Tyrosine, biosynthesis catabolism

A variety of other enzymes involved in amino acid catabolism have been detected in both protozoa and helminths. These include deaminases such as histidase, decarboxylases, some of which are involved in biosynthesis of amines and related compounds, and hydroxylases of proline, tryptophan and tyrosine. These additional enzymes have mostly been reported in helminths (1). L-Amino acid oxidases and D-amino acid oxidases are also present and the availability of the latter would allow D-amino acids to be metabolized in the absence of amino acid racemases. 

In the aromatic amino acid biosynthesis, chorismic acid (51) is converted into anthranilic acid, which would be a potential precursor providing both nitrogens for the ring as well as the aromatic system of phenazines. However, anthranilic acid and other proposed intermediates like quinic acid, tryptophan, tyrosine, and phenylalanine have been questioned on the basis of studies of mutants of phenazine producing organisms with blocked catabolism of these various possible intermediates. 

Tyrosine is either used for the biosynthesis of proteins, thyroxine, epinephrine, or melanin, or catabo-lized to yield fumaryl acetoacetate. The biosynthesis of proteins and thyroxine is discussed elsewhere this discussion is restricted to epinephrine and melanin synthesis and tyrosine catabolism. Dopa 3,4-dihydroxy-phenylalanine is an intermediate common to epinephrine and melanin. To yield epinephrine, dopa is first decarboxylated by an enzyme called dopa decarboxylase. This enzyme is present in several mammalian tissues, including the adrenal medulla, where the reaction yields hydroxytryptamine chloride. From this... 

For the biosynthesis of cell components a microorganism must be supplied with appropriate low molecular weight compounds such as sugars, organic acids, amino acids etc. Many of 2-, 3-, 4- and 5-carbon compounds are formed in catabolic reactions. In propionic acid bacteria these reactions comprise the propionic acid fermentation, TCA cycle and hexose monophosphate shunt. The latter supplies the cell with erythrose-phosphate, ribose-5-phosphate and reducing equivalents (NADPH) needed for many syntheses. Erythrose-4-phosphate is used in the formation of aromatic amino acids phenylalanine, tryptophane, tyrosine. Ribose-5-phosphate is incorporated into nucleic acids. The pentose cycle and propionic acid fermentation, as mentioned before, have a number of common precursors and enzymes. The inclusion of common precursors into one or another pathway is regulated by the level of ATP (Labory, 1970), and this regulation in fact determines the ratio of catabolic and anabolic processes in the cell. 

It is clearly not possible to discuss here at any length, the metabolism of individual amino acids. In addition, the details of the biosynthesis and catabolism of amino acids, well reviewed in Volume II of Meister s recent book , are concerned more with the formation and breakdown of the carbon skeleton than with the introduction or loss of the amino group. Modifications of some of the twenty amino cicids normally found in proteins have been detected in some protein hydrolysates, e.g. iodinated tyrosine, phosphoserine and hydroxylysine. In some cases the modification appears to be made before the amino acid is incorporated into protein (e.g. iodination of tyrosine) while in other cases modification is believed to occur when the amino acid is already present in proteins (e.g. hydroxylation of lysine, and in some cases, of... 

Fig. 1.1. Biosynthesis and regeneration of tetrahydrobiopterin including possible metabolic defects and catabolism of phenylalanine. l.l=phenylalanine-4-hydroxylase (PAH) 1.2/1.6 = GTP cyclohydrolase I (GTPCH), 1.3 = 6-pyruvoyl-tetra-hydropterin synthase (PTPS), 1.4 = dihydropteridine reductase (DHPR), 1.5 = pterin-4a-carbinolamine dehydratase (PCD), 1.7 = sepiapterin reductase SR, carbonyl reductase (CR), aldose reductase (AR), dihydrofolate reductase (DHFR), aromatic amino acid decarboxylase (AADC), tyrosine hydroxylase (TH), tryptophan hydroxylase (TPH), nitric oxide synthase (NOS). Pathological metabolites used as specific markers in the differential diagnosis are marked in squares. n.e.=non-enzymatic...

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