The production of diazotizable amines by a simple degradative reaction of purines
12
Citation
5
Reference
10
Related Paper
Keywords:
Hypoxanthine
Purine metabolism
Xanthine
Eimeria maxima
Cite
Citations (15)
Hypoxanthine
Purine metabolism
Xanthine
Cite
Citations (12)
Hypoxanthine
Allantoin
Xanthine
Purine metabolism
Chlorella pyrenoidosa
Catabolism
Cite
Citations (42)
ABSTRACT The discovery that two distinct enzyme catalysts, purine hydroxylase (PH) and xanthine dehydrogenase (XDH), are required for the overall conversion of hypoxanthine to uric acid by Clostridium purinolyticum was unexpected. In this reaction sequence, hypoxanthine is hydroxylated to xanthine by PH and then xanthine is hydroxylated to uric acid by XDH. PH and XDH, which contain a labile selenium cofactor in addition to a molybdenum cofactor, flavin adenine dinucleotide, and FeS centers, were purified and partially characterized as reported previously. In the present study, the activities of these two enzymes were measured in cells grown in media containing various concentrations of selenite, molybdate, and various purine substrates. The levels of PH protein in extracts were determined by immunoblot assay. The amount of PH protein, as well as the specific activities of PH and XDH, increased when either selenite or molybdate was added to the culture medium. PH levels were highest in the cells cultured in the presence of either adenine or purine. XDH activity increased dramatically in cells grown with either xanthine or uric acid. The apparent increases in protein levels and activities of PH and XDH in response to selenium, molybdenum, and purine substrates demonstrate that these enzymes are tightly regulated in response to these nutrients.
Xanthine dehydrogenase
Hypoxanthine
Xanthine
Molybdenum Cofactor
Purine metabolism
Formate dehydrogenase
Cite
Citations (25)
Aspergillus nidulans
Xanthine
Purine metabolism
Hypoxanthine
Catabolism
Structural gene
Cite
Citations (5)
Journal Article Arxula adeninivorans xanthine oxidoreductase and its application in the production of food with low purine content Get access D.A. Jankowska, D.A. Jankowska Leibniz Institute of Plant Genetics and Crop Plant Research (IPK) Gatersleben Germany Search for other works by this author on: Oxford Academic Google Scholar A. Trautwein‐Schult, A. Trautwein‐Schult Leibniz Institute of Plant Genetics and Crop Plant Research (IPK) Gatersleben Germany Search for other works by this author on: Oxford Academic Google Scholar A. Cordes, A. Cordes ASA Spezialenzyme GmbH Am Exer 19c Wolfenbüttel Germany Search for other works by this author on: Oxford Academic Google Scholar P. Hoferichter, P. Hoferichter ASA Spezialenzyme GmbH Am Exer 19c Wolfenbüttel Germany Search for other works by this author on: Oxford Academic Google Scholar C. Klein, C. Klein ASA Spezialenzyme GmbH Am Exer 19c Wolfenbüttel Germany Search for other works by this author on: Oxford Academic Google Scholar R. Bode, R. Bode Institute of Biochemistry University of Greifswald Greifswald Germany Search for other works by this author on: Oxford Academic Google Scholar K. Baronian, K. Baronian School of Biological Sciences University of Canterbury Christchurch New Zealand Search for other works by this author on: Oxford Academic Google Scholar G. Kunze G. Kunze Leibniz Institute of Plant Genetics and Crop Plant Research (IPK) Gatersleben Germany Correspondence Gotthard Kunze, Leibniz Institute of Plant Genetics and Crop Plant Research (IPK), Corrensstr. 3, D‐06466 Gatersleben, Germany. E‐mail: kunzeg@ipk-gatersleben.de Search for other works by this author on: Oxford Academic Google Scholar Journal of Applied Microbiology, Volume 115, Issue 3, 1 September 2013, Pages 796–807, https://doi.org/10.1111/jam.12284 Published: 01 September 2013 Article history Received: 05 April 2013 Revision received: 04 June 2013 Accepted: 11 June 2013 Published: 01 September 2013
Cite
Citations (22)
Inosine
Hypoxanthine
Xanthine
Purine metabolism
Inosine monophosphate
Guanosine monophosphate
Cite
Citations (5)
Aspergillus mutants resistant to various purine analogues (purine, 8-azaguanine, 2-thioxanthine, and 2-thiouric acid) are defective in at least one step of purine uptake or breakdown. The properties of these mutants show that there are two uptake systems for purines, one which mediates the uptake of hypoxanthine, guanine, and adenine, and the other, xanthine and uric acid. Allantoinase-less strains are sensitive to the toxic effects of allantoin accumulation. They are severely inhibited when grown in the presence of naturally occurring purines. Mutant strains derived from these, resistant to naturally occurring purines, may be isolated. These are either wild-type revertants, or carry a second metabolic block in the uptake or breakdown of purines. The properties of these double mutants confirm the interpretation of the nature of the analogue-resistant mutants.
Purine metabolism
Hypoxanthine
Aspergillus nidulans
Xanthine
Cite
Citations (89)
Allantoin
Hypoxanthine
Xanthine
Catabolism
Purine metabolism
Inosine
Theobromine
De novo synthesis
Cite
Citations (4)
The overall metabolism of purines was studied in tobacco (Nicotiana tabacum) mesophyll protoplasts. Metabolic pathways were studied by measuring the conversion of radioactive adenine, adenosine, hypoxanthine and guanine into purine ribonucleotides, ribonucleosides, bases and nucleic acid constituents. Adenine was extensively deaminated to hypoxanthine, whereupon it was also converted into AMP and incorporated into nucleic acids. Adenosine was mainly hydrolysed to adenine. Inosinate formed from hypoxanthine was converted into AMP and GMP, which were then catabolized to adenine and guanosine respectively. Guanine was mainly deaminated to xanthine and also incorporated into nucleic acids via GTP. Increased RNA synthesis in the protoplasts resulted in enhanced incorporation of adenine and guanine, but not of hypoxanthine and adenosine, into the nucleic acid fraction. The overall pattern of purine-nucleotide metabolic pathways in protoplasts of tobacco leaf mesophyll is proposed.
Hypoxanthine
Purine metabolism
Xanthine
Adenine nucleotide
Cite
Citations (30)