Arginine decarboxylase

AMINOLEVULINATE DEHYDRATASE 5-AMINOLEVULINATE SYNTHASE ARGININE DECARBOXYLASE ARGININE RACEMASE... 

Pyruvoyl cofactor is derived from the posttranslational modification of an internal amino acid residue, and it does not equilibrate with exogenous pyruvate. Enzymes that possess this cofactor play an important role in the metabolism of biologically important amines from bacterial and eukaryotic sources. These enzymes include aspartate decarboxylase, arginine decarboxylase," phosphatidylserine decarboxylase, . S-adenosylmethionine decarboxylase, histidine decarboxylase, glycine reductase, and proline reductase. ... 

Low, K.B., and Canellakis, E.S. (1987) Biosynthesis of polyamines in ornithine decarboxylase, arginine decarboxylase, and agmatine ureohydrolase deletion mutants of Escherichia coli strain K-12. Proc. Natl Acad. Sci. USA., 84 (13), 4423 -4427. 

Species of Pseudomonas can utilize the a,(i)-diamines putrescine, spermidine, and spermine as sources of carbon and nitrogen, and putrescine can be produced from the secondary amine spermidine together with 1,3-diaminopropane (Dasu et al. 2006). Putrescine (1,4-diaminobutane) is an intermediate in the arginine decarboxylase (ADC) pathway of L-arginine degradation, which is described later, and can be degraded, by two pathways ... 

Graham DE, H Xu, RH White (2002) Methanococcus jannaschii uses a pyruvoyl-dependent arginine decarboxylase in polyamine biosynthesis. J Biol Chem 211 23500-23507. 

Dependence of tyrosine, lysine, arginine and ornithine decarboxylase on a phosphorylated pyridoxal derivative shown. 6, 8... 

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). ... 

Figure 2.5 Logarithmic scale comparison of k,d and kuncat (= (rnon) for some representative reactions at 25 °C. The length of each vertical bar represents the rate enhancement. (Wolfenden, 2001). ADC arginine decarboxylase ODC orotidine 5 -phosphate decarboxylase STN staphylococcal nuclease GLU sweet potato /3-amylase FUM fumarase MAN mandelate racemase PEP carboxypeptodase B CDA E. coli cytidine deaminase KSI ketosteroid isomerase CMU chorismate mutase CAN carbonic anhydrase.

Further modifications using the same strain of ODC S. cerevisiae reconstituted a bacterial/plant polyamine synthesis pathway in yeast [41], The ODC strain was transformed with plasmids encoding arginine decarboxylase and ag-matine ureohydrolase, which conferred polyamine-independent growth on the recombinant microbe. A similar construction could be used to screen for inhibitors of the homologous enzymes from Apicomplexan protozoa, which synthesize poly amines through this pathway [42]. 

The precise role of polyamines in the control of dormancy and the onset of cell division in Jerusalem artichoke tubers, and for that matter in plant development per se, remains in question. Evidence from arginine decarboxylase mutants of Arabidopsis does indicate a possible role in root meristem function (Watson et al., 1998). 

Watson, M.B., Emory, K.K., Piatak, R.M., and Malmberg, R.L., Arginine decarboxylase (polyamine synthesis) mutants of Arabidopsis thaliana exhibit altered root growth, Plant J., 13, 231-239, 1998. 

Bagni, N., Torrigiani, P., and Barbieri, R, In vitro and in vivo effect of ornithine and arginine decarboxylase inhibitors in plant tissue culture, Adv. Polyamine Res., 4, 409-417, 1983. 

Arginine decarboxylase (ADC) catalyzed decarboxylation of arginine is the initial step in an alternative pathway to putrescine in bacteria and higher plants. a-Difluoro-methylarginine (DFMA) (110)17 is an effective mechanism-based inhibitor of ADC and has been used to study compensatory processes involving ADC and ODC175. 

The V-methyl -A1 -pyrrol ini um cation is the last common intermediate in both TA and nicotine biosynthesis (Fig.7.4). V-Methy 1-A1 -pyrrolinium cation formation begins with the decarboxylation of ornithine and arginine by ornithine decarboxylase (ODC) and arginine decarboxylase (ADC), respectively. Putrescine is formed... 

BELL, E., MALMBERG, R.L., Analysis of a cDNA encoding arginine decarboxylase from oat reveals similarity to the Escherichia coli arginine decarboxylase and evidence for protein processing. Mol. Gen. Genet., 1990, 224, 431-436. 

RASTOGI, R., DULSON, J., ROTHSTEIN, S.J., Cloning of tomato (Lycopersicon esculentum Mill.) arginine decarboxylase gene and its expression during fruit ripening. Plant Physiol., 1994,103, 829-834. 

Alanine and aspartic acid are produced commercially utilizing enzymes. In the case of alanine, the process of decarboxylation of aspartic acid by the aspartate decarboxylase from Pseudomonas dacunhae is commercialized. The annual world production of alanine is about 200 tons. Aspartic acid is produced commercially by condensing fumarate and ammonia using aspartase from Escherichia coli. This process has been made more convenient with an enzyme immobilization technique. Aspartic acid is used primarily as a raw material with phenylalanine to produce aspartame, a noncaloric sweetener. Production and sales of aspartame have increased rapidly since its introduction in 1981. Tyrosine, valine, leucine, isoleucine, serine, threonine, arginine, glutamine, proline, histidine, cit-rulline, L-dopa, homoserine, ornithine, cysteine, tryptophan, and phenylalanine also can be produced by enzymatic methods. 

The assay described for amino acid decarboxylase can be used to quantitate the substrates and products associated with the decarboxylation of arginine, aspartate, 2,6-diaminopimelate, histidine, glutamate, lysine, and ornithine. 

L-Lysine and L-arginine are determined in a rapid fashion by using a bienzyme-immobilized system, decarboxylase-diamine oxidase ... 

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