Decarboxylases methionine decarboxylase

KYNURENINE AMINOTRANSFERASE LEUCINE AMINOTRANSFERASE LYSINE 2,3-AMINOMUTASE LYSINE 6-AMINOTRANSFERASE LYSINE DECARBOXYLASE METHIONINE y-LYASE ORNITHINE AMINOTRANSFERASE PHENYLALANINE DECARBOXYLASE PHOSPHATIDYLSERINE DECARBOXYLASE... 

Two-dimensional structures of 2 -deoxy-2 -(3-methoxybenzamido) adenosine (MMBA), a selective T.brucei GAPDH inhibitor and MDL 73811, an irreversible inhibitor of trypanosomal S-adenosyl methionine decarboxylase. 

Lysine is formed in bacteria by decarboxylation of meso-diamino-pimelic acid (Fig. 24-14). Glycine is decarboxylated oxidatively in mitochondria in a sequence requiring lipoic acid and tetrahydrofolate as well as PLP (Fig. 15-20). A methionine decarboxylase has been isolated in pure form from a fem. ° The bacterial dialkylglycine decarboxylase is both a decarboxylase and an aminotransferase which uses pyruvate as its second substrate forming a ketone and L-alanine as products (See Eq. 

Wrenger, C., Luersen, K., Krause, T., Muller, S., and Walter, R. D. (2001). The Plasmodium falciparum bifunctional ornithine decarboxylase, S-adenosyl-L-methionine decarboxylase, enables a well balanced polyamine synthesis without domain-domain interaction. ]. Biol. Chem. 276,29651-29656. 

Using a similar experimental strategy, the pyruvyl-dependent S-adenosyl-methionine decarboxylase Escherichia coli) was also demonstrated to involve retention of configuration at the a-carbon of the methionyl moiety (269). The... 

Tekwani, B. L., Bacchi, C. J. and Pegg, A. E. (1992) Putrescine activated S-adenosyl-methionine decarboxylase from Trypanosoma brucei brucei. Mol. Cell. Biochem. 117 53-61. 

The aromatic diamidines are compounds of considerable pharmaceutical interest. This is, among others, for the following reasons they have a strong antiprotozoan action and participate in the metabolism and transport of polyamines, inhibiting, for instance, 5-adenosyl-L-methionine decarboxylase (SAMDC). Therefore, because this route is closely linked to cell proliferation processes, aromatic diamidines can slow down or prevent the growth of tumors. The substances used in this work are as follows " ... 

Fig. 194. Formation of spermidine and spermine 1 S-Adenosyl-L-methionine decarboxylase 2 aminopropyltransferase...

Gomez-Jimenez M, Paredes M, Geillardo M, Femandez-Garda N, Ohnos E, Sanchez-CaUe I (2010) Tissue-specific expression of olive S-adenosyl methionine decarboxylase and spermidine synthase genes and polyamine metabolism during flower opening and eady fruit development. Planta (Bed) 232 629-647... 

In the case of hyperphenylalaninaemia, which occurs ia phenylketonuria because of a congenital absence of phenylalanine hydroxylase, the observed phenylalanine inhibition of proteia synthesis may result from competition between T.-phenylalanine and L-methionine for methionyl-/RNA. Patients sufferiag from maple symp urine disease, an inborn lack of branched chain oxo acid decarboxylase, are mentally retarded unless the condition is treated early enough. It is possible that the high level of branched-chain amino acids inhibits uptake of L-tryptophan and L-tyrosiae iato the brain. Brain iajury of mice within ten days after thek bkth was reported as a result of hypodermic kijections of monosodium glutamate (MSG) (0.5—4 g/kg). However, the FDA concluded that MSG is a safe kigredient, because mice are bom with underdeveloped brains regardless of MSG kijections (106). 

Pyridoxamine phosphate serves as a coenzyme of transaminases, e.g., lysyl oxidase (collagen biosynthesis), serine hydroxymethyl transferase (Cl-metabolism), S-aminolevulinate synthase (porphyrin biosynthesis), glycogen phosphoiylase (mobilization of glycogen), aspartate aminotransferase (transamination), alanine aminotransferase (transamination), kynureninase (biosynthesis of niacin), glutamate decarboxylase (biosynthesis of GABA), tyrosine decarboxylase (biosynthesis of tyramine), serine dehydratase ((3-elimination), cystathionine 3-synthase (metabolism of methionine), and cystathionine y-lyase (y-elimination). 

SNA does not affect the concentrations of histamine and glutamic add, but It decreases the activity of glutamic acid decarboxylase and reduces the concentrations of gamma-aminobutyric acid (GABA) In rat brain. 5 GABA release Is Inhibited by acute administration, but not by chronic treatment. 5 SNA Increases serum creatinine phosphoklnase content In stressed rats. Recently, SNA was found to decrease methionine-enkephalin content In the medulla oblongata and mldbraln In the mouse, whereas other areas remained unaffected.48... 

Polyamines such as spermine and spermidine, involved in DNA packaging, are derived from methionine and ornithine by the pathway shown in Figure 22-30. The first step is decarboxylation of ornithine, a precursor of arginine (Fig. 22-10). Ornithine decarboxylase, a PLP-requiring enzyme, is the target of several powerful inhibitors used as pharmaceutical agents (Box 22-2). ... 

Taurine is a dietary essential in the cat, which is an obligate carnivore with a limited capacity for taurine synthesis from cysteine. On a taurine-free diet, neither supplementary methionine nor cysteine will maintain normal plasma concentrations of taurine, because cats have an alternative pathway of cysteine metabolism reaction with mevalonic acid to yield felinine (3-hydroxy-1,1-dimethylpropyl-cysteine), which is excreted in the urine. The activity of cysteine sulfinic acid decarboxylase in cat liver is very low. 

It is not known to what extent taurine may be a dietary essential for human beings. There is little cysteine sulfinic acid decarboxylase activity in the human liver and, like the cat, loading doses of methionine and cysteine do not result in any significant increase in plasma taurine. This may be because cysteine sulfinic acid can also undergo transamination to /3-sulfhydryl pyruvate, which then loses sulfur dioxide nonenzymically to form pyruvate, thus regulating the amount of taurine that is formed from cysteine. There is no evidence of the development of any taurine deficiency disease under normal conditions. 

Polyamine biosynthesis is associated with regulation of a number of metabolic functions including growth of cells in most of the living organisms. In mammals, ornithine is the precursor of aliphatic polyamines. Putrescine, formed by decarboxylation of the former by ornithine decarboxylase, is the first amine formed in polyamine biosynthesis. Putrescine gives rise to the other two polyamines, spermine and spermidine by successive addition of 3-aminopropyl residues derived from S-adenosyl-L-methionine (SAM) in the presence of different enzymes [44] (Chart 7). 

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