytic activity of wild type, feedback resistant
A509V
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naturally occurring mutation, early onset in patients, 105% activity compared to the wild-type enzyme
E134G
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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
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site-directed mutagenesis, less than 0.2% activity compared to the wild-type enzyme
N404I
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naturally occurring mutation, early and late onset in patients, 83% activity compared to the wild-type enzyme
N500I
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naturally occurring mutation, early onset in patients, 3.9% activity compared to the wild-type enzyme
R207W
R264W
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naturally occurring mutation, early onset in patients, 58% activity compared to the wild-type enzyme
R286C
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naturally occurring mutation, early and late onset in patients, 176% activity compared to the wild-type enzyme
R532W
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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
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naturally occurring mutation, early and late onset in patients, 78% activity compared to the wild-type enzyme
S471N
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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
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naturally occurring mutation, early onset in patients, 91% activity compared to the wild-type enzyme
T528M
F247A
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
F254A
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
F254A/F247A
site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
F247A
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site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
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F254A
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site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
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F254A/F247A
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site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
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F247A
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site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
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F254A
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site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
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F254A/F247A
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site-directed mutagenesis, determination of the crystal structure and comparion with the wild-type enzyme structure and the structure of Escherichia coli enzyme EcPanK
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additional information
G219V
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naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
G219V
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naturally occurring mutation, early and late onset in patients, 0.4% activity compared to the wild-type enzyme
G521R
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naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
G521R
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the splice variant PanK2 naturally contains mutation which is associated with neurodegenerative disease in brain, early and late onset in patients, less than 0.2% activity compared to the wild-type enzyme
T234A
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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
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naturally occurring mutation, early and late onset in patients, 112% activity compared to the wild-type enzyme
T528M
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naturally occurring disease-related point mutation which leads to reduced enzyme activity, and altered processing and stability of the mutant PanK2, reconstruction by site-sirected mutagenesis
T528M
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naturally occurring mutation, early and late onset in patients, 146% activity compared to the wild-type enzyme
additional information
epigenetic gene silencing of PanK resulting in a significant reduction of PanK activity, intracellular CoA concentrations, and growth retardation in vitro, reinforcing the importance of this gene in Entamoeba histolytica. In Pank-silenced cells, the genes encoding other enzymes involved in CoA biosynthesis are upregulated 1.2, 2.1, 3.0, and 5.2 fold for PPCS-PPCDC, PPAT, DPCK1, and DPCK2, respectively. Growth kinetic analysis
additional information
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epigenetic gene silencing of PanK resulting in a significant reduction of PanK activity, intracellular CoA concentrations, and growth retardation in vitro, reinforcing the importance of this gene in Entamoeba histolytica. In Pank-silenced cells, the genes encoding other enzymes involved in CoA biosynthesis are upregulated 1.2, 2.1, 3.0, and 5.2 fold for PPCS-PPCDC, PPAT, DPCK1, and DPCK2, respectively. Growth kinetic analysis
additional information
an allelic variant mislocates and thereby causes disease
additional information
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an allelic variant mislocates and thereby causes disease
additional information
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identification of naturally occuring pantothenate kinase 2 mutant in patients with neurodegenerative disease in brain with iron accumulation, formerly termed Hallervorden-Spatz disease, identification of other disease related point mutations which lead to reduced enzyme activity, mutations alter processing, stability, and catalytic activity of the mutant PanK2
additional information
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several natural mutants with frame shifts show no activity, identification of mutants with mutations which introduce stop codons, overview
additional information
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two siblings with the adult-onset slowly progressive type of pantothenate kinase-associated neurodegeneration have the I346S mutation in pantothenate kinase-2
additional information
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human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity
additional information
human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity
additional information
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construction of chimeric mutant enzymes PanK1beta-3-1beta and PanK3-1beta-3 by combination of isozymes PanK3 and PanK1beta, mutant show different sensitivity to feedback inhibitors compared to the wild-type isozymes, overview
additional information
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generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/- Pank-/-double knock-out mice
additional information
generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/- Pank-/-double knock-out mice
additional information
generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/- Pank-/-double knock-out mice
additional information
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generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/-Pank-/-3 double knock-out mice
additional information
generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/-Pank-/-3 double knock-out mice
additional information
generation of unction Pank1-/-Pank2-/-, Pank1-/-Pank3-/-, and Pank2-/-Pank-/-3 double knock-out mice
additional information
generation of two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures, structure-function analysis, overview. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region, but in three of the four crystallographically independent mutant molecules the structure is similar to that in the Escherichia coli enzyme
additional information
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generation of two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures, structure-function analysis, overview. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region, but in three of the four crystallographically independent mutant molecules the structure is similar to that in the Escherichia coli enzyme
additional information
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generation of two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures, structure-function analysis, overview. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region, but in three of the four crystallographically independent mutant molecules the structure is similar to that in the Escherichia coli enzyme
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additional information
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generation of two point mutants and the corresponding double mutant of Mycobacterium tuberculosis pantothenate kinase to weaken the affinity of the enzyme for the feedback inhibitor CoA. The mutants exhibit reduced activity, which can be explained in terms of their structures, structure-function analysis, overview. The crystals of the mutants are not isomorphous to any of the previously analysed crystals of the wild-type enzyme or its complexes. Although the mutants involve changes in the CoA-binding region, the dimer interface and the ligand-binding region move in a concerted manner, an observation which might be important in enzyme action. The mycobacterial enzyme and its homologous Escherichia coli enzyme exhibit structural differences in their nucleotide complexes in the dimer interface and the ligand-binding region, but in three of the four crystallographically independent mutant molecules the structure is similar to that in the Escherichia coli enzyme
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additional information
parasites pressured with pantothenol or CJ-15,801 become resistant to these antiplasmodial pantothenate analogues. Pfpank1 mutations mediate parasite resistance to PanOH and CJ-15,801. Whole-genome sequencing reveals mutations in one of two putative PanK genes (Pfpank1) in each resistant line. These mutations significantly alter PfPanK activity, with two conferring a fitness cost, consistent with Pfpank1 coding for a functional PanK that is essential for normal growth. Pfpank1 disruption plasmid, DELTAPfpank1-pCC-1 (SI), is transfected into wild-type Palsmodium falciparum strain 3D7
additional information
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parasites pressured with pantothenol or CJ-15,801 become resistant to these antiplasmodial pantothenate analogues. Pfpank1 mutations mediate parasite resistance to PanOH and CJ-15,801. Whole-genome sequencing reveals mutations in one of two putative PanK genes (Pfpank1) in each resistant line. These mutations significantly alter PfPanK activity, with two conferring a fitness cost, consistent with Pfpank1 coding for a functional PanK that is essential for normal growth. Pfpank1 disruption plasmid, DELTAPfpank1-pCC-1 (SI), is transfected into wild-type Palsmodium falciparum strain 3D7
additional information
expression of acetyl-CoA carboxylase (acc) obtained from Corynebacterium glutamicum in Escherichia coli, it causes accumulation of 2.2fold more fatty acids in Escherichia coli that in the wild-type. The addition of gene coaX encoding patothenate kinase from Pseudomonas putida or fatty acid synthase (fasA) from Corynebacterium glutamicum results in a 3.1 and 3.6fold increased fatty acid synthesis in Escherichia coli cells, which express acc and coaA, or acc and fasA, respectively. The transformants, simultaneously possessing all three genes, produce 5.6fold more fatty acids. The strain possessing acc, coaA, and fasA stores 691 mg/l of fatty acids, primarily as phospholipids, inside the inner membrane after 72-h cultivation. In addition, 19% of the total CoA pool is occupied by malonyl-CoA
additional information
improvement of acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass. PanK overexpression or PDH bypass introduction alone only lead to a 2.0fold or 6.74fold increase in naringenin titer, but the combination of both (strain CENFPAA01) results in 24.4fold increase as compared to the control (strain CENF09) in the presence of 0.5 mM substrate p-coumaric acid. The supplement of PanK substrate pantothenate results in another 19% increase in naringenin production
additional information
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improvement of acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass. PanK overexpression or PDH bypass introduction alone only lead to a 2.0fold or 6.74fold increase in naringenin titer, but the combination of both (strain CENFPAA01) results in 24.4fold increase as compared to the control (strain CENF09) in the presence of 0.5 mM substrate p-coumaric acid. The supplement of PanK substrate pantothenate results in another 19% increase in naringenin production
additional information
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improvement of acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass. PanK overexpression or PDH bypass introduction alone only lead to a 2.0fold or 6.74fold increase in naringenin titer, but the combination of both (strain CENFPAA01) results in 24.4fold increase as compared to the control (strain CENF09) in the presence of 0.5 mM substrate p-coumaric acid. The supplement of PanK substrate pantothenate results in another 19% increase in naringenin production
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additional information
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improvement of acetyl-CoA biosynthesis in Saccharomyces cerevisiae via the overexpression of pantothenate kinase and PDH bypass. PanK overexpression or PDH bypass introduction alone only lead to a 2.0fold or 6.74fold increase in naringenin titer, but the combination of both (strain CENFPAA01) results in 24.4fold increase as compared to the control (strain CENF09) in the presence of 0.5 mM substrate p-coumaric acid. The supplement of PanK substrate pantothenate results in another 19% increase in naringenin production
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