Endogenous Ammonia Production

Compared with the surprising variety of biochemical compounds that can be readily synthesized in Miller-type one-pot simulation experiments, the suite of organics produced under the conditions proposed by Wachtershauser is quite limited. However, the impressive demonstration that the FeS/H2S combination can reduce nitrogen to ammonia shows that considerable attention should be given to the reducing power of pyrite formation. Primordial life may have not been autotrophic, but should we hesitate to accept the idea that the primitive soup was formed from both extraterrestrial sources and endogenous synthesis in which pyrite production played a role After all, a spicy, thick bouillon is always tastier than a bland, diluted broth. 

Monoamine oxidases catalyze oxidative deamination of many primary, secondary, and tertiary amines. They have a wide tissue distribution including brain, liver, and intestine. A variety of endogenous amines, such as catecholamines, and pharmacological substances are metabolized. The products of primary amines are the corresponding aldehydes, ammonia, and hydrogen peroxide. 

Endogenous ammonia is converted to a nonresponsive product creatinine does not react with glutamate dehydrogenase (GlDH) and is converted to ammonia when it reaches the immobilized creatinine deiminase. 

The transamination of the a-amino group to a keto acid acceptor (reaction 2) has been demonstrated in a number of higher plant studies (Nahler and Ruis, 1973 Streeter, 1977 Lloyd and Joy, 1978). The product of the transamination is 2-oxosuccinamate. This can be deamidated to oxaloacetate by lettuce and spinach leaf preparations (Meister, 1953). A similar reaction was reported by Streeter (1977) in soybean and pea leaf extracts. On the other hand, Joy (1978) reported that the 2-oxosuccinamate is reduced to 2-hydroxysuccinamate in these leaves in vivo. The apparent discrepancy between the results of Streeter (1977) and those of Joy (1978) may be due to the enzyme assay used by the former. It consisted of the oxidation of NADH in the presence of the enzyme extract and 2-oxosuccinamate. The assumption was that deamidation occurred leading to oxaloacetate which then acted as the substrate of endogenous malate dehydrogenase. The work of Davies (1961) showed that plant malate dehydrogenase is not specific for oxaloacetate, and it is possible that the 2-oxosuccinamate may act as a substrate. Meister (1953). actually measured the production of ammonia from 2-oxosuccinamate by his leaf preparations. 

Urea is synthesized from the ammonia derived from protein, polypeptide, and amino acid catabolism. Consequently, the amount of urea in the blood is partly determined by protein and amino acid metabolism. Therefore, in considering urea production, the source of the ammonia and the biosynthesis of urea must be discussed. The ammonia is derived mainly from amino acid breakdown. In liver, the amino acid pool is derived from the breakdown products of ingested and endogenous proteins and from amino acids synthesized de novo. 

Endogenous acid production (H" ), and thus control of acid-base balance, is regulated by the kidney through three mechanisms, i.e., the production of NH4 ions and reabsorption of filtered bicarbonate in the proximal tubule and the buffering of hydrogen ion secretion by ammonia in the collecting tubule. 

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