negative regulation of protein amino acid phosphorylation

Any process that stops, prevents or decreases the rate of addition of phosphoric groups to amino acids within a protein.

Catalysis of the reaction: peptidyl-L-lysine(or L-arginine) + H2O = peptide + L-lysine(or L-arginine). Release of a C-terminal basic amino acid, preferentially lysine; inactivates bradykinin and anaphylatoxins in blood plasma.

positive regulation of protein amino acid phosphorylation

Any process that activates or increases the rate of addition of phosphoric groups to amino acids within a protein.

Catalysis of the hydrolysis of carboxyl terminal peptide linkages in oligopeptides or polypeptides; a serine residue is at the active center.

Interacting selectively with cholesterol (cholest-5-en-3-beta-ol); the principal sterol of vertebrates and the precursor of many steroids, including bile acids and steroid hormones.

Any process that modulates the frequency, rate or extent of hydrolase activity, the catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc. Hydrolase is the systematic name for any enzyme of EC class 3.

Catalysis of the release of a C-terminal amino acid with a broad specificity.

Catalysis of the preferential release of a C-terminal arginine or lysine residue. Function is inhibited by diisopropyl fluorophosphate and sensitive to thiol-blocking reagents.

Any process that modulates the frequency, rate or extent of transferase activity, the catalysis of the transfer of a group, e.g. a methyl group, glycosyl group, acyl group, phosphorus-containing, or other groups, from one compound (generally regarded as the donor) to another compound (generally regarded as the acceptor). Transferase is the systematic name for any enzyme of EC class 2.

negative regulation of macrophage differentiation

Any process that stops, prevents or reduces the rate of macrophage differentiation.

Catalysis of an oxidation-reduction (redox) reaction in which the hydrogen donor and acceptor are the same molecule, and no oxidized product appears.