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 hide
4.1.1.65
-
RECOMMENDED NAME
GeneOntology No.
phosphatidylserine decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphatidyl-L-serine = phosphatidylethanolamine + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
-
Glycerophospholipid metabolism
-
-
Metabolic pathways
-
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phosphatidylethanolamine biosynthesis I
-
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phosphatidylethanolamine bioynthesis
-
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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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
calf
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain GS115
-
-
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
-
-
-
Manually annotated by BRENDA team
strain FY1679
-
-
Manually annotated by BRENDA team
strain SP870
-
-
Manually annotated by BRENDA team
strain SP870
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
low activity
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
247% stimulation at 15 mM
Ca2+
-
170% stimulation at 15 mM
Mg2+
-
102% stimulation at 15 mM
additional information
-
no requirement for divalent metal ions
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,4-Dinitrophenol
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-
4-Bromo-3-hydroxybenzyloxyamine
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-
Bile salt detergents
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inactivation by dissociating the oligomeric enzyme
Cyanoborohydride
cycloserine
-
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D-penicillamine
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deoxypyridoxine
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reversion by pyridoxal phosphate
Hydrazines
hydroxylamine
Ionic detergents
Isonicotinic acid hydrazide
-
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L-Penicillamine
-
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N-Dodecyl-N,N-dimethyl-3-ammonio-1-propanesulfonate
-
-
NaBH4
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in presence of an amine
NaCNBH3
-
in presence of an amine
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Nonionic detergents
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e.g. Brij 35 or Tween 80, partial
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O-Benzylhydroxylamine
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-
p-hydroxymercuribenzoate
phosphatidylinositol
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-
Thiosemicarbazide
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-
Triton X-100
Zwitterionic detergents
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inactivation by dissociating the oligomeric enzyme
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additional information
-
DMSO has no discernable effect on product formation
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cutsum
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maximal activity in presence of 0.1% cutsum
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Nonionic detergents
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e.g. Triton X-100, absolute requirement
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Pdr17
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the presence of a phosphatidylinositol transfer protein called Pdr17 is required for Psd2 function
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pyruvate
sodium taurocholate
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maximal activity in presence of 0.1% sodium taurocholate
Triton X-100
additional information
-
optimal activity under anaerobic conditions
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.067 - 63
phosphatidyl-L-serine
0.04 - 6.5
phosphatidylserine
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0035
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-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8.5
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pH 6.0: about 35% of maximal activity, pH 8.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37 - 40
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-
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 50
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35°C: about 60% of maximal activity, 50°C: about 25% of maximal activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
phosphatidylserine decarboxylase 1
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
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SDS-PAGE
55000
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gel filtration
60000 - 170000
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sucrose density gradient centrifugation, in presence of Triton
100000 - 200000
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gel filtration
170000
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sucrose density gradient centrifugation in absence of Triton
200000
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gel filtration in presence of Triton X-100
400000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
oligomer
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x * 60000, probably a trimer, SDS-PAGE after treatment with 2-mercaptoethanol
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
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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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 7.5
-
maximal stability in the range
4786
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
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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
LITERATURE
presence of 5 mM 2-mercaptoethanol, 1 mM EDTA, and 10% glycerol stabilizes
-
stable upon acid quenching with 69 mM HCl
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, in 0.02 M maleate buffer, pH 5.8, 4 mM EDTA, more than 90% loss of activity after 7 days
-
-25°C, pH 6.0-7.8, 10% glycerol, 0.1% Triton X-100, stable for 1.5 years. 0°C, stable for several months. Room temperature, stable for at least 1 week
-
-80°C to -20°C, stable for several years
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-80°C, 72 h, remains stable
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0°C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+-nitrilotriacetic acid-agarose affinity column chromatography, and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli EH150 cells; expressed in Escherichia coli EH150 cells; expressed in Escherichia coli EH150 cells
expressed in Escherichia coli strain Rosetta (DE3) or Sf-9 insect cells
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expressed in HEK 293F cells
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expressed in Saccharomyces cerevisiae, Escherichia coli strain BL21 and Escherichia coli strain Rosetta
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the 46000 Da pssC gene product is converted into mature phosphatidylserine decarboxylase through multiple steps of post-translational processing
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the specific enzyme activity increases by 3fold during the replication of Toxoplasma gondii
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Psd+/-
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mice appear normal
Psd-/-
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PSD-deficient mice do not survive beyond embryonic day 9
G315A
no processing of pro-enzyme, pro-enzyme is inactive
G315A/S316A
no processing of pro-enzyme, pro-enzyme is inactive
S316A
no processing of pro-enzyme
S316T
no processing of pro-enzyme
V314L/S317T
processing occurs to a slightly greater extent as in wild type, enzyme is twice as active
LGS461AAA
replaced the LGS tripeptide starting at position 461 with three alanine residues with the goal of preventing normal enzymatic maturation
CS111 mutant
pss-deficient mutant, forms fewer nodules than the wild type on its alfalfa host plant. Membrane lipid composition between mutants and wild type differs
MAV01 mutant
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
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