Information on EC 6.3.2.5 - phosphopantothenate-cysteine ligase (CTP)

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

EC NUMBER
COMMENTARY hide
6.3.2.5
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RECOMMENDED NAME
GeneOntology No.
phosphopantothenate-cysteine ligase (CTP)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxamide formation
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carboxylic acid amide formation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
coenzyme A biosynthesis I (prokaryotic)
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coenzyme A metabolism
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Pantothenate and CoA biosynthesis
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
(R)-4'-phosphopantothenate:L-cysteine ligase
A key enzyme in the production of coenzyme A. The bacterial enzyme requires CTP, in contrast to the eukaryotic enzyme, EC 6.3.2.51, which requires ATP. Cysteine can be replaced by some of its derivatives.
CAS REGISTRY NUMBER
COMMENTARY hide
9023-50-1
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
no activity in Lactobacillus arabinosus
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Manually annotated by BRENDA team
no activity in Lactobacillus helveticus
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Manually annotated by BRENDA team
no activity in Saccharomyces cerevisiae
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Manually annotated by BRENDA team
single gene coaBC encoding a bifunctional protein catalyzing two consecutive steps in the CoA pathway converting 4-phosphopantothenate to 4-phosphopantetheine
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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 + 2-aminoethanethiol disulfide
?
show the reaction diagram
ATP + (R)-4'-phosphopantothenate + 2-methylcysteine
N-(phosphopantothenyl)-alpha-methylcysteine + ADP + phosphate
show the reaction diagram
ATP + (R)-4'-phosphopantothenate + beta-mercaptoethylamine
phosphopantetheine + ADP + phosphate
show the reaction diagram
ATP + (R)-4'-phosphopantothenate + cystine
(R)-4'-phosphopantothenoyl-L-cystine + ADP + phosphate
show the reaction diagram
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5% of activity compared to L-Cys
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-
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
show the reaction diagram
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cysteine
show the reaction diagram
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-
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r
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
show the reaction diagram
CTP + (R)-4'-phosphopantothenate + L-Cys
?
show the reaction diagram
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Browns pathway of CoA synthesis
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-
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
additional information
?
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ATP, GTP, and UTP cannot substitute for CTP
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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
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cysteine
show the reaction diagram
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-
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r
CTP + (R)-4'-phosphopantothenate + L-Cys
?
show the reaction diagram
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Browns pathway of CoA synthesis
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?
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+
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required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
phosphate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.013 - 0.29
(R)-4'-phosphopantothenate
0.78
(R)-4'-phosphopantothenoyl-L-cysteine
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pH 7.6
0.071 - 0.29
4'-phosphopantothenate
0.269
ATP
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pH 7.6, 37C
0.156 - 0.29
CTP
0.24
cysteine
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pH 7.6
0.014 - 0.086
L-Cys
0.24
L-cysteine
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at pH 7.6 and 25C
0.78
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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at pH 7.6 and 25C
additional information
additional information
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enzyme shows cooperative binding of ATP, measured as a Hill constant of 1.7
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.88
(R)-4'-phosphopantothenate
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at pH 7.6 and 25C
0.56
ATP
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pH 7.6, 37C
0.53 - 2.9
CTP
0.83
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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at pH 7.6 and 25C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.7
AMP
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pH 7.6, 37C
0.465
ATP
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pH 7.6, 37C
4.69
CMP
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pH 7.6, 37C
0.074
CTP
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pH 7.6, 37C
0.372
GTP
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pH 7.6, 37C
0.766
L-Cys
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substrate CTP, pH 7.6, 37C
0.662
UTP
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pH 7.6, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.371
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after 1280fold purification, at pH 7.6 and 25C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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normal and infected with Plasmodium lophurae
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26100
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2 * 26100, SDS-PAGE
28415
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2 * 28415, ESI-MS
42000
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gel filtration
60000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 45000, SDS-PAGE; x * 45471, ESI/FTMS
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structure of the C-terminal recombinant fragment of Escherichia coli Dfp protein spanning Ser181 to Arg406 which harbors the structures of the phosphopantothenoylcysteine synthetase, apo-form and the synthetase complexed with CTP, the activated acyl-intermediate, 4'-phosphopantothenoyl-CMP and with the reaction product CMP, sitting drop vapor diffusion
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Sephacryl S-200 column chromatography, DEAE-Sepharose column chromatography, hydroxyapatite column chromatography, HiTrap Blue column chromatography, and Superdex 200 gel filtration; partial
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Ni-NTA resin column chromatography; purified as His tag protein
recombinant enzyme
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli M15 (pREP4) cells; overexpression in Escherichia coli
expressed in Escherichia coli Tuner(DE3) cells
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expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A275T
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temperature sensitive mutant dfp-1
A275V
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unable to form dimers
D203N
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unable to form dimers
K289Q
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complete loss of enzymic activity
N210D
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complete loss of enzymic activity, but intermediate 4-phosphopanthotenoyl-CMP is formed
N210H
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used for isolation of reaction intermediate
N210K
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used for isolation of reaction intermediate
T194V
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unable to form dimers
T198V
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unable to form dimers
K310Q
the mutant has very low activity; very low activity
N217H
mutant enzyme has residual activity; the mutant has only residual enzyme activity
K310Q
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the mutant has very low activity; very low activity
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N217H
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mutant enzyme has residual activity; the mutant has only residual enzyme activity
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additional information
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mutation in dPPCS impair female fecundity and fertility, and disrupts the organization of the somatic and germ line cells, affects F-actin organization and results in abnormal PtdIns(4,5)P2 localization. Improper cell organization coincides with aberrant localization of the membrane molecules Gurken (Grk) and Notch, whose activities are required for specification of the follicle cells that pattern the eggshell. Mutations in dPPCS also induce alterations in scutellar patterning and cause wing vein abnormalities, phenotype, detailed overview
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