Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
additional information
?
-
phosphatidyl-L-serine
?
-
-
-
-
?
phosphatidyl-L-serine
?
-
the enzyme catalyzes the final step in the biosynthesis of phosphatidylethanolamine
-
-
?
phosphatidyl-L-serine
?
-
important enzyme in the synthesis of phosphatidylethanolamine
-
-
?
phosphatidyl-L-serine
?
-
important enzyme in the synthesis of phosphatidylethanolamine
-
-
?
phosphatidyl-L-serine
?
-
important enzyme in the synthesis of phosphatidylethanolamine
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
localization of the phosphatidylserine-specific binding site in the enzyme
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
phosphatidyl-L-serine species with a 20:4 fatty acid on the sn-2 position are preferentially decarboxylated
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
Micrococcus cerificans
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
phosphatidyl-L-serine species with a 20:4 fatty acid on the sn-2 position are preferentially decarboxylated
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
661239, 661240, 693510, 694089, 702464, 705619, 727269, 727929, 727932, 727991, 728629 -
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
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
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
phosphatidylserine decarboxylase 1 is the major source of cellular and mitochondrial phosphatidylethanolamine
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
high selectivity, preference for the formation of C34:2 and C32:2 species, phosphatidylserine decarboxylase 1
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
high selectivity, preference for the formation of C34:2 and C32:2 species, phosphatidylserine decarboxylase 2
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
activity towards natural phosphatidylserine is greater than towards saturated phosphatidylserine
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
liposomal phosphatidyl-L-serine
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
liposomal phosphatidyl-L-serine
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
?
Phosphatidyl-L-serine
Phosphatidylethanolamine + CO2
-
-
-
-
?
additional information
?
-
-
enzyme of the phospholipid metabolism
-
-
?
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
?
-
-
effect of the enzyme in neural excitation. The carboxyl groups of phosphatidylserine function as ion exchange sites in the nerve membrane
-
-
?
additional information
?
-
-
substrate transport to enzyme implicates specific lipid domains with pure phosphatidylserine vesicles being most effective
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
metabolism
the stability of endogenous Psd1 is influenced by inner membrane protease Yme1
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
-
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
-
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
-
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
-
psd1 and psd2 deletion mutants exhibit defects in filamentous growth
malfunction
-
the psd1-deficient strain shows reduced fusion kinetics and also has impaired mitochondrial activity such as oxidative phosphorylation and reduced mitochondrial ATP levels. The loss of Psd1 also impairs the biogenesis of s-Mgm1, a protein essential for mitochondrial fusion
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
-
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
-
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
-
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
-
phosphatidylserine decarboxylase is essential for cell wall integrity and virulence in Candida albicans
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
-
the psd1, psd2, and psd3 gene products share overlapping functions essential for the normal growth of Schizosaccharomyces pombe cells
physiological function
-
isoform PSD1 reduces externalized phosphatidylserine on host cells, enabling evasion of phagocytosis
physiological function
-
phosphatidylethanolamine from phosphatidylserine decarboxylase2 (PSD2) is essential for autophagy under cadmium stress in Saccharomyces cerevisiae. Overexpression of PSD2 confers resistance to cadmium
physiological function
-
Psd1 is required for normal mitochondrial morphology, proper mitochondrial fusion during yeast mating, and proper mitochondrial activity
physiological function
-
the enzyme is required for an optimal parasite growth and replication
physiological function
after 4 days of gene silencing, procyclic forms of Trypanosoma brucei show a growth defect compared to control parasites, while growth of PSD-depleted bloodstream forms is only slightly affected. In both life cycle forms, down-regulation of TbPSD leads to mitochondrial fragmentation and a decrease in ATP production via oxidative phosphorylation of more than 75% in PSD-depleted mitochondria
physiological function
enzyme is able to complement a Saccharomyces cerevisiae PSD mutant lacking PSD1 and PSD2 and DPL1 activities
physiological function
enzyme is responsible for remodeling of human phosphatidylserine to bacterial phosphatidylethanolamine in human pathogen Chlamydia trachomatis
physiological function
the plasma membrane of a isoforms Psd1/Psd2 double mutant strain displays increased membrane fluidity and reduced plasma membrane dipole potential. In comparison to wild-type, the apparent phase transition temperature is reduced by about 3°C in the mutant strain. The mutant shows high diffusion of fluorescent dye rhodamine 6G and radiolabelled fluconazole, resulting in an increased drug accumulation in the mutant cells, and in an increased susceptibility to azoles
physiological function
the plasma membrane of isoforms Psd1/Psd2 double mutant strain displays increased membrane fluidity and reduced plasma membrane dipole potential. In comparison to wild-type, the apparent phase transition temperature is reduced by about 3°C in the mutant strain. The mutant shows high diffusion of fluorescent dye rhodamine 6G and radiolabelled fluconazole, resulting in an increased drug accumulation in the mutant cells, and in an increased susceptibility to azoles
physiological function
-
phosphatidylethanolamine from phosphatidylserine decarboxylase2 (PSD2) is essential for autophagy under cadmium stress in Saccharomyces cerevisiae. Overexpression of PSD2 confers resistance to cadmium
-
physiological function
-
enzyme is responsible for remodeling of human phosphatidylserine to bacterial phosphatidylethanolamine in human pathogen Chlamydia trachomatis
-
physiological function
-
the plasma membrane of a isoforms Psd1/Psd2 double mutant strain displays increased membrane fluidity and reduced plasma membrane dipole potential. In comparison to wild-type, the apparent phase transition temperature is reduced by about 3°C in the mutant strain. The mutant shows high diffusion of fluorescent dye rhodamine 6G and radiolabelled fluconazole, resulting in an increased drug accumulation in the mutant cells, and in an increased susceptibility to azoles
-
physiological function
-
the plasma membrane of isoforms Psd1/Psd2 double mutant strain displays increased membrane fluidity and reduced plasma membrane dipole potential. In comparison to wild-type, the apparent phase transition temperature is reduced by about 3°C in the mutant strain. The mutant shows high diffusion of fluorescent dye rhodamine 6G and radiolabelled fluconazole, resulting in an increased drug accumulation in the mutant cells, and in an increased susceptibility to azoles
-
physiological function
-
after 4 days of gene silencing, procyclic forms of Trypanosoma brucei show a growth defect compared to control parasites, while growth of PSD-depleted bloodstream forms is only slightly affected. In both life cycle forms, down-regulation of TbPSD leads to mitochondrial fragmentation and a decrease in ATP production via oxidative phosphorylation of more than 75% in PSD-depleted mitochondria
-
physiological function
-
the psd1, psd2, and psd3 gene products share overlapping functions essential for the normal growth of Schizosaccharomyces pombe cells
-
physiological function
-
isoform PSD1 reduces externalized phosphatidylserine on host cells, enabling evasion of phagocytosis
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Psd+/-
-
mice appear normal
Psd-/-
-
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
D139A
mutation prevents processing of the proenzyme
D139N
mutation prevents processing of the proenzyme
G307A
mutation eliminates processing
G307P
mutation eliminates processing
H195A
mutation produces significant levels of enzyme processing, although the level of the beta-subunit is reduced compared with wild-type
H195A/H198A
mutation prevents processing of the proenzyme
H198A
mutation prevents processing of the proenzyme
S*308A
mutation eliminates processing
S*308T
mutation eliminates processing
S309A
proenzyme is processed comparably to wild-type, modest reductions in catalytic activity
S309T
proenzyme is processed comparably to wild-type, modest reductions in catalytic activity
D139N
-
mutation prevents processing of the proenzyme
-
H195A
-
mutation produces significant levels of enzyme processing, although the level of the beta-subunit is reduced compared with wild-type
-
H198A
-
mutation prevents processing of the proenzyme
-
S309A
-
proenzyme is processed comparably to wild-type, modest reductions in catalytic activity
-
S309T
-
proenzyme is processed comparably to wild-type, modest reductions in catalytic activity
-
G462A
mutation in the conserved LGST motif, mutant retains some, albeit reduced, phosphatidylserine decarboxylase activity
G482P
mutation in conserved glycin residue, no major growth defect. The autocatalytic processing of G482P imported into mitochondria is delayed
G488P
mutation in conserved glycin residue, causes a dramatic growth defect of the mutant similar to that observed for a gene deletion mutant
G492P
mutation in conserved glycin residue, no major growth defect
K356/RF397L/E429G/M448T
mutations in beta-subunit. Mutant is temperature sensitive and autocatalytically impaired. Inner membrane proteases, Oma1p and Yme1p are responsible for degradation of the mutant precursor. Upon heat exposure postautocatalysis, mutant subunits accumulate in protein aggregates that are resolved by Yme1p acting alone, while the released alpha subunit is degraded in parallel by an unidentified protease
K486A
mutation of the the most conserved Lys486 residue
L461A
mutation in the conserved LGST motif, mutant retains some, albeit reduced, phosphatidylserine decarboxylase activity
LGS461AAA
replaced the LGS tripeptide starting at position 461 with three alanine residues with the goal of preventing normal enzymatic maturation
T464I
mutation in the conserved LGST motif, mutant retains some, albeit reduced, phosphatidylserine decarboxylase activity
S463A
-
the mutant does not display detectable decarboxylase activity due to the inability to generate the active site of the enzyme
-
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
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
S463A
-
the mutant does not display detectable decarboxylase activity due to the inability to generate the active site of the enzyme
S463A
mutation of the conserved serine residue, completely abolishes decarboxylase activity
S318A
mutation in putative cleavage motif, inhibits processing of the proenzyme. Mutant corrextly localizes to the mitochondrion
S318A
-
mutation in putative cleavage motif, inhibits processing of the proenzyme. Mutant corrextly localizes to the mitochondrion
-
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
triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity
additional information
triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity
additional information
triple mutant, psd1 psd2 psd3 is totally devoid of PS decarboxylase activity
additional information
amino acids between positions 40 and 70 are critical for proenzyme processing and decarboxylase activity. During progressive removal of 10 amino acid segments between positions 1 and 70 of PSD, deletions up to residue 50 do not reduce the ability of the enzyme to complement a Saccharomyces cerevisiae mutant. Deletions of the first 60 or 70 residues result in loss of complementation in both solid and liquid media
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
fluorescence microscopy, different GFP-tagged versions of Psd1
additional information
-
fluorescence microscopy, different GFP-tagged versions of Psd1
additional information
removal of the complete inner membrane-associated domain IM2 leads to an altered topology of the protein with the soluble domain exposed to the mitochondrial matrix and to decreased enzyme activity. Psd1 variants lacking portions of the N-terminal moiety of IM2 are inserted into the inner mitochondrial membrane with an altered topology. Psd1 variants with deletions of C-terminal portions of IM2 accumulate at the outer mitochondrial membrane and lose their enzyme activity
additional information
-
removal of the complete inner membrane-associated domain IM2 leads to an altered topology of the protein with the soluble domain exposed to the mitochondrial matrix and to decreased enzyme activity. Psd1 variants lacking portions of the N-terminal moiety of IM2 are inserted into the inner mitochondrial membrane with an altered topology. Psd1 variants with deletions of C-terminal portions of IM2 accumulate at the outer mitochondrial membrane and lose their enzyme activity
additional information
removal of three to six amino acids of the conserved motif of the alpha subunit compromises the function of Psd1 as reflected by impaired growth of the mutants. In mutant Ax3, substitution of all positively charged amino acids of the highly conserved motif of the alpha subunit by alanine, the autocatalytic processing after import into mitochondria is delayed
additional information
-
removal of three to six amino acids of the conserved motif of the alpha subunit compromises the function of Psd1 as reflected by impaired growth of the mutants. In mutant Ax3, substitution of all positively charged amino acids of the highly conserved motif of the alpha subunit by alanine, the autocatalytic processing after import into mitochondria is delayed
additional information
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Volker, D.R.; Golden, E.B.
Phosphatidylserine decarboxylase from rat liver
Methods Enzymol.
209
360-365
1992
Rattus norvegicus
brenda
Bell, R.M.; Mavis, R.D.; Osborn, M.J.; Vagelos, P.R.
Enzymes of phospholipid metabolism: localization in the cytoplasmic and outer membrane of the cell envelope of Escherichia coli and Salmonella typhimurium
Biochim. Biophys. Acta
249
628-635
1971
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Cook, A.M.; Low, E.; Ishijimi, M.
Effect of phosphatidyl serine decarboxylase on neural excitation
Nature New Biol.
239
150-151
1972
Rattus norvegicus
brenda
Dowhan, W.; Wickner, W.T.; Kennedy, E.P.
Purification and properties of phosphatidylserine decarboxylase from Escherichia coli
J. Biol. Chem.
249
3079-3084
1974
Escherichia coli
brenda
Suda, T.; Matsuda, M.
Studies on decarboxylation of phosphatidylserine
Biochim. Biophys. Acta
369
331-337
1974
Mus musculus
-
brenda
Warner, T.G.; Dennis, E.A.
Phosphatidylserine decarboxylase: analysis of its action towards unsaturated and saturated phosphatidylserine and the effect of Triton X-100 on activity
Arch. Biochem. Biophys.
167
761-768
1975
Tetrahymena pyriformis
brenda
Warner, T.G.; Dennis, E.A.
Action of the highly purified, membrane-bound enzyme phosphatidylserine decarboxylase Escherichia coli toward phosphatidylserine in mixed micelles and erythrocyte ghosts in the presence of surfactant
J. Biol. Chem.
250
8004-8009
1975
Escherichia coli
brenda
Dutt, A.; Dowhan, W.
Intracellular distribution of enzymes of phospholipid metabolism in several gram-negative bacteria
J. Bacteriol.
132
159-165
1977
Klebsiella aerogenes, Micrococcus cerificans, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens
brenda
Satre, M.; Kennedy, E.P.
Identification of bound pyruvate essential for the activity of phosphatidylserine decarboxylase of Escherichia coli
J. Biol. Chem.
253
479-483
1978
Escherichia coli
brenda
Tyhach, R.J.; Hawrot, E.; Satre, M.; Kennedy, P.
Increased synthesis of phosphatidylserine decarboxylase in a strain of Escherichia coli bearing a hybrid plasmid
J. Biol. Chem.
254
627-633
1979
Escherichia coli
brenda
Hostetler, K.Y.; Zenner, B.D.; Morris, H.P.
Phosphatidylserine biosynthesis in mitochondria from the Morris 7777 hepatoma
J. Lipid Res.
20
607-613
1979
Rattus norvegicus
brenda
Igarashi, K.; Kaneda, M.; Yamaji, A.; Saido, T.C.; Kikkawa, U.; Ono, Y.; Inoue, K.; Umeda, M.
A novel phosphatidylserine-binding peptide motif defined by an anti-idiotypic monoclonal antibody
J. Biol. Chem.
270
29075-29078
1995
Cricetulus griseus
brenda
Rizzolo, L.J.
Kinetics and protein subunit interactions of Escherichia coli phosphatidylserine decarboxylase in detergent solution
Biochemistry
20
868-873
1981
Escherichia coli
brenda
Silber, P.; Borie, R.P.; Mikowski, E.J.; Goldfine, H.
Phospholipid biosynthesis in some anaerobic bacteria
J. Bacteriol.
147
57-61
1981
Clostridium butyricum, Desulfovibrio vulgaris, Escherichia coli, Megasphaera elsdenii, Veillonella parvula
brenda
Hawrot, E.
Phosphatidylserine decarboxylase from Escherichia coli
Methods Enzymol.
71
571-576
1981
Escherichia coli
brenda
Percy, A.K.; Moore, J.F.; Carson, M.A.; Waechter, C.J.
Characterization of brain phosphatidylserine decarboxylase: localization in the mitochondrial inner membrane
Arch. Biochem. Biophys.
223
484-494
1983
Bos taurus, Rattus norvegicus
brenda
Zborowski, J.; Dygas, A.; Wojtczak, L.
Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane
FEBS Lett.
157
179-182
1983
Mus musculus, Rattus norvegicus
brenda
Cain, B.D.; Donohue, T.J.; Shepherd, W.D.; Kaplan, S.
Localization of phospholipid biosynthetic enzyme activities in cell-free fractions derived from Rhodopseudomonas sphaeroides
J. Biol. Chem.
259
942-948
1984
Cereibacter sphaeroides
brenda
Kuchler, K.; Daum, G.; Paltauf, F.
Subcellular and submitochondrial localization of phospholipid-synthesizing enzymes in Saccharomyces cerevisiae
J. Bacteriol.
165
901-910
1986
Saccharomyces cerevisiae
brenda
No, Z.; Sanders, C.R.; Dowhan, W.; Tsai, M.D.
Steric course of the reaction catalyzed by phosphatidylserine decarboxylase from Escherichia coli
Bioorg. Chem.
16
184-188
1988
Escherichia coli
-
brenda
Verma, J.N.; Goldfine, H.
Phosphatidylserine decarboxylase from Clostridium butyricum
J. Lipid Res.
26
610-616
1985
Clostridium butyricum
brenda
Kuge, O.; Saito, K.; Kojima, M.; Akamatsu, Y.; Nishijima, M.
Post-translational processing of the phosphatidylserine decarboxylase gene product in Chinese hamster ovary cells
Biochem. J.
319
33-38
1996
Cricetulus griseus
brenda
Voelker, D.R.
Phosphatidylserine decarboxylase
Biochim. Biophys. Acta
1348
236-244
1997
Arabidopsis thaliana, Saccharomyces cerevisiae, Caenorhabditis elegans, Escherichia coli, Homo sapiens, Mammalia, Mus musculus
brenda
Overmeyer, J.H.; Waechter, C.J.
Regulation of phosphatidylserine decarboxylase in Saccharomyces cerevisiae by inositol and choline: kinetics of repression and derepression
Arch. Biochem. Biophys.
290
511-516
1991
Saccharomyces cerevisiae
brenda
Dowhan, W.
Phosphatidylserine decarboxylases: pyruvoyl-dependent enzymes from bacteria to mammals
Methods Enzymol.
280
81-88
1997
Cricetulus griseus, Escherichia coli, Homo sapiens, Saccharomyces cerevisiae
brenda
Dowhan, W.; Li, Q.X.
Phosphatidylserine decarboxylase from Escherichia coli
Methods Enzymol.
209
348-359
1992
Escherichia coli
brenda
Auchi, L.; Tsvetnitsky, V.; Yeboah, F.A.; Gibbons, W.A.
Purification of plasma membrane rat liver phosphatidylserine decarboxylase
Biochem. Soc. Trans.
21
488S
1993
Rattus norvegicus
brenda
Dygas, A.; Zborowski, J.
Effect of Triton X-100 on the activity and solubilization of rat liver mitochondrial phosphatidylserine decarboxylase
Acta Biochim. Pol.
36
131-141
1989
Rattus norvegicus
brenda
Li, Q.X.; Dowhan, W.
Studies on the mechanism of formation of the pyruvate prosthetic group of phosphatidylserine decarboxylase from Escherichia coli
J. Biol. Chem.
265
4111-4115
1990
Escherichia coli
brenda
Li, Q.X.; Dowhan, W.
Structural characterization of Escherichia coli phosphatidylserine decarboxylase
J. Biol. Chem.
263
11516-11522
1988
Escherichia coli
brenda
Hovius, R.; Faber, B.; Brigot, B.; Nicolay, K.; de Kruijff, B.
On the mechanism of the mitochondrial decarboxylation of phosphatidylserine
J. Biol. Chem.
267
16790-16795
1992
Rattus norvegicus
brenda
Kevala, J.H.; Kim, H.Y.
Determination of substrate preference in phosphatidylserine decarboxylation by liquid chromatography-electrospray ionization mass spectrometry
Anal. Biochem.
292
130-138
2001
Rattus norvegicus
brenda
Kitamura, H.; Wu, W.I.; Voelker, D.R.
The C2 domain of phosphatidylserine decarboxylase 2 is not required for catalysis but is essential for in vivo function
J. Biol. Chem.
277
33720-33726
2002
Saccharomyces cerevisiae
brenda
Wu, W.I.; Voelker, D.R.
Reconstitution of phosphatidylserine transport from chemically defined donor membranes to phosphatidylserine decarboxylase 2 implicates specific lipid domains in the process
J. Biol. Chem.
279
6635-6642
2004
Saccharomyces cerevisiae
brenda
Salvador, G.A.; Lopez, F.M.; Giusto, N.M.
Age-related changes in central nervous system phosphatidylserine decarboxylase activity
J. Neurosci. Res.
70
283-289
2002
Rattus norvegicus
brenda
Baunaure, F.; Eldin, P.; Cathiard, A.M.; Vial, H.
Characterization of a non-mitochondrial type I phosphatidylserine decarboxylase in Plasmodium falciparum
Mol. Microbiol.
51
33-46
2004
Plasmodium falciparum (Q9GPP8), Plasmodium falciparum
brenda
Burgermeister, M.; Birner, R.; Hrastnik, C.; Daum, G.
Phosphatidylserine decarboxylation and CDP-ethanolamine pathway contribute to the supply of phosphatidylethanolamine to mitochondria of the yeast
NATO Asi Ser. Ser. A
322
19-25
2000
Saccharomyces cerevisiae
-
brenda
Rontein, D.; Wu, W.I.; Voelker, D.R.; Hanson, A.D.
Mitochondrial phosphatidylserine decarboxylase from higher plants. Functional complementation in yeast, localization in plants, and overexpression in Arabidopsis
Plant Physiol.
132
1678-1687
2003
Arabidopsis thaliana, Solanum lycopersicum, Solanum tuberosum
brenda
Nishibori, A.; Kusaka, J.; Hara, H.; Umeda, M.; Matsumoto, K.
Phosphatidylethanolamine domains and localization of phospholipid synthases in Bacillus subtilis membranes
J. Bacteriol.
187
2163-2174
2005
Bacillus subtilis
brenda
Brgermeister, M.; Birner-Grunberger, R.; Heyn, M.; Daum, G.
Contribution of different biosynthetic pathways to species selectivity of aminoglycerophospholipids assembled into mitochondrial membranes of the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1686
148-160
2004
Saccharomyces cerevisiae
brenda
Brgermeister, M.; Birner-Grunberger, R.; Nebauer, R.; Daum, G.
Contribution of different pathways to the supply of phosphatidylethanolamine and phosphatidylcholine to mitochondrial membranes of the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1686
161-168
2004
Saccharomyces cerevisiae
brenda
Steenbergen, R.; Nanowski, T.S.; Beigneux, A.; Kulinski, A.; Young, S.G.; Vance, J.E.
Disruption of the phosphatidylserine decarboxylase gene in mice causes embryonic lethality and mitochondrial defects
J. Biol. Chem.
280
40032-40040
2005
Mus musculus
brenda
Bleijerveld, O.B.; Brouwers, J.F.; Vaandrager, A.B.; Helms, J.B.; Houweling, M.
The CDP-ethanolamine pathway and phosphatidylserine decarboxylation generate different phosphatidylethanolamine molecular species
J. Biol. Chem.
282
28362-28372
2007
Cricetulus griseus, Rattus norvegicus
brenda
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
brenda
Nerlich, A.; von Orlow, M.; Rontein, D.; Hanson, A.D.; Doermann, P.
Deficiency in phosphatidylserine decarboxylase activity in the psd1 psd2 psd3 triple mutant of Arabidopsis affects phosphatidylethanolamine accumulation in mitochondria
Plant Physiol.
144
904-914
2007
Arabidopsis thaliana (A4GNA8), Arabidopsis thaliana (F4KAK5), Arabidopsis thaliana (Q84V22)
brenda
Larsson, K.E.; Nystroem, B.; Liljenberg, C.
A phosphatidylserine decarboxylase activity in root cells of oat (Avena sativa) is involved in altering membrane phospholipid composition during drought stress acclimation
Plant Physiol. Biochem.
44
211-219
2006
Avena sativa
brenda
Vences-Guzman, M.A.; Geiger, O.; Sohlenkamp, C.
Sinorhizobium meliloti mutants deficient in phosphatidylserine decarboxylase accumulate phosphatidylserine and are strongly affected during symbiosis with alfalfa
J. Bacteriol.
190
6846-6856
2008
Sinorhizobium meliloti 1021 (Q9FDI9)
brenda
Vance, J.E.
Phosphatidylserine and phosphatidylethanolamine in mammalian cells: two metabolically related aminophospholipids
J. Lipid Res.
49
1377-1387
2008
Saccharomyces cerevisiae, Mus musculus
brenda
Federovitch, C.M.; Jones, Y.Z.; Tong, A.H.; Boone, C.; Prinz, W.A.; Hampton, R.Y.
Genetic and structural analysis of Hmg2p-induced endoplasmic reticulum remodeling in Saccharomyces cerevisiae
Mol. Biol. Cell
19
4506-4520
2008
Saccharomyces cerevisiae
brenda
Gulshan, K.; Schmidt, J.A.; Shahi, P.; Moye-Rowley, W.S.
Evidence for the bifunctional nature of mitochondrial phosphatidylserine decarboxylase: role in Pdr3-dependent retrograde regulation of PDR5 expression
Mol. Cell. Biol.
28
5851-5864
2008
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae
brenda
Schuiki, I.; Schnabl, M.; Czabany, T.; Hrastnik, C.; Daum, G.
Phosphatidylethanolamine synthesized by four different pathways is supplied to the plasma membrane of the yeast Saccharomyces cerevisiae
Biochim. Biophys. Acta
1801
480-486
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae FY1679
brenda
Luo, J.; Matsuo, Y.; Gulis, G.; Hinz, H.; Patton-Vogt, J.; Marcus, S.
Phosphatidylethanolamine is required for normal cell morphology and cytokinesis in the fission yeast Schizosaccharomyces pombe
Eukaryot. Cell
8
790-799
2009
Schizosaccharomyces pombe, Schizosaccharomyces pombe SP870
brenda
Wriessnegger, T.; Sunga, A.J.; Cregg, J.M.; Daum, G.
Identification of phosphatidylserine decarboxylases 1 and 2 from Pichia pastoris
FEMS Yeast Res.
9
911-922
2009
Komagataella pastoris, Komagataella pastoris GS115
brenda
Gulshan, K.; Shahi, P.; Moye-Rowley, W.S.
Compartment-specific synthesis of phosphatidylethanolamine is required for normal heavy metal resistance
Mol. Biol. Cell
21
443-455
2010
Saccharomyces cerevisiae
brenda
Chen, Y.L.; Montedonico, A.E.; Kauffman, S.; Dunlap, J.R.; Menn, F.M.; Reynolds, T.B.
Phosphatidylserine synthase and phosphatidylserine decarboxylase are essential for cell wall integrity and virulence in Candida albicans
Mol. Microbiol.
75
1112-1132
2010
Candida albicans
brenda
Thanawastien, A.; Montor, W.R.; Labaer, J.; Mekalanos, J.J.; Yoon, S.S.
Vibrio cholerae proteome-wide screen for immunostimulatory proteins identifies phosphatidylserine decarboxylase as a novel Toll-like receptor 4 agonist
PLoS Pathog.
5
e1000556
2009
Vibrio cholerae serotype O1
brenda
Hoerl, G.; Wagner, A.; Cole, L.K.; Malli, R.; Reicher, H.; Kotzbeck, P.; Koefeler, H.; Hoefler, G.; Frank, S.; Bogner-Strauss, J.G.; Sattler, W.; Vance, D.E.; Steyrer, E.
Sequential synthesis and methylation of phosphatidylethanolamine promote lipid droplet biosynthesis and stability in tissue culture and in vivo
J. Biol. Chem.
286
17338-17350
2011
Mus musculus
brenda
Muthukumar, K.; Nachiappan, V.
Phosphatidylethanolamine from phosphatidylserine decarboxylase2 is essential for autophagy under cadmium stress in Saccharomyces cerevisiae
Cell Biochem. Biophys.
67
1353-1363
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Choi, J.Y.; Augagneur, Y.; Ben Mamoun, C.; Voelker, D.R.
Identification of gene encoding Plasmodium knowlesi phosphatidylserine decarboxylase by genetic complementation in yeast and characterization of in vitro maturation of encoded enzyme
J. Biol. Chem.
287
222-232
2012
Plasmodium knowlesi
brenda
Gupta, N.; Hartmann, A.; Lucius, R.; Voelker, D.R.
The obligate intracellular parasite Toxoplasma gondii secretes a soluble phosphatidylserine decarboxylase
J. Biol. Chem.
287
22938-22947
2012
Toxoplasma gondii, Toxoplasma gondii TaTi
brenda
Horvath, S.E.; Boettinger, L.; Voegtle, F.N.; Wiedemann, N.; Meisinger, C.; Becker, T.; Daum, G.
Processing and topology of the yeast mitochondrial phosphatidylserine decarboxylase 1
J. Biol. Chem.
287
36744-36755
2012
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
brenda
Chan, E.Y.; McQuibban, G.A.
Phosphatidylserine decarboxylase 1 (Psd1) promotes mitochondrial fusion by regulating the biophysical properties of the mitochondrial membrane and alternative topogenesis of mitochondrial genome maintenance protein 1 (Mgm1)
J. Biol. Chem.
287
40131-40139
2012
Saccharomyces cerevisiae
brenda
Riekhof, W.R.; Wu, W.I.; Jones, J.L.; Nikrad, M.; Chan, M.M.; Loewen, C.J.; Voelker, D.R.
An assembly of proteins and lipid domains regulates transport of phosphatidylserine to phosphatidylserine decarboxylase 2 in Saccharomyces cerevisiae
J. Biol. Chem.
289
5809-5819
2014
Saccharomyces cerevisiae
brenda
Hartmann, A.; Hellmund, M.; Lucius, R.; Voelker, D.R.; Gupta, N.
Phosphatidylethanolamine synthesis in the parasite mitochondrion is required for efficient growth but dispensable for survival of Toxoplasma gondii
J. Biol. Chem.
289
6809-6824
2014
Toxoplasma gondii
brenda
Gsell, M.; Mascher, G.; Schuiki, I.; Ploier, B.; Hrastnik, C.; Daum, G.
Transcriptional response to deletion of the phosphatidylserine decarboxylase Psd1p in the yeast Saccharomyces cerevisiae
PLoS ONE
8
e77380
2013
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
brenda
Soupene, E.; Kuypers, F.A.
Phosphatidylserine decarboxylase CT699, lysophospholipid acyltransferase CT775, and acyl-ACP synthase CT776 provide membrane lipid diversity to Chlamydia trachomatis
Sci. Rep.
7
15767
2017
Chlamydia trachomatis (P0CD79), Chlamydia trachomatis, Chlamydia trachomatis serovar D (P0CD79)
brenda
Khandelwal, N.; Sarkar, P.; Gaur, N.; Chattopadhyay, A.; Prasad, R.
Phosphatidylserine decarboxylase governs plasma membrane fluidity and impacts drug susceptibilities of Candida albicans cells
Biochim. Biophys. Acta
1860
2308-2319
2018
Candida albicans (Q5ABC5), Candida albicans (Q5AK66), Candida albicans, Candida albicans ATCC MYA-2876 (Q5ABC5), Candida albicans ATCC MYA-2876 (Q5AK66)
brenda
Di Bartolomeo, F.; Doan, K.N.; Athenstaedt, K.; Becker, T.; Daum, G.
Involvement of a putative substrate binding site in the biogenesis and assembly of phosphatidylserine decarboxylase 1 from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1862
716-725
2017
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae
brenda
Wagner, A.; Di Bartolomeo, F.; Klein, I.; Hrastnik, C.; Doan, K.N.; Becker, T.; Daum, G.
Identification and characterization of the mitochondrial membrane sorting signals in phosphatidylserine decarboxylase 1 from Saccharomyces cerevisiae
Biochim. Biophys. Acta
1863
117-125
2018
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae
brenda
Choi, J.Y.; Duraisingh, M.T.; Marti, M.; Ben Mamoun, C.; Voelker, D.R.
From protease to decarboxylase the molecular metamorphosis of phosphatidylserine decarboxylase
J. Biol. Chem.
290
10972-10980
2015
Plasmodium knowlesi (B3L2V1), Plasmodium knowlesi, Plasmodium knowlesi H (B3L2V1)
brenda
Onguka, O.; Calzada, E.; Ogunbona, O.B.; Claypool, S.M.
Phosphatidylserine decarboxylase 1 autocatalysis and function does not require a mitochondrial-specific factor
J. Biol. Chem.
290
12744-12752
2015
Saccharomyces cerevisiae (P39006), Saccharomyces cerevisiae
brenda
Choi, J.Y.; Surovtseva, Y.V.; Van Sickle, S.M.; Kumpf, J.; Bunz, U.H.F.; Ben Mamoun, C.; Voelker, D.R.
A novel fluorescence assay for measuring phosphatidylserine decarboxylase catalysis
J. Biol. Chem.
293
1493-1503
2018
Plasmodium knowlesi (B3L2V1), Plasmodium knowlesi H (B3L2V1)
brenda
Ogunbona, O.; Onguka, O.; Calzada, E.; Claypool, S.
Multitiered and cooperative surveillance of mitochondrial phosphatidylserine decarboxylase 1
Mol. Cell. Biol.
37
e00049
2017
Saccharomyces cerevisiae (P39006)
brenda
Farine, L.; Jelk, J.; Choi, J.Y.; Voelker, D.R.; Nunes, J.; Smith, T.K.; Buetikofer, P.
Phosphatidylserine synthase 2 and phosphatidylserine decarboxylase are essential for aminophospholipid synthesis in Trypanosoma brucei
Mol. Microbiol.
104
412-427
2017
Trypanosoma brucei (Q38DZ5), Trypanosoma brucei, Trypanosoma brucei 927/4 GUTat10.1 (Q38DZ5)
brenda
Choi, J.Y.; Kumar, V.; Pachikara, N.; Garg, A.; Lawres, L.; Toh, J.Y.; Voelker, D.R.; Ben Mamoun, C.
Characterization of Plasmodium phosphatidylserine decarboxylase expressed in yeast and application for inhibitor screening
Mol. Microbiol.
99
999-1014
2016
Plasmodium falciparum (Q9GPP8)
brenda
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
brenda