Molecular structure--activity relationship of hydrazides inhibiting glutamic acid decarboxylase, GABA-alpha-oxoglutarate aminotransferase, and monoamine oxidase activities in chick brain.

Abstract

Several aryl and heteroaryl hydrazides were synthesized and evaluated for their inhibitory effects on glutamic acid decarboxylase (GAD), GABA-alpha-oxoglutarate aminotransferase (GABA-T), and monoamine oxidase (MAO) enzyme systems in chick brain 24 h after their intramuscular administration (0.75 mmol/kg). All compounds produced a reduction in GAD, GABA-T, and MAO activity. Structure-activity relationships indicated that the ring structure had a greater influence on the degree of GAD and GABA-T inhibition than did the N'-terminal group. In contrast, structural requirements for MAO inhibition were much more restrictive. The intramuscular administration of benzoic acid hydrazide to chicks 24 h prior to their being exposed to oxygen at high pressure provided significant protection against the onset of the hyperbaric oxygen-induced seizures.

• Authors: J D Wood, D K Gorecki, J R Dimmock, E M Hawes
• Journal: Canadian journal of physiology and pharmacology (Can J Physiol Pharmacol) Vol. 53 Issue 1 Pg. 47-55 (Feb 1975) ISSN: 0008-4212 [Print] Canada
• PMID: 1139448 (Publication Type: Journal Article)

Chemical References

• Anticonvulsants
• Benzoates
• Glutamates
• Hydrazines
• Ketoglutaric Acids
• Monoamine Oxidase Inhibitors
• gamma-Aminobutyric Acid
• Transaminases
• Carboxy-Lyases

Topics

• Animals
• Animals, Newborn
• Anticonvulsants (pharmacology)
• Benzoates
• Brain (drug effects, enzymology)
• Carboxy-Lyases (antagonists & inhibitors)
• Chickens
• Glutamates
• Hydrazines (pharmacology)
• Hyperbaric Oxygenation
• Ketoglutaric Acids
• Monoamine Oxidase Inhibitors (pharmacology)
• Structure-Activity Relationship
• Transaminases (antagonists & inhibitors)
• gamma-Aminobutyric Acid