EC Number   |
Posttranslational Modification |
Reference |
|---|
    4.1.1.65 | acylation |
the pyruvoyl moiety is detected at the N-termini of alpha-subunits |
-, 748184 |
| 4.1.1.65 | 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 |
748188 |
| 4.1.1.65 | proteolytic modification |
amino acids between positions 40 and 70 are critical for proenzyme processing and decarboxylase activity |
748688 |
| 4.1.1.65 | proteolytic modification |
autocatalytic processing, precursor acts as self-processing serine protease |
748652 |
| 4.1.1.65 | proteolytic modification |
presence of a putative proteolytic PSD cleavage recognition motif, WGSS, amino acids 316-319 |
-, 748671 |
| 4.1.1.65 | 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 |
-, 748184 |
| 4.1.1.65 | 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 |
4783 |
| 4.1.1.65 | 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 |
4785 |
