Enables the directed movement of thiamin into, out of, within or between cells. Thiamin is vitamin B1, a water soluble vitamin present in fresh vegetables and meats, especially liver.

Combining with acetylated low-density lipoproteins, advanced glycation end products, or other polyanionic ligands to initiate a change in cell activity.

Catalysis of the reaction: L-proline + NADP+ = 1-pyrroline-5-carboxylate + NADPH + H+.

Enables the directed movement of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom, into, out of or within a cell.

Catalysis of the reaction: ATP + pyruvate + HCO3- = ADP + phosphate + oxaloacetate.

Interacting selectively with a KDEL sequence, the C terminus tetrapeptide sequence Lys-Asp-Glu-Leu found in proteins that are to be retained in the endoplasmic reticulum.

Interacting selectively with the signal recognition particle.

Interacting selectively with the enzyme nitric-oxide synthase.

The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA.

Catalysis of the oxidative decarboxylation of pyruvate.

Enables the directed movement of a drug into, out of, within or between cells. A drug is any naturally occurring or synthetic substance, other than a nutrient, that, when administered or applied to an organism, affects the structure or functioning of the organism; in particular, any such substance used in the diagnosis, prevention, or treatment of disease.

Interacting selectively with a signal sequence, a specific peptide sequence found on protein precursors or mature proteins that dictates where the mature protein is localized.

regulation of nitric-oxide synthase activity

Any process that modulates the activity of the enzyme nitric-oxide synthase.

The process of coupling asparagine to asparaginyl-tRNA, catalyzed by asparaginyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA.