Caspase-3/Sandbox: Difference between revisions
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====Posttranslational Modifications==== | ====Posttranslational Modifications==== | ||
Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa. | Cleavage by granzyme B, caspase-6, caspase-8 and caspase-10 generates the two active subunits. Additional processing of the propeptides is likely due to the autocatalytic activity of the activated protease. Active heterodimers between the small subunit of caspase-7 protease and the large subunit of caspase-3 also occur and vice versa. | ||
Acetylation: Protein which is posttranslationally modified by the attachment of at least one acetyl group; generally at the N-terminus. | Acetylation: Protein which is posttranslationally modified by the attachment of at least one acetyl group; generally at the N-terminus. Residue 1 modified by N-acetylmethionine (ref 12) | ||
Phosphoprotein: Protein which is posttranslationally modified by the attachment of either a single phosphate group, or of a complex molecule, such as 5'-phospho-DNA, through a phosphate group. Target amino acid is usually serine, threonine or tyrosine residues (mostly in eukaryotes), aspartic acid or histidine residues (mostly in prokaryotes). | |||
S-nitrosylation: Protein which is posttranslationally modified by the attachment of a nitric oxide group on the sulfur atom of one or more cysteine residues. | Phosphoprotein: Protein which is posttranslationally modified by the attachment of either a single phosphate group, or of a complex molecule, such as 5'-phospho-DNA, through a phosphate group. Target amino acid is usually serine, threonine or tyrosine residues (mostly in eukaryotes), aspartic acid or histidine residues (mostly in prokaryotes). Residue 26 perhaps modified by Phosphoserine. | ||
S-nitrosylation: Protein which is posttranslationally modified by the attachment of a nitric oxide group on the sulfur atom of one or more cysteine residues. Residue 163 modified by S-nitrosocysteine in inhibited form. | |||
Zymogen: The enzymatically inactive precursor of mostly proteolytic enzymes. | Zymogen: The enzymatically inactive precursor of mostly proteolytic enzymes. | ||
