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Information on EC 4.1.1.36 - phosphopantothenoylcysteine decarboxylase and Organism(s) Homo sapiens

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.36 phosphopantothenoylcysteine decarboxylase
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This record set is specific for:
Homo sapiens
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
athal3a, ppcdc, coabc, phosphopantothenoylcysteine decarboxylase, ppc-dc, hal3a, 4'-phosphopantothenoylcysteine decarboxylase, ppc decarboxylase, nthal3, 4'-phosphopantothenoyl-l-cysteine decarboxylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4'-Phospho-N-(D-pantothenoyl)-L-cysteine carboxy-lyase
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4'-Phosphopantothenoyl-L-cysteine decarboxylase
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4'-Phosphopantotheoylcysteine decarboxylase
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Decarboxylase, phosphopantothenoylcysteine
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N-((R)-4-phosphopantothenoyl)-L-cysteine carboxy-lyase
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P-PaCysSH decarboxylase
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Phosphopantothenoylcysteine decarboxylase
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PPC-decarboxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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PATHWAY SOURCE
PATHWAYS
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-, -, -
SYSTEMATIC NAME
IUBMB Comments
N-[(R)-4'-phosphopantothenoyl]-L-cysteine carboxy-lyase (pantotheine-4'-phosphate-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9024-69-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R)-4'-phospho-N-pantothenoylcysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
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-
-
-
?
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
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
N-[(R)-4'-phosphopantothenoyl]-L-cysteine
pantotheine 4'-phosphate + CO2
show the reaction diagram
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essential enzyme in the biosynthesis of coenzyme A
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4'-phospho-N-(1-mercaptomethyl-cyclopropyl)-pantothenamide
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i.e. PPanDELTASH, mechanism-based inhibitor, alkylating C173 residue of enzyme
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.118
(R)-4'-phospho-N-pantothenoylcysteine
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pH 7.6, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.9
(R)-4'-phospho-N-pantothenoylcysteine
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pH 7.6, 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.58
4'-phospho-N-(1-mercaptomethyl-cyclopropyl)-pantothenamide
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pH 7.6, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
COAC_HUMAN
204
0
22395
Swiss-Prot
other Location (Reliability: 4)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
space group R3, 4 monomers per asymmetric unit
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned and expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Manoj, N.; Ealick, S.E.
Unusual space-group pseudosymmetry in crystals of human phosphopantothenoylcysteine decarboxylase
Acta Crystallogr. Sect. D
59
1762-1766
2003
Homo sapiens
Manually annotated by BRENDA team
Strauss, E.; Zhai, H.; Brand, L.A.; McLafferty, F.W.; Begley, T.P.
Mechanistic studies on phosphopantothenoylcysteine decarboxylase: trapping of an enethiolate intermediate with a mechanism-based inactivating agent
Biochemistry
43
15520-15533
2004
Homo sapiens
Manually annotated by BRENDA team