Zobrazeno 1 - 10
of 106
pro vyhledávání: '"Barbiturase"'
Autor:
Zarrin Basharat
Publikováno v:
African Journal of Biotechnology; Vol 13, No 2 (2014)
Barbiturases exist solely in bacteria and encompass an undistinguished protein family. s-Triazine compound introduction into the environment owing to recent industrial practices have revitalized barbiturases. Codon usage patterns were analysed in thi
Publikováno v:
In Journal of Biological Chemistry 1 March 2002 277(9):7051-7058
Autor:
Azra Yasmin, Zarrin Basharat
Barbiturases have scarce structural information available and do not fit in the conventional group of proteins. It is contemplated that they play a role in catabolism of s-triazine herbicide compounds. Structure as well as interaction data informatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::049502b8f48f94cb030a7b2e953c4e5e
https://doi.org/10.7287/peerj.preprints.2070v1
https://doi.org/10.7287/peerj.preprints.2070v1
Publikováno v:
In Biochemical and Biophysical Research Communications 10 August 2001 286(1):222-226
Akademický článek
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Publikováno v:
Biochemical and Biophysical Research Communications. 286:222-226
Amidohydrolytic reactions in oxidative pyrimidine metabolism were investigated in detail. Barbiturase has been reported to catalyze the amidohydrolysis of barbituric acid to urea and malonic acid. However, purification of the enzyme revealed that it
Autor:
Anthony G. Dodge, Jack E. Richman, Seunghee Cho, Lawrence P. Wackett, Stephan M. Cameron, Jennifer L. Seffernick, Jasmine S. Erickson, Michael J. Sadowsky
Cyanuric acid hydrolases (AtzD) and barbiturases are homologous, found almost exclusively in bacteria, and comprise a rare protein family with no discernible linkage to other protein families or an X-ray structural class. There has been confusion in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40c7c800b040007ffcc6135c7c4eaf48
https://europepmc.org/articles/PMC3415516/
https://europepmc.org/articles/PMC3415516/
Publikováno v:
The Journal of biological chemistry. 277(9)
Barbiturase, which catalyzes the reversible amidohydrolysis of barbituric acid to ureidomalonic acid in the second step of oxidative pyrimidine degradation, was purified to homogeneity from Rhodococcus erythropolis JCM 3132. The characteristics and g
Autor:
Dietmar Schomburg, Margit Salzmann
Publikováno v:
Enzyme Handbook 4 ISBN: 9783642489860
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6dd4da9bb75c6ed1be09c3e41780009c
https://doi.org/10.1007/978-3-642-84437-9_169
https://doi.org/10.1007/978-3-642-84437-9_169
Akademický článek
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