Information on EC 4.1.1.36 - phosphopantothenoylcysteine decarboxylase

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

EC NUMBER
COMMENTARY
4.1.1.36
-
RECOMMENDED NAME
GeneOntology No.
phosphopantothenoylcysteine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2
show the reaction diagram
stereochemistry and mechanisms
-
N-[(R)-4'-phosphopantothenoyl]-L-cysteine = pantotheine 4'-phosphate + CO2
show the reaction diagram
C173 serves as an active site acid in the protonation of the enethiolate intermediate
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
coenzyme A biosynthesis
-
Metabolic pathways
-
Pantothenate and CoA biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
N-[(R)-4'-phosphopantothenoyl]-L-cysteine carboxy-lyase (pantotheine-4'-phosphate-forming)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4'-Phospho-N-(D-pantothenoyl)-L-cysteine carboxy-lyase
-
-
-
-
4'-phosphopantothenoyl-cysteine decarboxylase
-
-
4'-Phosphopantothenoyl-L-cysteine decarboxylase
-
-
-
-
4'-phosphopantothenoylcysteine decarboxylase
-
-
4'-Phosphopantotheoylcysteine decarboxylase
-
-
-
-
4-phosphopantothenoylcysteine decarboxylase
-
-
CoaC
-
part of the bifunctional Dfp protein
decarboxylase AtHAL3a
-
-
Decarboxylase, phosphopantothenoylcysteine
-
-
-
-
dfp flavoprotein
-
-
flavoprotein AtHal3a
-
-
N-((R)-4-phosphopantothenoyl)-L-cysteine carboxy-lyase
-
-
-
-
P-PaCysSH decarboxylase
-
-
-
-
Phosphopantothenoylcysteine decarboxylase
-
-
-
-
Phosphopantothenoylcysteine decarboxylase
-
-
PPC decarboxylase
-
-
PPC decarboxylase
-
-
PPC decarboxylase
-
-
PPC-DC
-
-
PPC-decarboxylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9024-69-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isozymes NtHal3a, NtHal3b, NtHal3c. NtHal3a relates both to hyper-osmotic stress and sodium ion toxicity, overproduction increases the intracellular ratio of proline
-
-
Manually annotated by BRENDA team
no activity in Plasmodium lophurae
-
-
-
Manually annotated by BRENDA team
japonica cultivar Nipponbare
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
Hal3 and Vhs3 as moonlighting proteins involved in both CoA biosynthesis and protein phosphatase regulation
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-4'-phospho-N-pantothenoylcysteine
4'-phosphopantetheine + CO2
show the reaction diagram
-
-
-
?
(R)-4'-phospho-N-pantothenoylcysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
alpha-Carboxy-CoA
?
show the reaction diagram
-
at low rate
-
-
-
D-pantothenoylcysteine
pantotheine + CO2
show the reaction diagram
-
pantothenoylaminoethenethiol is the intermediate in decarboxylation
-
?
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
-
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
Pantotheine 4-phosphate + CO2
show the reaction diagram
-
specific for
-
-
N-((R)-4-Phosphopantothenoyl)-L-Cys
?
show the reaction diagram
-
enzyme is involved in coenzyme A biosynthesis
-
-
-
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-, Q9SWE5
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
step in coenzyme A biosynthesis
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
activity is fused with another enzyme bearing phosphopantothenoylcysteine synthetase activity to form a bifunctional enzyme, CoABC, biosynthesis of coenzyme A
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
essential enzyme in the biosynthesis of coenzyme A
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
key step in coenzyme A biosynthesis
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-, Q9SWE5
key step in coenzyme A biosynthesis
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
key step in coenzyme A biosynthesis
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
key step in coenzyme A biosynthestic pathway
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
the 4-phosphopantothenoylcysteine decarboxylase activity of HAL3 is not associated with its role in cell division
-
-
?
Dephospho-alpha-carboxy-CoA
?
show the reaction diagram
-
at low rate
-
-
-
additional information
?
-
-
pantothenylcysteine is decarboxylated
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(R)-4'-phospho-N-pantothenoylcysteine
4'-phosphopantetheine + CO2
show the reaction diagram
-
-
-
?
D-pantothenoylcysteine
pantotheine + CO2
show the reaction diagram
-
pantothenoylaminoethenethiol is the intermediate in decarboxylation
-
?
N-((R)-4-Phosphopantothenoyl)-L-Cys
?
show the reaction diagram
-
enzyme is involved in coenzyme A biosynthesis
-
-
-
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
-
step in coenzyme A biosynthesis
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
biosynthesis of coenzyme A
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
essential enzyme in the biosynthesis of coenzyme A
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
key step in coenzyme A biosynthesis
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-, Q9SWE5
key step in coenzyme A biosynthesis
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
key step in coenzyme A biosynthesis
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
key step in coenzyme A biosynthestic pathway
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
-
the 4-phosphopantothenoylcysteine decarboxylase activity of HAL3 is not associated with its role in cell division
-
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
flavin
-
flavoenzyme
flavin
-
flavoprotein
flavin
-
flavin-containing Cys decarboxylase
flavin
-
flavoprotein
flavin
-
flavin-containing cysteine decarboxylase
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
Mg2+ has no effect
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4'-phospho-N-(1-mercaptomethyl-cyclopropyl)-pantothenamide
-
i.e. PPanDELTASH, mechanism-based inhibitor, alkylating C173 residue of enzyme
4'-phosphopantothenol
-
-
4,4-Bis(dimethylaminodiphenylcarbinol)
-
-
ATP
-
reversed by equimolar amount of semicarbazide
Diketene
-
irreversibly inactivated by N-acetoacetylation with diketene following a pseudo-first order kinetics, substrate protects
hydroxylamine
-
-
hydroxylamine
-
-
iodoacetamide
-
-
pantotheine 4-phosphate
-
competitive product inhibition
phenylhydrazine
-
-
phenylhydrazine
-
-
pyridoxal
-
reversed by equimolar amount of semicarbazide
pyridoxal 5'-phosphate
-
reversed by equimolar amount of semicarbazide
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
UTP
-
reversed by equimolar amount of semicarbazide
additional information
-
no effect of ADP and AMP
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
increases activity
cysteine
-
increases activity
DTT
-
increases activity
GSH
-
activates
pyruvate
-
covalently bound, involved in catalytic activity
pyruvate
-
covalently bound through an ester linkage to the enzyme
Urea
-
0.2-0.5 M, increases activity
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.118
-
(R)-4'-phospho-N-pantothenoylcysteine
-
pH 7.6, 37C
0.9
-
4-phosphopantothenoyl-L-Cys
-
-
1.43
-
4-phosphopantothenoyl-L-Cys
-
-
0.133
0.15
phosphopantothenoyl-L-Cys
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.9
-
(R)-4'-phospho-N-pantothenoylcysteine
-
pH 7.6, 37C
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.58
-
4'-phospho-N-(1-mercaptomethyl-cyclopropyl)-pantothenamide
-
pH 7.6, 37C
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.063
-
4'-phosphopantothenol
-
in 50 mM Tris, 0.2 mM cysteine, 0.2 mM CTP, 0.2 mM dithiothreitol, 0.2 mM MgCl2, at 37C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.089
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
7.7
-
-
7.6
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
9.5
-
pH 9.5: 75% of optimal activity, pH 6: 23% of optimal activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.99
-
-
isozyme NtHal3a, calculated
5.51
-
-
isozyme NtHal3b, calculated
5.61
-
-
isozyme NtHal3c, calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
activity reaches maximal levels in the early stationary phase
Manually annotated by BRENDA team
-
normal and infected with Plasmodium lophurae
Manually annotated by BRENDA team
additional information
-
mRNA of isoforms a-c is present in all organs of plant, its amount does not change after treatment with 100 mM NaCl or potassium shortage
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
not bound to any cellular structure
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
110000
-
-
gel filtration
146000
-
-
gel filtration
242000
-
-
gel filtration
270000
-
-
CoAC domain, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 35000, SDS-PAGE
?
-
x * 22800, isozyme NtHal3a, calculated, x * 23000, isozymes NtHal3b and NtHal3c, calculated
dodecamer
-
12 * 20100, homododecamer, SDS-PAGE
heterotrimer
-
consists of Ykl088w and Hal3/Vhs3 monomers that separately provide two essential catalytic residues
homodecamer
-
10 * 24060, gel filtration
homodimer
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of mutant C175S in complex with reaction intermediate pantotheoylaminoethenethiol and FMNH(2)
-
space group R3, 4 monomers per asymmetric unit
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
histidine photo-oxidation with methylene blue or rose bengal causes total loss of activity
-
4416
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, stable for at least 2 months
-
stable for at least 2 months if frozen as diluted solution, less than 1 mg/ml, or concentrated solution, 1-10 mg/ml
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme
-
recombinant enzyme
-
Ni-NTA resin chromatography and Superdex 200 gel filtration
-
Ni-NTA metal-affinity column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21 (DE3)
-
5'partof the dfp gene is cloned and overexpressed
-
cloned and expressed in Escherichia coli
-
expressed in Escherichia coli strain M15
-
expressed in Escherichia coli BL21 (DE3) cells
-
cloned by reverse transcriptase (RT)-PCR using leaf total RNA as template, expression in Escherichia coli K-12
-
Hal3, Vhs3 and Ykl088w proteins are expressed in Escherichia coli as GST fusion proteins
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
A174S
-
site-directed mutagenesis
A174V
-
site-directed mutagenesis
C175S
-
site-directed mutagenesis
C175S
-
active site mutant
D177N
-
site-directed mutagenesis
G179A
-
site-directed mutagenesis
H90N
-
exchange leads to complete inactivation of the enzyme
R95Q
-
site-directed mutagenesis
A17D
-
site-directed mutagenesis
C158A
-
constructed by sequential polymerase chain reaction
G14S
-
site-directed mutagenesis
G15A
-
site-directed mutagenesis
H90N
-
constructed by sequential polymerase chain reaction
I16L
-
site-directed mutagenesis
K20N
-
site-directed mutagenesis
K20Q
-
site-directed mutagenesis
C54A
-
comparable activity with that of the wild type enzyme
C73A
-
comparable activity with that of the wild type enzyme
C94A
-
comparable activity with that of the wild type enzyme
C96A
-
comparable activity with that of the wild type enzyme
E168A
-
drastically reduced activity
E168D
-
significantly decreased activity
E168K
-
residual activity
H139A/E168K
-
drastically reduced PPC decarboxylase activity
H87A
-
reduced activity
H87N
-
reduced activity
D178N
-
site-directed mutagenesis, Asp 178 is not important for the activity
G180A
-
site-directed mutagenesis, mutant enzyme has a partly reduced activity