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Information on EC 6.3.2.5 - phosphopantothenate-cysteine ligase (CTP)
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EC Tree
6.3.2.5 phosphopantothenate-cysteine ligase (CTP)IUBMB Comments
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.
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The enzyme appears in viruses and cellular organisms
Synonyms
coupling enzyme, phosphopantothenoylcysteine synthetase, ppc synthetase, phosphopantothenate-cysteine ligase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-phosphopantothenoylcysteine synthetase
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-
-
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CoaB
CoaBC
coupling enzyme
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-
-
-
Dfp
pantothenate 4´-phosphate:L-cysteine ligase
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-
-
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phosphopantothenate-cysteine ligase
phosphopantothenoyl-cysteine ligase
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-
-
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phosphopantothenoylcysteine synthetase
PPC synthase
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-
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PPC synthetase
the bifunctional protein Dfp from Escherichia coli harbors the activity of phosphopantothenoylcysteine synthetase and phosphopantothenoylcysteine decarboxylase
PPCS
synthetase, phosphopantothenoylcysteine
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-
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CoaB
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-
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phosphopantothenoylcysteine synthetase
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
mechanism
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CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
ping pong mechanism
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CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
cysteine can be replaced by some of its derivatives
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-
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CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
bi uni uni bi ping pong mechanism, with the nucleotide CTP binding first and CMP released last
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CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
bi uni uni bi ping pong mechanism. 18O from [carboxyl-18O] phosphopantothenate is incorporated into the AMP or CMP produced during PPCS catalysis, consistent with the formation of a phosphopantothenoyl cytidylate or phosphopantothenoyl adenylate intermediate, supporting similar catalytic mechanisms under both CTP and ATP conditions
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxamide formation
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carboxylic acid amide formation
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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.
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CAS REGISTRY NUMBER
COMMENTARY
9023-50-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + (R)-4'-phosphopantothenate + 2-methylcysteine
N-(phosphopantothenyl)-alpha-methylcysteine + ADP + phosphate
ATP + (R)-4'-phosphopantothenate + beta-mercaptoethylamine
phosphopantetheine + ADP + phosphate
ATP + (R)-4'-phosphopantothenate + cystine
(R)-4'-phosphopantothenoyl-L-cystine + ADP + phosphate
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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
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cysteine
-
-
-
-
r
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
CTP + (R)-4'-phosphopantothenate + L-Cys
?
-
Brown´s pathway of CoA synthesis
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-
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
additional information
?
-
-
ATP, GTP, and UTP cannot substitute for CTP
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-
?
ATP + (R)-4'-phosphopantothenate + 2-aminoethanethiol disulfide
?
-
10% of activity compared to L-Cys
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-
?
ATP + (R)-4'-phosphopantothenate + 2-aminoethanethiol disulfide
?
-
-
-
-
?
ATP + (R)-4'-phosphopantothenate + 2-methylcysteine
N-(phosphopantothenyl)-alpha-methylcysteine + ADP + phosphate
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10% of the activity compared to L-cysteine
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?
ATP + (R)-4'-phosphopantothenate + 2-methylcysteine
N-(phosphopantothenyl)-alpha-methylcysteine + ADP + phosphate
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-
-
-
?
ATP + (R)-4'-phosphopantothenate + beta-mercaptoethylamine
phosphopantetheine + ADP + phosphate
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25% of activity compared to L-Cys
-
?
ATP + (R)-4'-phosphopantothenate + beta-mercaptoethylamine
phosphopantetheine + ADP + phosphate
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-
-
-
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
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8% of the activity with CTP
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-
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
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-
-
-
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
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human enzyme can use both ATP and CTP with similar affinity. Catalysis under CTP conditions displays Michaelis-Menten kinetics
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-
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
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mammalian enzyme differs from the bacterial enzyme in that it can use any of the other nucleotide triphosphates equally as well as CTP
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?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
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-
-
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?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
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-
-
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
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-
-
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
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-
-
-
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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mammalian enzyme differs from the bacterial enzyme in that it can use any of the other nucleotide triphosphates equally as well as CTP
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-
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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-
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?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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CTP specifically required
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?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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CTP specifically required
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r
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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human enzyme can use both ATP and CTP with similar affinity. Enzyme shows cooperative binding of ATP, measured as a Hill constant of 1.7
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?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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CTP specifically required
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?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
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CTP specifically required
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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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the enzyme is required for various processes that occur during oogenesis including chorion patterning, e.g. for F-actin remodeling during cytoplasmic dumping, overview
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?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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r
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
detection of the 4'-phosphopantothenoyl-CMP intermediate
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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
detection of the 4'-phosphopantothenoyl-CMP intermediate
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-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cysteine
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-
-
-
r
CTP + (R)-4'-phosphopantothenate + L-Cys
?
-
Brown´s pathway of CoA synthesis
-
-
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
the enzyme is required for various processes that occur during oogenesis including chorion patterning, e.g. for F-actin remodeling during cytoplasmic dumping, overview
-
-
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
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-
-
-
r
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + 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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CMP
-
competitive to CTP, mixed type to (R)-4'-phosphopantothenate, uncompetitive to L-Cys
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cardiomyopathy, Dilated
Mutations in PPCS, Encoding Phosphopantothenoylcysteine Synthetase, Cause Autosomal-Recessive Dilated Cardiomyopathy.
Dehydration
Channeling of 3-hydroxy-4-trans-decenoyl coenzyme A on the bifunctional beta-oxidation enzyme from rat liver peroxisomes and on the large subunit of the fatty acid oxidation complex from Escherichia coli.
Neoplasms
Suppressive effects on cancer cell proliferation of the enhancement of superoxide dismutase (SOD) activity associated with the protein-bound polysaccharide of Coriolus versicolor QUEL.
phosphopantothenoylcysteine decarboxylase deficiency
Pantethine rescues phosphopantothenoylcysteine synthetase and phosphopantothenoylcysteine decarboxylase deficiency in Escherichia coli but not in Pseudomonas aeruginosa.
Tuberculosis
Overcoming synthetic challenges in targeting coenzyme A biosynthesis with the antimicrobial natural product CJ-15,801.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
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
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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-
brenda
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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-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
gene coaBC is essential, but Escherichia coli can effectively metabolize pantethine to bypass the requirement for coaBC
physiological function
-
gene coaBC is essential. Contrary to Escherichia coli, Pseudomonas aeruginosa cannot metabolize pantethine to bypass the requirement for coaBC
physiological function
-
gene coaBC is essential, but Escherichia coli can effectively metabolize pantethine to bypass the requirement for coaBC
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
enzymic activity lies within the C-terminal domain of Dfp protein
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N210D
-
complete loss of enzymic activity, but intermediate 4-phosphopanthotenoyl-CMP is formed
K310Q
N217H
K310Q
N217H
additional information
-
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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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
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Brown, G.M.
The metabolism of pantothenic acid
J. Biol. Chem.
234
370-378
1959
Bacteria, Escherichia coli, Mammalia, Morganella morganii, no activity in Saccharomyces cerevisiae, no activity in Lactobacillus arabinosus, no activity in Lactobacillus helveticus, Rattus norvegicus
brenda
Brohn, F.H.; Trager, W.
Coenzyme A requirement of malaria parasites: enzymes of coenzyme A biosynthesis in normal duck erythrocytes and erythrocytes infected with Plasmodium lophurae
Proc. Natl. Acad. Sci. USA
72
2456-2458
1975
Anas platyrhynchos
brenda
Nishimura, N.; Kakimoto, T.; Chibata, I.
Mechanism of coenzyme A biosynthesis by Sarcina lutea
J. Ferment. Technol.
61
95-99
1983
Micrococcus luteus
-
brenda
Shimizu, S.; Tani, Y.; Ogata, K.
Synthesis of coenzyme A and its biosynthetic intermediates by microbial processes
Methods Enzymol.
62
236-245
1979
Corynebacterium ammoniagenes
brenda
Abiko, Y.
Pantothenic acid and coenzyme A: phosphopantothenoylcysteine synthetase from rat liver (pantothenate 4-phosphate: L-cysteine ligase, EC 6.3.2.5)
Methods Enzymol.
18A
350-354
1976
Rattus norvegicus
-
brenda
Abiko, Y.; Tomikawa, M.; Shimizu, M.
Further studies on phosphopantothenoylcysteine synthetase
J. Biochem.
64
115-117
1968
Rattus norvegicus
brenda
Abiko, Y.
Investigation on pantothenic acid and its related compounds
J. Biochem.
61
290-299
1967
Rattus norvegicus
brenda
Shimizu, S.; Morioka, H.; Tani, Y.; Ogata, K.
A microbial synthesis of pantothenylalcohol 4-phosphate
Agric. Biol. Chem.
42
889-890
1978
Corynebacterium ammoniagenes
-
brenda
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