Probable mechanism of catalysis of pineal gland hydroxyindole-O-methyltransferase (HIOMT) from rainbow trout (Salmo gairdneri)

• DOI: 10.1007/bf01250644
• Publication Date: 2005-03-23T15:06:25Z
• Authors: D. J. Morton; H. J. Forbes
• Keywords: Acetylserotonin O-Methyltransferase; Male; 0303 health sciences; Indoles; Trout; Methyltransferases; Hydrogen-Ion Concentration; In Vitro Techniques; Methylation; Pineal Gland; Kinetics; 03 medical and health sciences; Animals; Salmonidae

Activity of trout pineal HIOMT was found to increase with increase in incubation temperature from 5 to 40 degrees C although the activation energy remained constant over this range. From examination of the effects of the products of HIOMT catalysis on the enzyme it was apparent that the catalytic mechanism was ordered Bi-Bi with S-adenosylmethionine as the obligatory first substrate. Trout HIOMT was found to methylate all the common pineal hydroxyindoles with hydroxytryptophol having the greatest affinity for the enzyme. The pH optimum for trout HIOMT was found to be about pH 9.0 although routine use of a pH of 7.9 is recommended to limit potentially deliterious effects caused by degradation of S-adenosylmethionine at elevated pHs.