Arginine deaminase

Hibbs, J.B., Tiantor, R.R., and Vavrin, Z., Macrophage cytotoxicity Role for L-arginine deaminase and iminonitrogenoxidation of nitrite, Science, 235,473, 1987. 

Kenny (1973) recommends a Soy peptone-yeast dialysate medium (Appendix 4) for culture of mycoplasma. Inclusion of arginine (16 mM) and 0.4 mg% phenol red indicates the presence of arginine deaminase by formation of alkali (purple coloration). Alternatively, incubation with tritiated thymidine and analysis of the culture medium for tritiated thymine can be used to detect thymidine phosphorylase (House and Waddell, 1967). 

Figure 21 Haloacetamide-derived probes as potent tools for the labeling of arginine deaminase PAD4. The probe design is based on arginine as a natural substrate that is converted into a F/CI reactive group. Active site labeling occurs via a nucleophilic substitution of the halogene by the catalytically active cysteine of PAD4.

Active immobilized L-arginine deaminase for 442 the continuous production of L-citrulline Active immobilized enzyme for the continuous 409 conversion of starch into maltose... 

Bacterial electrodes [11, 31, 33, 46, 48, 49, 60] In this type of electrode, a suspension of suitable bacteria is placed between the sensor proper and a dialysis membrane that prevents passage of high-molecular substances (see fig. 8.3). The sensor is usually a gas probe. In the simple types of bacterial electrode, the determinand is converted by a suitable strain of bacteria into a product sensed by the gas probe. Thus it is possible to determine arginine [46], glutamine [48],/.-aspartic acid [31],/.-histidine [60] and nitrate [33]. Hybrid bacterial - enzyme electrodes contain both a bacterial strain and a suitable enzyme. For example, an extract from ivingas Neurospora chossa can be used as a source of NAD nucleosidase and an Escherichia coli culture as a source of nicotinamide deaminase, so that the electrode responds to NAD [49] as a result of the series of reactions... 

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.

Figure 4.7 (a) interaction of a dipyrromethane-based cofactor in porphobilinogen deaminase with an aspartic acid-derived side chain. The carboxylate residues of the co-factor are stabilised by protein arginine residnes. (b) general strnctnre of the prodigiosins (R, R = alkyl). 

Myosin sufficiently purified in the usual way does not dephosphorylate any of the numerous phosphate compounds of living muscle other than ATP, and perhaps ITP, nor can it transphosphorylate. Menne (1943) finds that myosin, unlike the other main fractions of muscle, can convert arginine, histidine, glycocyamine, and choline into creatine. The myosin used, however, was only reprecipitated once and subsequently washed, and it is possible that the enzyme activity might be lost on further precipitation. After fractionation and precipitating three times, myosin possesses an appreciable adenylic deaminase activity (Hermann and Josepovits, 1949 Summerson and Meister, 1944). 

Adenylosuccinate formed by adenylosuccinate synthetase is cleaved by adenylosuccinate lyase to form AMP. The reaction steps are illustrated in Fig. 1. Included in the sequence is the additional reaction catalyzed by AMP deaminase. These three enzymes have been suggested to function in a cyclic process termed the purine nucleotide cycle 7,8). The two-step conversion of IMP to AMP is very similar to both the conversion of citrulline to arginine, which involves formation of argininosuccinate as an intermediate, and formation of 5-amino-imidazole 4-carboxamide ribonucleotide from 5-aminoimidazole 4-carboxylate ribonucleotide as part of IMP biosynthesis. Adenylosuccinate lyase is a dual function enzyme catalyzing the cleavage of both adenylosuccinate and 5-aminoimidazole 4-N-succinocarboxamide ribonucleotide. 

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