Adenosine Aminohydrolase from <i>Halobacterium cutirubrum</i>

Bauer, Randy J.; Carlberg, David M.

doi:10.1139/o73-077

Cited by 9 publications

(5 citation statements)

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“…However, two reports have been published on purine enzymes from H. cutirubrum, one regarding a search for deaminase activities in crude extracts by using guanine, guanosine, adenine, adenosine, and 2Ј-deoxyadenosine, as well as a number of purine nucleotides, as substrates. Only adenosine and 2Ј-deoxyadenosine deaminase activities were found (1). This agrees with the results of the present study, except for our demonstration of the presence of guanine deaminase activity.…”

Section: Discussionsupporting

confidence: 93%

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Purine Salvage in Two Halophilic Archaea: Characterization of Salvage Pathways and Isolation of Mutants Resistant to Purine Analogs

Stuer‐Lauridsen

Nygaard

1998

J Bacteriol

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In exponentially growing cultures of the extreme halophileHalobacterium halobium and the moderate halophileHaloferax volcanii, growth characteristics including intracellular protein levels, RNA content, and nucleotide pool sizes were analyzed. This is the first report on pool sizes of nucleoside triphosphates, NAD, and PRPP (5-phosphoribosyl-α-1-pyrophosphate) in archaea. The presence of a number of salvage and interconversion enzymes was determined by enzymatic assays. The levels varied significantly between the two organisms. The most significant difference was the absence of GMP reductase activity in H. halobium. The metabolism of exogenous purines was investigated in growing cultures. Both purine bases and nucleosides were readily taken up and were incorporated into nucleic acids. Growth of both organisms was affected by a number of inhibitors of nucleotide synthesis.H. volcanii was more sensitive than H. halobium, and purine base analogs were more toxic than nucleoside analogs. Growth of H. volcanii was inhibited by trimethoprim and sulfathiazole, while these compounds had no effect on the growth of H. halobium. Spontaneous mutants resistant to purine analogs were isolated. The most frequent cause of resistance was a defect in purine phosphoribosyltransferase activity coupled with reduced purine uptake. A single phosphoribosyltransferase seemed to convert guanine as well as hypoxanthine to nucleoside monophosphates, and another phosphoribosyltransferase had specificity towards adenine. The differences in the metabolism of purine bases and nucleosides and the sensitivity to purine analogs between the two halobacteria were reflected in differences in purine enzyme levels. Based on our results, we conclude that purine salvage and interconversion pathways differ just as much between the two archaeal species as among archaea, bacteria, and eukarya.

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Section: Discussionsupporting

confidence: 93%

“…Most investigations of purine salvage metabolism within the archaea have dealt with members of the methanogens (2,(6)(7)(8)39). The presence of a few purine salvage enzymes in the halophilic archaeon Halobacterium cutirubrum has been demonstrated (1,9).…”

mentioning

confidence: 99%

Purine Salvage in Two Halophilic Archaea: Characterization of Salvage Pathways and Isolation of Mutants Resistant to Purine Analogs

Stuer‐Lauridsen

Nygaard

1998

J Bacteriol

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“…Later on, further studies were carried out to determine the substrate specificity for adenosine analogs. The enzyme was able to deaminate 8-azaadenosine, whereas no activity was detected for 6-chloropurineribofuranoside and 8aminoadenosine (Bauer and Carlberg 1973). These results agree with those reported for both Halobacteirum volcanii and Halobacterium halobium (Stuer-Lauridsen and Nygaard 1998) (Fig.…”

Section: Purine Deaminases (Das)supporting

confidence: 92%

“…Besides the deaminases from methanogens, Bauer and Carlberg (1973) looked for enzymes with deaminase activity in crude extracts of Halobacterium cutirubrum. Guanine, guanosine, adenine, adenosine, and 2′-deoxyadenosine were tested as substrates, and deaminase activity was exclusively detected with the last two substrates.…”

Section: Purine Deaminases (Das)mentioning

confidence: 99%

Purine and pyrimidine salvage pathway in thermophiles: a valuable source of biocatalysts for the industrial production of nucleic acid derivatives

Arco

Fernández‐Lucas

2018

Appl Microbiol Biotechnol

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Your article is protected by copyright and all rights are held exclusively by Springer-Verlag GmbH Germany, part of Springer Nature. This e-offprint is for personal use only and shall not be self-archived in electronic repositories. If you wish to self-archive your article, please use the accepted manuscript version for posting on your own website. You may further deposit the accepted manuscript version in any repository, provided it is only made publicly available 12 months after official publication or later and provided acknowledgement is given to the original source of publication and a link is inserted to the published article on Springer's website. The link must be accompanied by the following text: "The final publication is available at link.springer.com".

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“…The results show that the hydrolytic deaminating activity of the extracts of P. politans NRC-510 was similar to that of Aspergillus terricola DSM 358(ABU-SHADY et al 1994), Escherichia coliK-12 (TAKETO and KUNO 1972), Aspergillus melleus(FUJISHIMA and YOSHINO 1972), Streptomyces aureofaciens(HODALOVA et al 1972), Halobacterium cutirubrum(BAUER and CALBERG 1973), Streptomyces viridiviolaceus NRC 35 (ALLAM et al 1981), Pseudomonas iodinum IFO 3558(SAKAI and JUN 1978) and Klebsiella sp. LF1202(LING et al 1991) which contain a deaminating mechanism that deaminate purine nucleoside adenosine and differs from Peni-…”

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confidence: 67%

Deamination of adenosine by extracts of Penicillium politans NRC‐510

Elshafei

Mohamed

Ali

2005

J. Basic Microbiol.

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Cell-free extracts of nitrate-grown Penicillium politans NRC-510 could catalyze the hydrolytic deamination of adenosine to inosine maximally at pH 6.0 and 45 degrees C. However the same extracts could not catalyze the N-glycosidic bond cleavage of adenosine at pH 4.0, 6.0 and 8.0. Incubation of the extracts at 55 degrees C for 30 minutes caused about 31% loss in activity whereas incubation of the extracts at 60 degrees C for 15 minutes caused a complete loss of enzyme activity. Results indicated the absence of the involvement of sulfhydryl groups in the catalytic site of adenosine deaminase. The enzyme is inhibited by ethylene diamine tetraacetate indicating that adenosine deaminase is a metalloenzyme. MnCl2 and MgCl2 had a remarkable activating effect, whereas HgCl2, CaCl2 and ZnSO4 showed an inhibitory effect on enzyme activity. Dialyzing the extracts for 24 hours significantly increase deaminase activity by about 33%. The apparent K(m) value was calculated for adenosine and found to be 3.63 x 10(-3) M, which indicates high affinity of adenosine deaminase for its substrate adenosine.

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Adenosine Aminohydrolase from Halobacterium cutirubrum

Cited by 9 publications

References 0 publications

Purine Salvage in Two Halophilic Archaea: Characterization of Salvage Pathways and Isolation of Mutants Resistant to Purine Analogs

Purine Salvage in Two Halophilic Archaea: Characterization of Salvage Pathways and Isolation of Mutants Resistant to Purine Analogs

Purine and pyrimidine salvage pathway in thermophiles: a valuable source of biocatalysts for the industrial production of nucleic acid derivatives

Deamination of adenosine by extracts of Penicillium politans NRC‐510

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