4.1.1.65: phosphatidylserine decarboxylase
This is an abbreviated version!
For detailed information about phosphatidylserine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.65
-
4.1.1.65
-
phospholipid
-
phosphatidylcholine
-
kennedy
-
cdp-ethanolamine
-
decarboxylases
-
3hserine
-
ptdetn
-
cdp-diacylglycerol
-
phosphatidylglycerophosphate
-
dowhan
-
spinothalamic
-
base-exchange
-
aminophospholipids
-
interorganelle
-
cdp-diglyceride
-
medicine
-
analysis
- 4.1.1.65
- phospholipid
- phosphatidylcholine
-
kennedy
- cdp-ethanolamine
- decarboxylases
-
3hserine
-
ptdetn
- cdp-diacylglycerol
- phosphatidylglycerophosphate
-
dowhan
-
spinothalamic
-
base-exchange
-
aminophospholipids
-
interorganelle
- cdp-diglyceride
- medicine
- analysis
Reaction
Synonyms
CT699, Decarboxylase, phosphatidylserine, phosphatidyl serine decarboxylase, Phosphatidylserine decarboxylase, phosphatidylserine decarboxylase 1, phosphatidylserine decarboxylase 2, phosphatidylserine decarboxylase2, PISD, PKH_072580, PS decarboxylase, PSD, PSD1, Psd1 enzyme, Psd1p, PSD2, Psd2p, PSD3, PSDC, Tb927.9.10080, type I PtdSer decarboxylase
ECTree
4.1.1.65 phosphatidylserine decarboxylaseAdvanced search results
results (
results (Posttranslational Modification
Posttranslational Modification on EC 4.1.1.65 - phosphatidylserine decarboxylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
POSTTRANSLATIONAL MODIFICATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acylation
proteolytic modification
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
acylation
the pyruvoyl moiety is detected at the N-termini of alpha-subunits
acylation
-
the pyruvoyl moiety is detected at the N-termini of alpha-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
proteolytic modification
amino acids between positions 40 and 70 are critical for proenzyme processing and decarboxylase activity
proteolytic modification
the post-translational processing is inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride. Residues Asp139, His198, and Ser308 are all essential for endoproteolytic processing of PSD, which occurs in cis. Within the GS(S/T) motif found in all PSDs, the Gly307 residue is also essential, but the Ser/Thr309 is nonessential
proteolytic modification
-
the post-translational processing is inhibited by the serine protease inhibitor, phenylmethylsulfonyl fluoride. Residues Asp139, His198, and Ser308 are all essential for endoproteolytic processing of PSD, which occurs in cis. Within the GS(S/T) motif found in all PSDs, the Gly307 residue is also essential, but the Ser/Thr309 is nonessential
-
proteolytic modification
a conserved LGST motif separates the enzyme into alpha- and beta-subunits. Only the serine residue of the motif is absolutely required for Psd1 autocatalysis and function. Yeast Psd1 does not require its substrate phosphatidylserine for autocatalysis. Yeast Psd1 autocatalysis does not require mitochondrion-specific phospholipids, proteins, or cofactors
proteolytic modification
autocatalytic processing, precursor acts as self-processing serine protease
proteolytic modification
presence of a putative proteolytic PSD cleavage recognition motif, WGSS, amino acids 316-319
proteolytic modification
Trypanosoma brucei 927/4 GUTat10.1
-
presence of a putative proteolytic PSD cleavage recognition motif, WGSS, amino acids 316-319
-
