KUNOW, J and SCHWORER, B and STETTER, KO and THAUER, RK (1993) A F(420)-DEPENDENT NADP REDUCTASE IN THE EXTREMELY THERMOPHILIC SULFATE-REDUCING ARCHAEOGLOBUS-FULGIDUS. ARCHIVES OF MICROBIOLOGY, 160 (3). pp. 199-205. ISSN 0302-8933,
Full text not available from this repository.Abstract
Archaeoglobus fulgidus, a sulfate-reducing Archaeon with a growth temperature optimum of 83-degrees-C, uses the 5-deazaflavin coenzyme F420 rather than pyridine nucleotides in catabolic redox processes. The organism does, however, require reduced pyridine nucleotides for biosynthetic purposes. We describe here that the Archaeon contains a coenzyme F420-dependent NADP reductase which links anabolism to catabolism. The highly thermostable enzyme was purified 3600-fold by affinity chromatography to apparent homogeneity in a 60% yield. The native enzyme with an apparent molecular mass of 55 kDa was composed of only one type of subunit of apparent molecular mass of 28 kDa. Spectroscopic analysis of the enzyme did not reveal the presence of any chromophoric prosthetic group. The purified enzyme catalyzed the reversible reduction of NADP (apparent K(M) 40 muM) with reduced F420 (apparent K(M) 20 muM) with a specific activity of 660 U/mg (apparent V(max)) at pH 8.0 (pH optimum) and 80-degrees-C (temperature optimum). It was specific for both coenzyme F420 and NADP. Stereochemical investigations showed that the F420-dependent NADP reductase was Si face specific with respect to C5 of F420 and Si face specific with respect to C4 of NADP.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | METHANOCOCCUS-VANNIELII; METHANOPYRUS-KANDLERI; TETRAHYDROMETHANOPTERIN; ARCHAEBACTERIA; PURIFICATION; METHANOGENESIS; DEHYDROGENASE; CLEAVAGE; BACTERIA; ARCHAEA; SULFATE REDUCERS; HYPERTHERMOPHILES; COENZYME-F(420); DEAZAFLAVIN; F(420)-DEPENDENT NADP REDUCTASE; STEREOSELECTIVITY; STEREOSPECIFICITY; ARCHAEOGLOBUS-FULGIDUS |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:42 |
| URI: | https://pred.uni-regensburg.de/id/eprint/53786 |
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