1.5.1.25 3,3',5'-L-triiodothyronine - 220662 1.5.1.25 3,5,3'-L-triiodothyronine - 220663 1.5.1.25 3,5,3'-triiodothyronine - 101783 1.5.1.25 3,5-diiodo-L-tyrosine - 3597 1.5.1.25 3,5-L-diiodothyronine - 262440 1.5.1.25 4,5-dibromopyrrole-2-carboxylate - 220660 1.5.1.25 L-thyroxine - 1380 1.5.1.25 L-tyrosine - 109 1.5.1.25 picolinate - 15921 1.5.1.25 pyrrole-2-carboxylate - 4860 1.5.1.25 3,3',5'-L-triiodothyronine competitive inhibition 220662 1.5.1.25 3,5,3'-L-triiodothyronine competitive inhibition 220663 1.5.1.25 3,5-diiodothyronine competitive inhibition 21471 1.5.1.25 L-thyroxine competitive inhibition 1380 1.5.1.25 L-tyrosine competitive inhibition 109 1.5.1.25 picolinate competitive inhibition, picolinate is a much poorer inhibitor than pyrrole-2-carboxylate because it does not possess a ring -NH and relies on a relatively weak ring interaction 15921 1.5.1.25 pyrrole-2-carboxylate competitive inhibition, pyrrole-2-carboxylate is an effective inhibitor of ketimine reductase/CRYM mainly as a result of the -NH hydrogen bonding to an active site residue 4860 1.5.1.25 additional information in silico docking of substrates and inhibitors using ketimine reductase/CRYM cyrstal structure, PDB ID 4BVA, overview 2 1.5.1.25 Triton X-100 irreversible inactivation 61 1.5.1.25 3,5-diiodo-L-tyrosine low competitive inhibition 3597 1.5.1.25 DELTA1-piperideine 2-carboxylate substrate inhibition 49519 1.5.1.25 S-(2-aminoethyl)-L-cysteine ketimine substrate inhibition 220661 1.5.1.25 3,5,3'-triiodothyronine the enzyme shows strong binding to 3,5,3'-triiodothyronine (T3), the active form of thyroxine 101783 1.5.1.25 3,5,3'-triiodothyronine the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3 101783 1.5.1.25 3,5,3'-triiodothyronine the ketimine reductase activity of CRYM is strongly inhibited by the thyroid hormone T3, especially at neutral pH, reversible inhibition 101783 1.5.1.25 additional information the P2C reductase activity is potently inhibited by thyroid hormones 2 1.5.1.25 additional information the P2C reductase activity is potently inhibited by thyroid hormones, thyroid hormones and analogues docked into the active site of the crystal structure of human KR, overview 2