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EC Tree
IUBMB Comments A key enzyme in the production of coenzyme A. The eukaryotic enzyme requires ATP, in contrast to the bacterial enzyme, EC 6.3.2.5, phosphopantothenate---cysteine ligase, which requires CTP.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
4'-phosphopantothenoylcysteine synthetase,
more
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4'-phosphopantothenoylcysteine synthetase
phosphopantothenoylcysteine synthetase
4'-phosphopantothenoylcysteine synthetase
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4'-phosphopantothenoylcysteine synthetase
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CoaB
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phosphopantothenoylcysteine synthetase
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ambiguous
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phosphopantothenoylcysteine synthetase
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phosphopantothenoylcysteine synthetase
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phosphopantothenoylcysteine synthetase
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phosphopantothenoylcysteine synthetase
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phosphopantothenoylcysteine synthetase
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phosphopantothenoylcysteine synthetase
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PPC synthetase
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PPCS
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gene name, ambiguous
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ATP + (R)-4'-phosphopantothenate + L-cysteine = AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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(R)-4'-phosphopantothenate:L-cysteine ligase (ATP-utilizing)
A key enzyme in the production of coenzyme A. The eukaryotic enzyme requires ATP, in contrast to the bacterial enzyme, EC 6.3.2.5, phosphopantothenate---cysteine ligase, which requires CTP.
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ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
additional information
?
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ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
additional information
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the wild-type enzyme is not able to couple L-serine, L-alanine or DL-homocysteine to (R)-4'-phosphopantothenate
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?
additional information
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neither GTP nor UTP support enzyme activity with the human enzyme
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?
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ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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?
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ATP
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Mg2+
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activity is supported by Mg2+
Mn2+
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activity is supported by Mn2+
additional information
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not influenced by Zn2+, Fe2+, Ca2+, and Cd2+
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5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
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5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
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5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
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5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
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5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
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5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
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5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
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5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
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CTP
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0.013 - 0.057
(R)-4'-phosphopantothenate
0.269
ATP
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at pH 7.6 and 37°C
0.013
(R)-4'-phosphopantothenate
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with ATP as cosubstrate, at pH 7.6 and 37°C
0.017
(R)-4'-phosphopantothenate
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at pH 7.6 and 37°C
0.057
(R)-4'-phosphopantothenate
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with CTP as cosubstrate, at pH 7.6 and 37°C
0.156
CTP
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at pH 7.6 and 37°C
0.265
CTP
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at pH 7.6 and 37°C
0.014
L-cysteine
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with ATP as cosubstrate, at pH 7.6 and 37°C
0.016
L-cysteine
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with CTP as cosubstrate, at pH 7.6 and 37°C
0.086
L-cysteine
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at pH 7.6 and 37°C
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0.53 - 2.9
(R)-4'-phosphopantothenate
2.9
CTP
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at pH 7.6 and 37°C
2.9
L-cysteine
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at pH 7.6 and 37°C
0.53
(R)-4'-phosphopantothenate
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with CTP as cosubstrate, at pH 7.6 and 37°C
0.56
(R)-4'-phosphopantothenate
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with ATP as cosubstrate, at pH 7.6 and 37°C
2.9
(R)-4'-phosphopantothenate
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at pH 7.6 and 37°C
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3.7
AMP
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at pH 7.6 and 37°C
0.465
ATP
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at pH 7.6 and 37°C
4.69
CMP
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at pH 7.6 and 37°C
0.372
GTP
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at pH 7.6 and 37°C
0.662
UTP
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at pH 7.6 and 37°C
0.074
CTP
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at pH 7.6 and 37°C
0.652
CTP
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at pH 7.6 and 37°C
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0.00001 - 0.01
5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
0.003 - 2.7
5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
0.00001
5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
Streptococcus pneumoniae
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pH and temperature not specified in the publication
0.000065
5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
Enterococcus faecalis
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pH and temperature not specified in the publication
0.000068
5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
Escherichia coli
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pH and temperature not specified in the publication
0.01
5'-O-[hydroxy(3-[[(2R)-2-hydroxy-3,3-dimethyl-4-(phosphonooxy)butanoyl]amino]propoxy)phosphoryl]cytidine
Homo sapiens
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pH and temperature not specified in the publication
0.003
5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
Escherichia coli
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pH and temperature not specified in the publication
0.013
5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
Streptococcus pneumoniae
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pH and temperature not specified in the publication
0.018
5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
Enterococcus faecalis
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pH and temperature not specified in the publication
2.7
5'-O-[hydroxy(3-[[(4R)-2-hydroxy-5,5-dimethyl-2-oxo-1,3,2lambda5-dioxaphosphinane-4-carbonyl]amino]propoxy)phosphoryl]cytidine
Homo sapiens
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pH and temperature not specified in the publication
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
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brenda
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brenda
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brenda
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malfunction
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enzyme mutations disrupt female fecundity, affect egg chamber development, and also induce alterations in scutellar patterning and cause wing vein abnormalities
physiological function
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the enzyme is required for various processes that occur during oogenesis including chorion patterning
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PPCS1_ARATH
317
0
35369
Swiss-Prot
Chloroplast (Reliability: 5 )
PPCS_HUMAN
311
0
34005
Swiss-Prot
other Location (Reliability: 2 )
PPCS_MOUSE
311
0
33794
Swiss-Prot
other Location (Reliability: 2 )
A0A8J8W956_9EURO
400
0
44800
TrEMBL
other Location (Reliability: 1 )
A0A6J8DDW1_MYTCO
309
0
35302
TrEMBL
other Location (Reliability: 1 )
A0A812BZN9_SEPPH
311
0
35465
TrEMBL
other Location (Reliability: 1 )
A0A7R8CBZ6_LEPSM
194
0
22055
TrEMBL
Secretory Pathway (Reliability: 2 )
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28000
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2 * 28000, SDS-PAGE
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homodimer
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2 * 28000, SDS-PAGE
homodimer
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2 * 28415, electrospray ionization mass spectroemtry
homodimer
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2 * 28525, calculated from amino acid sequence
homodimer
x-ray crystallography
homodimer
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2 * 34940, electrospray mass spectrometry
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hanging drop vapor diffusion method, using 24% polyethyleneglycol monomethyl ether 2000, 120 mM (NH4)2SO4, and 100 mM Tris-HCl (pH 8.5)
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A276V
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the mutation affects enzyme activity
N210D
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the mutation affects enzyme activity
R206Q
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the mutation affects enzyme activity
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HiTrapQ column chromatography and Superdex 200 gel filtration
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Ni-NTA agarose column chromatography and Superdex 200 gel filtration
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Ni-NTA resin column chromatography
Ni-NTA resin column chromatography, and Mono Q column chromatography
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expressed in Escherichia coli B834(DE3) cells
expressed in Escherichia coli BL21 AI cells
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expressed in Escherichia coli BL21 cells
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expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli M15 cells
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expressed in Escherichia coli TB1 cells
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Kupke, T.
Active-site residues and amino acid specificity of the bacterial 4'-phosphopantothenoylcysteine synthetase CoaB
Eur. J. Biochem.
271
163-172
2004
Escherichia coli
brenda
Manoj, N.; Strauss, E.; Begley, T.P.; Ealick, S.E.
Structure of human phosphopantothenoylcysteine synthetase at 2.3 A resolution
Structure
11
927-936
2003
Homo sapiens (Q9HAB8)
brenda
Bosveld, F.; Rana, A.; Lemstra, W.; Kampinga, H.H.; Sibon, O.C.
Drosophila phosphopantothenoylcysteine synthetase is required for tissue morphogenesis during oogenesis
BMC Res. Notes
1
75
2008
Drosophila melanogaster
brenda
Yao, J.; Patrone, J.D.; Dotson, G.D.
Characterization and kinetics of phosphopantothenoylcysteine synthetase from Enterococcus faecalis
Biochemistry
48
2799-2806
2009
Enterococcus faecalis
brenda
Yao, J.; Dotson, G.D.
Kinetic characterization of human phosphopantothenoylcysteine synthetase
Biochim. Biophys. Acta
1794
1743-1750
2009
Homo sapiens
brenda
Balibar, C.J.; Hollis-Symynkywicz, M.F.; Tao, J.
Pantethine rescues phosphopantothenoylcysteine synthetase and phosphopantothenoylcysteine decarboxylase deficiency in Escherichia coli but not in Pseudomonas aeruginosa
J. Bacteriol.
193
3304-3312
2011
Escherichia coli, Pseudomonas aeruginosa, Escherichia coli K-1
brenda
Patrone, J.D.; Yao, J.; Scott, N.E.; Dotson, G.D.
Selective inhibitors of bacterial phosphopantothenoylcysteine synthetase
J. Am. Chem. Soc.
131
16340-16341
2009
Streptococcus pneumoniae, Escherichia coli, Enterococcus faecalis, Homo sapiens
brenda
Daugherty, M.; Polanuyer, B.; Farrell, M.; Scholle, M.; Lykidis, A.; de Crecy-Lagard, V.; Osterman, A.
Complete reconstitution of the human coenzyme A biosynthetic pathway via comparative genomics
J. Biol. Chem.
277
21431-21439
2002
Homo sapiens
brenda
Kupke, T.; Hernandez-Acosta, P.; Culianez-Macia, F.A.
4-phosphopantetheine and coenzyme A biosynthesis in plants
J. Biol. Chem.
278
38229-38237
2003
Arabidopsis thaliana
brenda
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