Information on EC 4.1.1.65 - phosphatidylserine decarboxylase

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

EC NUMBER
COMMENTARY
4.1.1.65
-
RECOMMENDED NAME
GeneOntology No.
phosphatidylserine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
show the reaction diagram
a Schiff base is formed by addition of the amino group of phosphatidylserine to the pyruvate residue of the enzyme as an essential step in the action of the decarboxylase
-
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
show the reaction diagram
reaction is completely stereospecific with overall retention of configuration
-
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
show the reaction diagram
decarboxylation via Schiff base formation between a covalently bound pyruvoyl prosthetic group and the amine of serine
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
decarboxylation
Q9FDI9
-
PATHWAY
KEGG Link
MetaCyc Link
Glycerophospholipid metabolism
-
Metabolic pathways
-
phosphatidylethanolamine biosynthesis I
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Decarboxylase, phosphatidylserine
-
-
-
-
phosphatidyl serine decarboxylase
-
-
Phosphatidylserine decarboxylase
-
-
-
-
Phosphatidylserine decarboxylase
-
-
Phosphatidylserine decarboxylase
P39006
-
Phosphatidylserine decarboxylase
Saccharomyces cerevisiae FY1679
-
-
-
Phosphatidylserine decarboxylase
Q9FDI9
-
phosphatidylserine decarboxylase 1
-
-
phosphatidylserine decarboxylase 2
-
-
PISD
-
-
PS decarboxylase
-
-
-
-
PS decarboxylase
A4GNA8, A4GNA9, Q84V22
-
PS decarboxylase
-
-
PS decarboxylase
-
-
PS decarboxylase
Q9FDI9
-
PSD
-
-
-
-
PSD
Saccharomyces cerevisiae FY1679
-
-
-
PSD
Schizosaccharomyces pombe SP870
-
-
-
PSD1
-
-
PSD1
-
isoform
Psd1 enzyme
P39006
-
Psd1p
-
isoform
Psd1p
Saccharomyces cerevisiae FY1679
-
isoform
-
PSD2
-
isoform
Psd2p
-
isoform
Psd2p
Saccharomyces cerevisiae FY1679
-
isoform
-
CAS REGISTRY NUMBER
COMMENTARY
9054-78-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
calf
-
-
Manually annotated by BRENDA team
ATCC 19398
-
-
Manually annotated by BRENDA team
barely detectable
-
-
Manually annotated by BRENDA team
a strain harboring a hybrid plasmid in which the level of the enzyme phosphatidylserine decarboxylase may be 40 to 50times higher than wild-type levels
-
-
Manually annotated by BRENDA team
strain GS115
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
barley detectable
-
-
Manually annotated by BRENDA team
Micrococcus cerificans
-
-
-
Manually annotated by BRENDA team
parasite-encoded enzyme in human erythrocytes
SwissProt
Manually annotated by BRENDA team
adult, i.e. 4-month-old, and aged, i.e. 30-month-old
-
-
Manually annotated by BRENDA team
strain FY1679
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae FY1679
strain FY1679
-
-
Manually annotated by BRENDA team
Schizosaccharomyces pombe SP870
strain SP870
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
deletion of PSD1 and/or PSD2 leads to depletion of total cellular and plasma membrane phosphatidylethanolamine level, whereas mutation in the other pathways has practically no effect
malfunction
-
mutants carrying deletions in any one or two psd genes are viable in complex rich medium and synthetic defined minimal medium. However, mutants carrying deletions in all three psd genes (psd1-3DELTA mutants) grow slowly in rich medium and are inviable in minimal medium. psd1-3_DELTAcells appear morphologically indistinguishable from wild type cells in medium supplemented with ethanolamine, but when cultured in nonsupplemented medium, they produce high frequencies of abnormally shaped cells as well as cells exhibiting severe septation defects, including multiple, mispositioned, deformed, and misoriented septa.
malfunction
-
deletion of isoform PSD1 causes loss of PSD activity in mitochondria, a severe growth defect on minimal media, and depletion of cellular and mitochondrial phosphatidylethanolamine levels. This defect cannot be compensated by Psd2p. In the homogenate of psd2DELTA, the PSD activity is only slightly reduced, whereas in psd1DELTA total PSD activity is only 25% of wild type
malfunction
-
loss of Psd2 causes cells to acquire sensitivity to cadmium even though Psd1 remains intact, loss of Psd2 causes a specific reduction in vacuolar membrane phosphatidylethanolamine levels, whereas total phosphatidylethanolamine levels are not significantly affected
malfunction
-
psd1 and psd2 deletion mutants exhibit defects in filamentous growth
malfunction
Saccharomyces cerevisiae FY1679
-
deletion of PSD1 and/or PSD2 leads to depletion of total cellular and plasma membrane phosphatidylethanolamine level, whereas mutation in the other pathways has practically no effect
-
malfunction
Schizosaccharomyces pombe SP870
-
mutants carrying deletions in any one or two psd genes are viable in complex rich medium and synthetic defined minimal medium. However, mutants carrying deletions in all three psd genes (psd1-3DELTA mutants) grow slowly in rich medium and are inviable in minimal medium. psd1-3_DELTAcells appear morphologically indistinguishable from wild type cells in medium supplemented with ethanolamine, but when cultured in nonsupplemented medium, they produce high frequencies of abnormally shaped cells as well as cells exhibiting severe septation defects, including multiple, mispositioned, deformed, and misoriented septa.
-
physiological function
-
the psd1, psd2, and psd3 gene products share overlapping functions essential for the normal growth of Schizosaccharomyces pombe cells
physiological function
-
the mitochondrial Psd1 provides roughly 70% of the phosphatidylethanolamine biosynthesis in the cell with Psd2 carrying out the remainder, Psd2 action enhances Ycf1-dependent transport activity
physiological function
-
phosphatidylserine decarboxylase is essential for cell wall integrity and virulence in Candida albicans
physiological function
-
phosphatidylserine decarboxylase is a Toll-like receptor 4 agonist, phosphatidylserine decarboxylase in concentrations as low as 100 ng/ml stimulates RAW264.7 murine macrophage cells and primary peritoneal macrophage cells to secrete tissue necrosis factor alpha and interleukin-6, respectively. PSD induces the production of interleukin-6, in part, via its enzymatic activity
physiological function
Schizosaccharomyces pombe SP870
-
the psd1, psd2, and psd3 gene products share overlapping functions essential for the normal growth of Schizosaccharomyces pombe cells
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
Micrococcus cerificans
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
Q9GPP8
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
A4GNA8, A4GNA9, Q84V22
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
Q9FDI9
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
P39006
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
localization of the phosphatidylserine-specific binding site in the enzyme
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
activity towards natural phosphatidylserine is greater than towards saturated phosphatidylserine
-
-
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
phosphatidylethanolamine formed by phosphatidylserine decarboxylase 2 is the preferred substrate for phosphatidylcholine synthesis, phosphatidylethanolamine formed by phosphatidylserine decarboxylase 2 can be imported into mitochondria, although with moderate efficiency, phosphatidylserine decarboxylase 1 is the major source of cellular and mitochondrial phosphatidylethanolamine
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
high selectivity, preference for the formation of C34:2 and C32:2 species, phosphatidylserine decarboxylase 1, high selectivity, preference for the formation of C34:2 and C32:2 species, phosphatidylserine decarboxylase 2
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
phosphatidyl-L-serine species with a 20:4 fatty acid on the sn-2 position are preferentially decarboxylated
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
Schizosaccharomyces pombe SP870
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
Saccharomyces cerevisiae FY1679
-
-
-
-
?
Phosphatidyl-L-serine
?
show the reaction diagram
-
-
-
-
-
Phosphatidyl-L-serine
?
show the reaction diagram
-
important enzyme in the synthesis of phosphatidylethanolamine
-
-
-
Phosphatidyl-L-serine
?
show the reaction diagram
-
the enzyme catalyzes the final step in the biosynthesis of phosphatidylethanolamine
-
-
-
additional information
?
-
-
the enzyme has both phosphatidylserine decarboxylase activity and phospholipid N-methyltransferase activity or two enzymes with identical electrophotetic properties
-
-
-
additional information
?
-
-
side chain preferrence of phosphatidylserine in liver in decreasing order: 18:0/18:1, 18:0/22:6, 18:0/20:4, side chain preferrence of phosphatidylserine in brain in decreasing order: 18:0/22:6, 18:0/18:1, 18:0/20:4
-
?
additional information
?
-
-
substrate preference of liver and cerebellum enzyme concerning 22:6n-3 content changes during aging
-
?
additional information
?
-
-
substrate transport to enzyme implicates specific lipid domains with pure phosphatidylserine vesicles being most effective
-
?
additional information
?
-
-
effect of the enzyme in neural excitation. The carboxyl groups of phosphatidylserine function as ion exchange sites in the nerve membrane
-
-
-
additional information
?
-
-
the level of enzyme activity is partially and reversibly suppressed by inositol and further diminished by the combination of inositol and choline
-
-
-
additional information
?
-
-
enzyme of the phospholipid metabolism
-
-
-
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
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
Q9FDI9
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
P39006
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
-
phosphatidylethanolamine formed by phosphatidylserine decarboxylase 2 is the preferred substrate for phosphatidylcholine synthesis, phosphatidylethanolamine formed by phosphatidylserine decarboxylase 2 can be imported into mitochondria, although with moderate efficiency, phosphatidylserine decarboxylase 1 is the major source of cellular and mitochondrial phosphatidylethanolamine
-
-
?
Phosphatidyl-L-serine
?
show the reaction diagram
-
-
-
-
-
Phosphatidyl-L-serine
?
show the reaction diagram
-
important enzyme in the synthesis of phosphatidylethanolamine
-
-
-
Phosphatidyl-L-serine
?
show the reaction diagram
-
the enzyme catalyzes the final step in the biosynthesis of phosphatidylethanolamine
-
-
-
additional information
?
-
-
effect of the enzyme in neural excitation. The carboxyl groups of phosphatidylserine function as ion exchange sites in the nerve membrane
-
-
-
additional information
?
-
-
the level of enzyme activity is partially and reversibly suppressed by inositol and further diminished by the combination of inositol and choline
-
-
-
additional information
?
-
-
enzyme of the phospholipid metabolism
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
247% stimulation at 15 mM
Ca2+
-
170% stimulation at 15 mM
Mg2+
-
102% stimulation at 15 mM
Mn2+
-
24% stimulation at 15 mM
Mn2+
-
stimulation up to 2-fold
additional information
-
no requirement for divalent metal ions
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,4-Dinitrophenol
-
-
4-Bromo-3-hydroxybenzyloxyamine
-
-
Bile salt detergents
-
inactivation by dissociating the oligomeric enzyme
Cyanoborohydride
-
inactivation in presence of phosphatidylserine, no inactivation in absence of phosphatidylserine
Cyanoborohydride
-
-
Cycloserine
-
-
D-penicillamine
-
-
Deoxypyridoxine
-
reversion by pyridoxal phosphate
Hydrazines
-
phenylhydrazine
Hydrazines
-
in presence of an amine
hydroxylamine
-
irreversible
hydroxylamine
-
-
hydroxylamine
-
-
hydroxylamine
-
-
hydroxylamine
-
in presence of an amine
Ionic detergents
-
e.g., Barlox-12, SDS
-
Ionic detergents
-
e.g. SDS or cetyl trimethylammonium bromide, strong
-
Isonicotinic acid hydrazide
-
-
N-Dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate
-
-
NaBH4
-
in presence of an amine
NaCNBH3
-
in presence of an amine
-
Nonionic detergents
-
e.g. Brij 35 or Tween 80, partial
-
O-Benzylhydroxylamine
-
-
p-hydroxymercuribenzoate
-
-
p-hydroxymercuribenzoate
-
-
Thiosemicarbazide
-
-
Triton X-100
-
effect is related to the molar ratio of triton to phospholipid
Triton X-100
-
Triton X-100, maximal activity, independent of phosphatidylserine concentration is expressed at Triton to phospholipid ration of 5.6, inhibition at a molar ratio higher than 5.6
Zwitterionic detergents
-
inactivation by dissociating the oligomeric enzyme
-
L-Penicillamine
-
-
additional information
-
DMSO has no discernable effect on product formation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Nonionic detergents
-
e.g. Triton X-100, absolute requirement
-
Pdr17
-
the presence of a phosphatidylinositol transfer protein called Pdr17 is required for Psd2 function
-
pyruvate
-
dependent on
pyruvate
-
the small subunit contains a pyruvoyl prosthetic group
pyruvate
-
the pyruvoyl residue is covalently bound to the amino terminus of one of the two nonidentical subunits
pyruvate
-
dependent on; the pyruvate prosthetic group is in amide linkage to the amino terminus of the alpha-subunit. The prosthetic group is derived from Ser through a post-tranlational cleavage of a proenzyme
sodium taurocholate
-
maximal activity in presence of 0.1% sodium taurocholate
Triton X-100
-
-
Triton X-100
-
maximal activity, independent of phosphatidylserine concentration is expressed at Triton to phospholipid ratio of 5.6, inhibition at a molar ratio higher than 5.6
Triton X-100
Q9GPP8
enzyme activity depends on presence of Triton X-100, optimum concentration 0.052%
Cutsum
-
maximal activity in presence of 0.1% cutsum
-
additional information
-
optimal activity under anaerobic conditions
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.09
-
Phosphatidyl-L-serine
-
in 100 mM potassium phosphate, pH 6.8, 10 mM EDTA, and 0.05% Triton X-100
63
-
Phosphatidyl-L-serine
Q9GPP8
pH 6.8, recombinant enzyme
0.04
-
phosphatidylserine
-
-
0.067
-
phosphatidylserine
-
-
0.4
-
phosphatidylserine
-
natural
1.5
-
phosphatidylserine
-
saturated
2.4
-
phosphatidylserine
-
-
6.5
-
phosphatidylserine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0035
-
-
-
0.032
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.8
-
Q9GPP8
strictly pH-dependent
7
-
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8.5
-
pH 6.0: about 35% of maximal activity, pH 8.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
40
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
50
-
35C: about 60% of maximal activity, 50C: about 25% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
chemoheterotrophically and phototrophically grown
Manually annotated by BRENDA team
A4GNA8, A4GNA9, Q84V22
-
Manually annotated by BRENDA team
A4GNA8, A4GNA9, Q84V22
-
Manually annotated by BRENDA team
A4GNA8, A4GNA9, Q84V22
-
Manually annotated by BRENDA team
A4GNA8, A4GNA9, Q84V22
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
phosphatidylserine decarboxylase 2
Manually annotated by BRENDA team
Saccharomyces cerevisiae FY1679
-
isoform Psd2p
-
Manually annotated by BRENDA team
-
high activity in cytoplasmic membrane and low activity in outer membrane of the cell envelope
Manually annotated by BRENDA team
-
intrinsic membrane protein
Manually annotated by BRENDA team
-
external side of the inner membrane
Manually annotated by BRENDA team
-
exclusively in the inner mitochondrial membrane
Manually annotated by BRENDA team
-
inner mitochondrial membrane and Golgi/vacuole membrane
Manually annotated by BRENDA team
-
associated with cytoplasmic membrane
Manually annotated by BRENDA team
-
plasma membrane
Manually annotated by BRENDA team
-
exclusively in the inner mitochondrial membrane; phosphatidylserine flows from the outer membrane to the inner membrane through contact sites between inner and outer membrane to become decarboxylated and the formed phosphatidylethanolamine flows directly back to the outer membrane, without mixing with inner membrane phosphatidylamine
Manually annotated by BRENDA team
Bacillus subtilis Marburg
-
septal
-
Manually annotated by BRENDA team
A4GNA8, A4GNA9, Q84V22
-
-
Manually annotated by BRENDA team
-
external side of the inner membrane
Manually annotated by BRENDA team
-
exclusively in the inner mitochondrial membrane
Manually annotated by BRENDA team
-
exclusively in the inner mitochondrial membrane
Manually annotated by BRENDA team
-
phosphatidylserine decarboxylase 1
Manually annotated by BRENDA team
-
membrane of mitochondria
Manually annotated by BRENDA team
A4GNA8, A4GNA9, Q84V22
-
Manually annotated by BRENDA team
-
inner mitochondrial membrane, isoform Psd1p
Manually annotated by BRENDA team
Saccharomyces cerevisiae FY1679
-
inner mitochondrial membrane, isoform Psd1p
-
Manually annotated by BRENDA team
A4GNA8, A4GNA9, Q84V22
-
-
Manually annotated by BRENDA team
-
phosphatidylserine decarboxylase 2
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35000
-
-
SDS-PAGE
60000
170000
-
sucrose density gradient centrifugation, in presence of Triton
65000
-
-
gel filtration in presence of 4 mM EDTA
65000
-
-
non-denaturing PAGE
100000
200000
-
gel filtration
170000
-
-
sucrose density gradient centrifugation in absence of Triton
200000
-
-
gel filtration in presence of Triton X-100
400000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 36500, SDS-PAGE
?
Q9GPP8
x * 42600, deduced from gene sequence, x * 35000, SDS-PAGE
dimer
-
1 * 3545, alpha, + 1 * 44172, beta
dimer
-
1 * 1090, alpha, + 1 * 118868, beta, enzyme form PSD2; 1 * 4192, alpha, + 1 * 52367, beta, enzyme form PSD1
dimer
-
x * 7332, alpha, + x * 28579, beta, the heterodimeric enzyme appears to form a defined multimeric structure in the absence of detergent and associate with detergent micelles to form a large detergent micelle-protein complex which is still made up of some multiple of the heterodimer
dimer
-
1 * 7332, alpha, + 1 * 28579, beta, calculation from nucleotide sequence
oligomer
-
x * 60000, probably a trimer, SDS-PAGE after treatment with 2-mercaptoethanol
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
the enzyme is synthesized as a single subunit proenzyme form, pi subunit, 35579 Da, which undergoes posttranslational processing in which an internal Ser residue becomes the covalently bound prosthetic group of one of the two resulting subunits
proteolytic modification
-
the proenzyme is sequentially processed from a size of 46000 Da to 34000 Da. Sequential removal of the mitochondrial targeting and inner membrane sorting sequence, followed by formation of the alpha and beta subunits. The final step in maturation is proposed to be cleavage and concerted prosthetic group attachment to the alpha subunit
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
maximal stability in the range
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
-
stable in presence of phosphatidylserine, 75% loss of activity in presence of Triton without phosphatidylserine present
65
-
-
10 min, 50% loss of activity, membrane-associated enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
stable upon acid quenching with 69 mM HCl
-
presence of 5 mM 2-mercaptoethanol, 1 mM EDTA, and 10% glycerol stabilizes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-25C, pH 6.0-7.8, 10% glycerol, 0.1% Triton X-100, stable for 1.5 years. 0C, stable for several months. Room temperature, stable for at least 1 week
-
-80C to -20C, stable for several years
-
0C, stable for several months
-
-80C, 72 h, remains stable
-
-20C, in 0.02 M maleate buffer, pH 5.8, 4 mM EDTA, more than 90% loss of activity after 7 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli EH150 cells; expressed in Escherichia coli EH150 cells; expressed in Escherichia coli EH150 cells
A4GNA8, A4GNA9, Q84V22
the 46000 Da pssC gene product is converted into mature phosphatidylserine decarboxylase through multiple steps of post-translational processing
-
expressed in HEK 293F cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
S254C
-
S254C and S254T are posttranslationally processed and active enzyme is made in vivo although in significantly reduced amounts. From the S254A mutant only the proenzyme form is made, which has no enzymatic activity. In the case of the S254C and S254T mutant proteins about 10-20% of the proenzyme is processed to the alpha and beta subunits, resulting in 15% and 2%, respectively of the level of activity of the wild-type enzyme
S254C
-
mutant proenzymes S254C and S254T are cleaved with a half-life of around 2-4 h, the S254A proenzyme does not undergo processing. Mutants encoding the S254C and S254T protein produce 16% and 2% respectively of the activity of the wild-type allele. The hydroxyl group of Ser254 plays a critical role in the cleavage of the peptide bond between Gly253 and Ser254 of the phosphatidylserine decarboxylase
S254T
-
S254C and S254T are posttranslationally processed and active enzyme is made in vivo although in significantly reduced amounts. From the S254A mutant only the proenzyme form is made, which has no enzymatic activity. In the case of the S254C and S254T mutant proteins about 10-20% of the proenzyme is processed to the alpha and beta subunits, resulting in 15% and 2%, respectively of the level of activity of the wild-type enzyme
S254T
-
mutant proenzymes S254C and S254T are cleaved with a half-life of around 2-4 h, the S254A proenzyme does not undergo processing. Mutants encoding the S254C and S254T protein produce 16% and 2% respectively of the activity of the wild-type allele. The hydroxyl group of Ser254 plays a critical role in the cleavage of the peptide bond between Gly253 and Ser254 of the phosphatidylserine decarboxylase
Psd+/-
-
mice appear normal
Psd-/-
-
PSD-deficient mice do not survive beyond embryonic day 9
G315A
Q9GPP8
no processing of pro-enzyme, pro-enzyme is inactive
G315A/S316A
Q9GPP8
no processing of pro-enzyme, pro-enzyme is inactive
S316A
Q9GPP8
no processing of pro-enzyme
S316T
Q9GPP8
no processing of pro-enzyme
V314L/S317T
Q9GPP8
processing occurs to a slightly greater extent as in wild type, enzyme is twice as active
CS111 mutant
Q9FDI9
pss-deficient mutant, forms fewer nodules than the wild type on its alfalfa host plant. Membrane lipid composition between mutants and wild type differs
additional information
-
enzyme knockout mutant, 6- to 9fold more mitochondrial enzyme mRNA and 9fold more mitochondrial enzyme activity, total enzyme activity in membranes is unchanged
additional information
A4GNA8, A4GNA9, Q84V22
triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity; triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity; triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity
LGS461AAA
P39006
replaced the LGS tripeptide starting at position 461 with three alanine residues with the goal of preventing normal enzymatic maturation
additional information
-
deletion of C2 homology domain and/or Golgi retention/localization domain of PSD2, both single deletion mutants are catalytically active and proteins localize normally, c2 deletion mutant has a severe defect in formation of phosphatidylethanolamin in both intact and permeabilized cells
additional information
-
deletion of PSD1 leads to a significant depletion of phosphatidylethanolamine in mitochondria and whole cells, in mitochondria of a psd1/psd2 double mutant phosphatidylethanolamine drops to a minimum level and also cardiolipin level decreases, in psd2 mutants, phosphatidylcholine levels decrease
additional information
P39006
fluorescence microscopy, different GFP-tagged versions of Psd1
MAV01 mutant
Q9FDI9
MAV01/pRK404, MAV01/pTB2086. Sinorhizobial psd gene is deleted, accumulated PS to about 20% of total lipids when grown in complex growth medium, forms fewer nodules than the wild type on its alfalfa host plant. Nodule formation in the mutant MAV01 sets in about 20 days later than that in the wild type. Leaves of alfalfa plants inoculated with the mutant MAV01 are yellowish, indicating that the plants are starved for nitrogen. Membrane lipid composition between mutants and wild type differs
additional information
Q9FDI9
properties of PE-deficient mutants lacking either Pss or Psd are compared with those of the Sinorhizobium meliloti wild type. Mutants deficient in phosphatidylserine decarboxylase, accumulate phosphatidylserine and are strongly affected during symbiosis with alfalfa. PE-deficient mutants grow in a wild-type-like manner on many complex media, they are unable to grow on minimal medium containing high phosphate concentrations. The psd-deficient mutant can grow on minimal medium containing low concentrations of inorganic phosphate, while the pss-deficient mutant can not. Addition of choline to the minimal medium rescued growth of the pss-deficient mutant, CS111, to some extent but inhibited growth of the psd-deficient mutant, MAV01
additional information
-
enzyme cDNA lacking the targeting sequence and a chimeric construct in which the targeting and sorting sequences were replaced by those from yeast PSD1, both complemented the ethanolamine requirement of a yeast psd1 psd2 mutant, enzyme activity is detected in mitochondria of the complemented cells