By Alton Meister (Auth.)
Biochemistry of the amino acids
summary: Biochemistry of the amino acids
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Additional info for Biochemistry of the Amino Acids
When glutamine plus glutamate or asparagine plus aspartate were added, there was no appreciable increase in inosinic acid formation above that obtained with the amides separately. On the other hand, addition of glutamine plus aspartate and, to a slightly lesser extent, asparagine plus glutamate, produced considerable increases in inosinic acid formation. The evidence therefore suggested that there is a requirement for a 4-carbon and a 5-carbon atom dicarboxylic acid derivative, one of which must possess an ω-amide group.
Fowden and associates (286, 287) observed transamination of y-aminobutyric acid in extracts of mitochondria from cotyledons of peanut seedlings; pyruvate was more active than α-ketoglutarate (see p. 64). Evidence was obtained for the conversion of y-aminobutyrate to succinate. The metabolism of yaminobutyrate by Saccharomyces cerevisiae and Torulopsis utilis was also investigated; transamination to succinic semialdehyde, and enzymatic reduction of the latter compound to y-hydroxybutyric acid by a dehydrogenase that required reduced triphosphopyridine nucleotide was reported.
It is of interest that a number of the enzymes that catalyze amide nitrogen transfer from glutamine also utilize ammonia; the K m values for un-ionized ammonia and glutamine are of the same order of magnitude. These observations and studies on the effect of pH indicate that the un-ionized form of ammonia is probably the reactive species rather than ammonium ion. Glutamine, which may be considered as an acyl derivative of ammonia, possesses an unprotonated nitrogen atom, which would be available for transfer reactions in which the un-ionized form of ammonia may also participate.
Biochemistry of the Amino Acids by Alton Meister (Auth.)