1.5.1.25	3,3',5'-L-triiodothyronine	competitive inhibition	220662	
1.5.1.25	3,3',5'-L-triiodothyronine	-	220662	
1.5.1.25	3,5,3'-L-triiodothyronine	competitive inhibition	220663	
1.5.1.25	3,5,3'-L-triiodothyronine	-	220663	
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	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	-	101783	
1.5.1.25	3,5-diiodo-L-tyrosine	low competitive inhibition	3597	
1.5.1.25	3,5-diiodo-L-tyrosine	-	3597	
1.5.1.25	3,5-diiodothyronine	competitive inhibition	21471	
1.5.1.25	3,5-L-diiodothyronine	-	262440	
1.5.1.25	4,5-dibromopyrrole-2-carboxylate	-	220660	
1.5.1.25	DELTA1-piperideine 2-carboxylate	substrate inhibition	49519	
1.5.1.25	L-thyroxine	competitive inhibition	1380	
1.5.1.25	L-thyroxine	-	1380	
1.5.1.25	L-tyrosine	competitive inhibition	109	
1.5.1.25	L-tyrosine	-	109	
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	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	
1.5.1.25	additional information	the P2C reductase activity is potently inhibited by thyroid hormones	2	
1.5.1.25	picolinate	-	15921	
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	-	4860	
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	S-(2-aminoethyl)-L-cysteine ketimine	substrate inhibition	220661	
1.5.1.25	Triton X-100	irreversible inactivation	61