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pro vyhledávání: '"and Andreas R. Klein"'
Publikováno v:
European Journal of Biochemistry. 239:93-97
Coenzyme F420 is a 5-deazaflavin. Upon reduction, 1,5-dihydro-coenzyme F420 is formed with a prochiral center at C5. In this study we report that the F420-dependent glucose-6-phosphate dehydrogenase from Mycobacterium smegmatis and the F420-dependent
Publikováno v:
Archives of Microbiology. 165:187-193
Publikováno v:
European Journal of Biochemistry. 233:372-376
H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase from methanogenic Archaea, which is a novel hydrogenase containing neither nickel nor iron-sulfur clusters, catalyzes the reversible reduction of N5,N10-methenyltetrahydomethanopterin (
Autor:
Rudolf K. Thauer, Andreas R. Klein
Publikováno v:
European Journal of Biochemistry. 227:169-174
Coenzyme F420-dependent methylenetetrahydromethanopterin dehydrogenase from methanogenic Archaea catalyzes the reversible transfer of a hydride ion from C14a of N5,N10-methylenetetra-hydromethanopterin to C5 of coenzyme F420. In this study, we report
Publikováno v:
Archives of Microbiology. 160:186-192
It was recently reported that the extreme thermophile Methanopyrus kandleri contains only a H2-forming N5,N10-methylenetetrahydromethanopterin dehydrogenase which uses protons as electron acceptor. We describe here the presence in this Archaeon of a
Publikováno v:
Archives of Microbiology. 159:225-232
The sulfate-reducing Archaeoglobus fulgidus contains a number of enzymes previously thought to be unique for methanogenic Archaea. The purification and properties of two of these enzymes, of formylmethanofuran: tetrahydromethanopterin formyltransfera
Publikováno v:
ChemInform. 28
Autor:
Rudolf K. Thauer, Andreas R. Klein
Publikováno v:
European journal of biochemistry. 245(2)
The mtd gene encoding coenzyme-F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase (Mtd) in the hyperthermophilic Methanopyrus kandleri has been cloned, sequenced and functionally overexpressed in Escherichia coli. The overproduced e
Publikováno v:
Chemical reviews. 96(7)
Publikováno v:
FEBS Letters. (2):203-206
H 2 -forming N 5 , N 10 -methylenetetrahydromethanopterin dehydrogenase catalyzes the reversible dehydrogenation of N 5 , N 10 -methylenetetrahydromethanopterin (CH 2 H 4 MPT) to N 5 , N 10 -methenyltetrahydromethanopterin (CH H 4 MPT + ) and