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Information on EC 4.1.1.65 - phosphatidylserine decarboxylase and Organism(s) Homo sapiens

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.65 phosphatidylserine decarboxylase
IUBMB Comments
A pyridoxal-phosphate protein. In Escherichia coli, the prosthetic group is a pyruvoyl group.
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This record set is specific for:
Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
phosphatidylserine decarboxylase, psdc, ps decarboxylase, psd1p, psd2p, phosphatidylserine decarboxylase 1, phosphatidylserine decarboxylase 2, phosphatidylserine decarboxylase2, ct699, psd1 enzyme, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Decarboxylase, phosphatidylserine
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-
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Phosphatidylserine decarboxylase
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-
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PISD
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PS decarboxylase
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-
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PSD
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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-
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SYSTEMATIC NAME
IUBMB Comments
phosphatidyl-L-serine carboxy-lyase (phosphatidylethanolamine-forming)
A pyridoxal-phosphate protein. In Escherichia coli, the prosthetic group is a pyruvoyl group.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-78-8
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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
phosphatidyl-L-serine
?
show the reaction diagram
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important enzyme in the synthesis of phosphatidylethanolamine
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-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + 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
phosphatidyl-L-serine
?
show the reaction diagram
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important enzyme in the synthesis of phosphatidylethanolamine
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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DMSO has no discernable effect on product formation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
phosphatidyl-L-serine
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in 100 mM potassium phosphate, pH 6.8, 10 mM EDTA, and 0.05% Triton X-100
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PISD_HUMAN
409
0
46672
Swiss-Prot
Mitochondrion (Reliability: 4)
B4DPS3_HUMAN
326
0
37436
TrEMBL
Mitochondrion (Reliability: 4)
A0A024R1K5_HUMAN
375
0
43047
TrEMBL
Mitochondrion (Reliability: 4)
B1AKM6_HUMAN
262
0
30258
TrEMBL
Mitochondrion (Reliability: 4)
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
stable upon acid quenching with 69 mM HCl
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, 72 h, remains stable
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in HEK 293F cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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phosphatidylserine decarboxylase PISD is downregulated by 8fold in migratory cells. Breast cancer cells overexpressing PISD exhibit reduced tumor-initiating potential in a high-throughput microfluidic mammosphere device and mouse xenograft model
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Voelker, D.R.
Phosphatidylserine decarboxylase
Biochim. Biophys. Acta
1348
236-244
1997
Arabidopsis thaliana, Caenorhabditis elegans, Escherichia coli, Homo sapiens, Mammalia, Mus musculus, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Dowhan, W.
Phosphatidylserine decarboxylases: pyruvoyl-dependent enzymes from bacteria to mammals
Methods Enzymol.
280
81-88
1997
Saccharomyces cerevisiae, Cricetulus griseus, Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Forbes, C.D.; Toth, J.G.; Ozbal, C.C.; Lamarr, W.A.; Pendleton, J.A.; Rocks, S.; Gedrich, R.W.; Osterman, D.G.; Landro, J.A.; Lumb, K.J.
High-throughput mass spectrometry screening for inhibitors of phosphatidylserine decarboxylase
J. Biomol. Screen.
12
628-634
2007
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.; Humphries, B.; Brien, R.; Gibbons, A.; Chen, Y.; Qyli, T.; Haley, H.; Pirone, M.; Chiang, B.; Xiao, A.; Cheng, Y.; Luan, Y.; Zhang, Z.; Cong, J.; Luker, K.; Luker, G.; Yoon, E.
Functional isolation of tumor-initiating cells using microfluidic-based migration identifies phosphatidylserine decarboxylase as a key regulator
Sci. Rep.
8
244
2018
Homo sapiens
Manually annotated by BRENDA team