Guanosine Deaminase and Guanine Deaminase from Tea Leaves

Negishi, Osamu; Ozawa, Tetsuo; Imagawa, Hiroshi

doi:10.1271/bbb.58.1277

Cited by 24 publications

(20 citation statements)

References 5 publications

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“…The enzyme produced by other organisms may be monomeric or dimeric [Glantz and Lewis, 1978;Maynes et al, 2000;Negishi et al, 1994;Nolan, 1984]. Guanine deaminases have been reported to have molecular masses per subunit of between 50 and 60 kDa [Bergstrom and Bieber, 1979;Gupta and Glantz, 1985;Miyamoto et al, 1982;Rossi et al, 1978], which is consistent with our findings.…”

Section: ) Was Homologous To the Conserved Sequence Pgx[v/i] Dxh[t/supporting

confidence: 92%

“…The reason for this and other changes in properties could be the C-terminal HisTag, which can influence protein structure and charge [Votchitseva et al, 2006]. The K m values are similar to the values described for other guanine deaminases (4-42 μ M ) [Bergstrom and Bieber, 1979;Fogle and Bieber, 1975;Maynes et al, 2000;Miyamoto et al, 1982;Negishi et al, 1994;Nolan, 1984;Rossi et al, 1978].…”

Section: ) Was Homologous To the Conserved Sequence Pgx[v/i] Dxh[t/supporting

confidence: 74%

“…The endogenous Agdap from A. adeninivorans LS3 has two pH optima, which is also the case for the guanine deaminase of Camellia sinensis [Negishi et al, 1994]. This is in contrast to guanine deaminases of other organisms, which have a single optimum between pH 6.8 and 9.4 [Bergstrom and Bieber, 1979;Fogle and Bieber, 1975;Miyamoto et al, 1982;Nolan, 1984].…”

Section: ) Was Homologous To the Conserved Sequence Pgx[v/i] Dxh[t/mentioning

confidence: 97%

“…It catalyses the irreversible deamination of guanine to xanthine and ammonia [Fernández et al, 2010;Glantz and Lewis, 1978;Lehninger, 2004;Maynes et al, 2000]. It is responsible for purine degradation in bacteria [Liaw et al, 2004;Maynes et al, 2000], lower eukaryotes [Nolan, 1984;Saint-Marc and Daignan-Fornier, 2004;Shavlovskii and Kuznetsova, 1974], plants [Barankiewicz and Paszkowski, 1980;Negishi et al, 1994] and is present in the liver [Gupta and Glantz, 1985;Lewis and Glantz, 1974] and kidney [Kubo et al, 2006] of higher eukaryotes. Guanine deaminase was also found to be active in the brain of higher eukaryotes [Berger et al, 1985;Kumar and Rathi, 1980;Miyamoto et al, 1982;Rossi et al, 1978] where it plays an important role in the branching of dendrites [Fernández et al, 2009].…”

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confidence: 99%

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Arxula adeninivorans Recombinant Guanine Deaminase and Its Application in the Production of Food with Low Purine Content

Trautwein-Schult

Jankowska²,

Cordes³

et al. 2014

Microb Physiol

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Purines of exogenous and endogenous sources are degraded to uric acid in human beings. Concentrations >6.8 mg uric acid/dl serum cause hyperuricemia and its symptoms. Pharmaceuticals and the reduction of the intake of purine-rich food are used to control uric acid levels. A novel approach to the latter proposition is the enzymatic reduction of the purine content of food by purine-degrading enzymes. Here we describe the production of recombinant guanine deaminase by the yeast Arxula adeninivorans LS3 and its application in food. In media supplemented with nitrogen sources hypoxanthine or adenine, guanine deaminase (AGDA) gene expression is induced and intracellular accumulation of guanine deaminase (Agdap) protein occurs. The characteristics of the guanine deaminase isolated from wild-type strain LS3 and a transgenic strain expressing the AGDA gene under control of the strong constitutive TEF1 promoter were determined and compared. Both enzymes were dimeric and had temperature optima of 55°C with high substrate specificity for guanine and localisation in both the cytoplasm and vacuole of yeast. The enzyme was demonstrated to reduce levels of guanine in food. A mixture of guanine deaminase and other purine degradation enzymes will allow the reduction of purines in purine-rich foods.

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Section: ) Was Homologous To the Conserved Sequence Pgx[v/i] Dxh[t/supporting

confidence: 92%

Section: ) Was Homologous To the Conserved Sequence Pgx[v/i] Dxh[t/supporting

confidence: 74%

Section: ) Was Homologous To the Conserved Sequence Pgx[v/i] Dxh[t/mentioning

confidence: 97%

mentioning

confidence: 99%

See 2 more Smart Citations

Arxula adeninivorans Recombinant Guanine Deaminase and Its Application in the Production of Food with Low Purine Content

Trautwein-Schult

Jankowska²,

Cordes³

et al. 2014

Microb Physiol

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show abstract

“…Neither XMP nor inosine gives rise to xanthosine in vivo. activity has been detected in cell-free extracts of potato (Solanum tuberosum) tubers (Katahira and Ashihara, 2006), and the enzyme has been partially purified from leaves of tea (Camellia sinensis; Negishi et al, 1994). Because GDA activity is generally absent or low in plant extracts (Katahira and Ashihara, 2006), it has been proposed that GSDA is the main deaminating activity in the catabolic route from GMP to xanthine (Stasolla et al, 2003).…”

Section: Discussionmentioning

confidence: 99%