Information on EC 6.3.2.51 - phosphopantothenate-cysteine ligase (ATP)

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

EC NUMBER
COMMENTARY hide
6.3.2.51
-
RECOMMENDED NAME
GeneOntology No.
phosphopantothenate-cysteine ligase (ATP)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + (R)-4'-phosphopantothenate + L-cysteine = AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme A biosynthesis II (eukaryotic)
-
-
taurine biosynthesis II
-
-
Pantothenate and CoA biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
(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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
enzyme mutations disrupt female fecundity, affect egg chamber development, and also induce alterations in scutellar patterning and cause wing vein abnormalities
physiological function
-
the enzyme is required for various processes that occur during oogenesis including chorion patterning
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)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + (R)-4'-phosphopantothenate + L-cysteine
AMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
activity is supported by Mg2+
Mn2+
-
activity is supported by Mn2+
additional information
-
not influenced by Zn2+, Fe2+, Ca2+, and Cd2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.057
(R)-4'-phosphopantothenate
0.269
ATP
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at pH 7.6 and 37C
0.156 - 0.265
CTP
0.014 - 0.086
L-cysteine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.53 - 2.9
(R)-4'-phosphopantothenate
2.9
CTP
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at pH 7.6 and 37C
2.9
L-cysteine
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at pH 7.6 and 37C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.7
AMP
-
at pH 7.6 and 37C
0.465
ATP
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at pH 7.6 and 37C
4.69
CMP
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at pH 7.6 and 37C
0.074 - 0.652
CTP
0.372
GTP
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at pH 7.6 and 37C
0.662
UTP
-
at pH 7.6 and 37C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
-
2 * 28000, SDS-PAGE
60000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 24% polyethyleneglycol monomethyl ether 2000, 120 mM (NH4)2SO4, and 100 mM Tris-HCl (pH 8.5)
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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