Any feedback?
No. of entries
Information on EC 6.3.2.5 - phosphopantothenate-cysteine ligase (CTP)
for references in articles please use BRENDA:EC6.3.2.5
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree 6 Ligases
6.3 Forming carbon-nitrogen bonds
6.3.2 Acid—amino-acid ligases (peptide synthases)
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.
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
showSynonyms
coupling enzyme, phosphopantothenoylcysteine synthetase, ppc synthetase, phosphopantothenate-cysteine ligase, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-phosphopantothenoylcysteine synthetase
-
-
-
-
CoaB
CoaBC
coupling enzyme
-
-
-
-
Dfp
pantothenate 4'-phosphate:L-cysteine ligase
-
-
-
-
phosphopantothenate-cysteine ligase
phosphopantothenoyl-cysteine ligase
-
-
-
-
phosphopantothenoylcysteine synthetase
PPC synthase
-
-
-
-
PPC synthetase
PPCS
synthetase, phosphopantothenoylcysteine
-
-
-
-
CoaB
-
-
-
-
phosphopantothenoylcysteine synthetase
-
-
-
-
PPC synthetase
the bifunctional protein Dfp from Escherichia coli harbors the activity of phosphopantothenoylcysteine synthetase and phosphopantothenoylcysteine decarboxylase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
ping pong mechanism
-
CTP + (R)-4'-phosphopantothenate + L-cysteine = CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
cysteine can be replaced by some of its derivatives
-
-
-
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
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxamide formation
-
-
-
-
carboxylic acid amide formation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
coenzyme A biosynthesis I (bacteria), coenzyme A biosynthesis III (archaea)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
9023-50-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: 5% of activity compared to L-Cys
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
r
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
CTP + (R)-4'-phosphopantothenate + L-Cys
?
-
Substrates: Brown´s pathway of CoA synthesis
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
CTP + (R)-4'-phosphopantothenate + L-cystine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cystine
Substrates: 69% activity compared to the reaction with L-cysteine
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + 2-aminoethanethiol disulfide
?
-
Substrates: 10% of activity compared to L-Cys
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + 2-aminoethanethiol disulfide
?
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + 2-methylcysteine
N-(phosphopantothenyl)-alpha-methylcysteine + ADP + phosphate
-
Substrates: 10% of the activity compared to L-cysteine
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + 2-methylcysteine
N-(phosphopantothenyl)-alpha-methylcysteine + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + beta-mercaptoethylamine
phosphopantetheine + ADP + phosphate
-
Substrates: 25% of activity compared to L-Cys
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + beta-mercaptoethylamine
phosphopantetheine + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
-
Substrates: 8% of the activity with CTP
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
-
Substrates: human enzyme can use both ATP and CTP with similar affinity. Catalysis under CTP conditions displays Michaelis-Menten kinetics
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
-
Substrates: mammalian enzyme differs from the bacterial enzyme in that it can use any of the other nucleotide triphosphates equally as well as CTP
Products: -
Products: -
?
ATP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + ADP + phosphate
-
Substrates: -
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: mammalian enzyme differs from the bacterial enzyme in that it can use any of the other nucleotide triphosphates equally as well as CTP
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: -
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: -
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: CTP specifically required
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: CTP specifically required
Products: -
Products: -
r
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: 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
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: CTP specifically required
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: -
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
-
Substrates: CTP specifically required
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
Substrates: the enzyme is required for various processes that occur during oogenesis including chorion patterning, e.g. for F-actin remodeling during cytoplasmic dumping, overview
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
Substrates: -
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
Substrates: -
Products: -
Products: -
r
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
Substrates: detection of the 4'-phosphopantothenoyl-CMP intermediate
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
Substrates: -
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
Substrates: detection of the 4'-phosphopantothenoyl-CMP intermediate
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
Substrates: -
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
Substrates: 69% activity compared to the reaction with ATP
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATP, GTP, and UTP cannot substitute for CTP
Products: -
Products: -
?
additional information
?
-
Substrates: no activity with L-serine
Products: -
Products: -
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: -
Products: -
Products: -
r
CTP + (R)-4'-phosphopantothenate + L-Cys
?
-
Substrates: Brown´s pathway of CoA synthesis
Products: -
Products: -
?
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
-
Substrates: the enzyme is required for various processes that occur during oogenesis including chorion patterning, e.g. for F-actin remodeling during cytoplasmic dumping, overview
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
Substrates: -
Products: -
Products: -
r
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
Substrates: -
Products: -
Products: -
?
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
Substrates: -
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
CMP
-
competitive to CTP, mixed type to (R)-4'-phosphopantothenate, uncompetitive to L-Cys
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
brenda
single gene coaBC encoding a bifunctional protein catalyzing two consecutive steps in the CoA pathway converting 4-phosphopantothenate to 4-phosphopantetheine
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Show AA Sequence and Transmembrane Helices (17630 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
-
enzymic activity lies within the C-terminal domain of Dfp protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
mutant enzyme H337A complexed with (R)-4'-phosphopantothenate, 4'-phosphopantothenoyl-CMP, or N-[(R)-4'-phosphopantothenoyl]-L-cysteine, hanging drop vapor diffusion method, using 20% (w/v) PEG 3350 as precipitant
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Ni-NTA column chromatography, and Superdex 200 gel filtration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Rattus norvegicus, Morganella morganii, Escherichia coli, Mammalia, Bacteria, no activity in Saccharomyces cerevisiae, no activity in Lactobacillus arabinosus, no activity in Lactobacillus helveticus
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
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
brenda
Strauss, E.; Kinsland, C.; Ge, Y.; McLafferty, F.W.; Begley, T.P.
Phosphopantothenoylcysteine synthetase from Escherichia coli. Identification and characterization of the last unidentified coenzyme A biosynthetic enzyme in bacteria
J. Biol. Chem.
276
13513-13516
2001
Escherichia coli
brenda
Kupke, T.
Molecular Characterization of the 4'-Phosphopantothenoylcysteine Synthetase Domain of Bacterial Dfp Flavoproteins
J. Biol. Chem.
277
36137-36145
2002
Escherichia coli
brenda
Stanitzek, S.; Augustin, M.A.; Huber, R.; Kupke, T.; Steinbacher, S.
Structural basis of CTP-dependent peptide bond formation in coenzyme A biosynthesis catalyzed by Escherichia coli PPC synthetase
Structure
12
1977-1988
2004
Escherichia coli (P0ABQ0), Escherichia coli
brenda
Kupke, T.; Schwarz, W.
4-Phosphopantetheine biosynthesis in archaea
J. Biol. Chem.
281
5435-5444
2006
Methanocaldococcus jannaschii (Q58323), Methanocaldococcus jannaschii DSM 2661 (Q58323)
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
brenda
Zheng, P.; Zhang, M.; Khan, M.H.; Liu, H.; Jin, Y.; Yue, J.; Gao, Y.; Teng, M.; Zhu, Z.; Niu, L.
Crystallographic analysis of the catalytic mechanism of phosphopantothenoylcysteine synthetase from Saccharomyces cerevisiae
J. Mol. Biol.
431
764-776
2019
Saccharomyces cerevisiae (P40506)
brenda
EXTERNAL LINKS (specific for EC-Number 6.3.2.5)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
