Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 6.3.2.5 - phosphopantothenate-cysteine ligase (CTP) and Organism(s) Escherichia coli and UniProt Accession P0ABQ0

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
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P0ABQ0
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
coupling enzyme, phosphopantothenoylcysteine synthetase, ppc synthetase, phosphopantothenate-cysteine ligase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphopantothenoylcysteine synthetase
-
PPC synthetase
the bifunctional protein Dfp from Escherichia coli harbors the activity of phosphopantothenoylcysteine synthetase and phosphopantothenoylcysteine decarboxylase
4’-phosphopantothenoylcysteine synthetase
-
-
-
-
CoaB
-
-
-
-
coupling enzyme
-
-
-
-
pantothenate 4´-phosphate:L-cysteine ligase
-
-
-
-
phosphopantothenoyl-cysteine ligase
-
-
-
-
phosphopantothenoylcysteine synthetase
PPC synthase
-
-
-
-
synthetase, phosphopantothenoylcysteine
-
-
-
-
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
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxylic acid amide formation
-
-
-
-
carboxamide formation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
-
SUBSTRATE
PRODUCT                       
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
-
-
-
-
r
CTP + (R)-4'-phosphopantothenate + L-Cys
(R)-4'-phosphopantothenoyl-L-cysteine + CDP + phosphate
show the reaction diagram
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
-
-
-
-
r
additional information
?
-
-
ATP, GTP, and UTP cannot substitute for CTP
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
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
-
-
-
-
r
CTP + (R)-4'-phosphopantothenate + L-cysteine
CMP + diphosphate + N-[(R)-4'-phosphopantothenoyl]-L-cysteine
show the reaction diagram
-
-
-
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.29
(R)-4'-phosphopantothenate
-
at pH 7.6 and 25°C
0.78
(R)-4'-phosphopantothenoyl-L-cysteine
-
pH 7.6
0.29
4'-phosphopantothenate
-
pH 7.6
0.29
CTP
0.24
cysteine
-
pH 7.6
0.24
L-cysteine
-
at pH 7.6 and 25°C
0.78
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
at pH 7.6 and 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.88
(R)-4'-phosphopantothenate
-
at pH 7.6 and 25°C
0.83
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
-
at pH 7.6 and 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.371
-
after 1280fold purification, at pH 7.6 and 25°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
gene coaBC is essential, but Escherichia coli can effectively metabolize pantethine to bypass the requirement for coaBC
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26100
-
2 * 26100, SDS-PAGE
42000
-
gel filtration
45000
-
x * 45000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
2 * 26100, SDS-PAGE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A275T
-
temperature sensitive mutant dfp-1
A275V
-
unable to form dimers
D203N
-
unable to form dimers
K289Q
-
complete loss of enzymic activity
N210D
-
complete loss of enzymic activity, but intermediate 4’-phosphopanthotenoyl-CMP is formed
N210H
-
used for isolation of reaction intermediate
N210K
-
used for isolation of reaction intermediate
T194V
-
unable to form dimers
T198V
-
unable to form dimers
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli Tuner(DE3) cells
-
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kupke, T.
Molecular Characterization of the 4'-Phosphopantothenoylcysteine Synthetase Domain of Bacterial Dfp Flavoproteins
J. Biol. Chem.
277
36137-36145
2002
Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team