Metabolic Pathways. Second Edition of Chemical Pathways of by David M. Greenberg

By David M. Greenberg

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4. Substitution in the benzene ring of phenylethylamine results in slight to marked changes in deamination rate by monoamine oxidase, depending on the nature and position of the substituent group. 5. 5-Hydroxytryptamine (serotonin) is an excellent substrate for mono­ amine oxidase. 6. Diamines of the type NH2(CH2)nNH2 are not oxidized, except those of fourteen-, sixteen-, and eighteen-carbon chain length. It has recently 26 p . p . COHEN AND H. J. 6) (15) 30 . MichaeUs constents {Km), Μ X ΙΟ"·.

Reaction (31), asparagine-a-keto acid trans­ aminase, has been demonstrated to occur in liver and kidney (355), This transamination reaction is reversible. A large number of amino acids and glutamine are active in forming asparagine from a-ketosuccinamic acid (see Table VIII). Asparagine acts with a large number of a-keto acids to form a-ketosuccinamic acid. The deamidation of the latter is catalyzed by the same ω-amidase which deamidates a-ketoglutaramic acid. 1 0 0 0 0 13. 22 the affinity of a-ketosuccinamic acid for the deamidase is ΙοΛν which ac­ counts for the reversibiUty of the transaminase system (260).

Ammonia {190), aliphatic monoamines {191), ephed­ rine {192), and choline {191) are weak inhibitors, whereas guanidines {193), imidazole {194), basic dyes such as pyocyanine {195), methylene blue {196), and toluylene blue {195), diamines such as thiamine {197), pyridoxamine {197), piperazine {197), and diamidines {198) (such as 4,4'diamidinostilbene and its dimethyl derivative) are potent competitive 32 p. p. COHEN AND H. J. SALLACH inhibitors. Streptomycin and dihydrostreptomycin and diguanidine derivates have been reported to be powerful inhibitors of bacterial diamine oxidase {199).

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