The dehydration of peptidyl-serine, followed by hydrogenation to produce peptidyl-D-alanine.

The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N'(omega)-dimethyl-L-arginine.

The process of methylation of peptidyl-arginine to form peptidyl-N(omega),N(omega)-dimethyl-L-arginine.

A mitochondrial complex of a regulatory and catalytic subunit that catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex. An example of this component is found in Mus musculus.

The action of a molecule that contributes to the structural integrity of the myelin sheath of a nerve.

Catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein; increases the activity of a cyclin-dependent protein kinase (CDK).

Modulation of the activity of the enzyme cyclin-dependent protein kinase activating kinase.

The racemization of peptidyl-alanine.

The cross-linking of a cysteine residue to an aspartic acid residue to form 3-(S-L-cysteinyl)-L-aspartic acid.

The cross-linking of a cysteine residue to a glutamic acid residue to form 4-(S-L-cysteinyl)-L-glutamic acid.

The chemical reactions and pathways resulting in the formation of internal peptidyl-1-thioglycine, which has an internal C=S bond, instead of an internal C=O bond, in the peptide.

The chemical reactions and pathways resulting in the formation of peptidyl-1-thioglycine from other compounds, including peptidyl-glycine.

The chemical reactions and pathways resulting in the formation of carboxy-terminal peptidyl-1-thioglycine, which has a carboxy-terminal thiocarboxy-C(=O)-SH bond.

OBSOLETE. The covalent linking of a chromophore to a protein via peptidyl-cysteines.

OBSOLETE. The covalent linking of the alpha-1-microglobulin chromophore to the protein; the structure of the chromophore is not known. It is probably heterogeneous and involving two cysteines in thioether bonds.

The oxidation of peptidyl-tryptophan to form tryptophan-6,7-dione, otherwise known as tryptophyl quinone, which is further modified by cross-linking to either tryptophan or cysteine.

The cross-linking of a cysteine residue to tryptophyl quinone to form 4'-(S-L-cysteinyl)-L-tryptophyl quinone, a cofactor found at the active site of amine dehydrogenase.