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Autor:
Motonari Tsubaki, Kazuo Kobayashi, Toshihide Okajima, Hiroshi Hori, Katsuyuki Tanizawa, Tadashi Nakai, Yasuhiro Takahashi, Hiroto Ito
Publikováno v:
Journal of Biological Chemistry. 290:11144-11166
The bacterial enzyme designated QhpD belongs to the radical S-adenosyl-L-methionine (SAM) superfamily of enzymes and participates in the post-translational processing of quinohemoprotein amine dehydrogenase. QhpD is essential for the formation of int
Publikováno v:
Journal of Biological Chemistry. 290:4118-4128
During the anaerobic fermentation of glucose to ethanol, the three micro-organisms Saccharomyces cerevisiae, Zymomonas mobilis, and Leuconostoc mesenteroides exploit, respectively, the Embden-Meyerhof-Parnas, the Entner-Doudoroff, and the reductive p
Autor:
Makoto Hashimoto, Katsuhiko Kitamoto, Isao Fujii, Tsukasa Koen, Hiroaki Takahashi, Chihiro Suda
Publikováno v:
Journal of Biological Chemistry. 289:19976-19984
The type III polyketide synthases from fungi produce a variety of secondary metabolites including pyrones, resorcinols, and resorcylic acids. We previously reported that CsyB from Aspergillus oryzae forms α-pyrone csypyrone B compounds when expresse
Publikováno v:
Journal of Biological Chemistry. 288:12175-12186
Cellulase enzymes cleave glycosidic bonds in cellulose to produce cellobiose via either retaining or inverting hydrolysis mechanisms, which are significantly pH-dependent. Many fungal cellulases function optimally at pH ~5, and their activities decre
Autor:
Alan R. Brash, William E. Boeglin
Publikováno v:
Journal of Biological Chemistry. 287:24139-24147
The ability of hemoproteins to catalyze epoxidation or hydroxylation reactions is usually associated with a cysteine as the proximal ligand to the heme, as in cytochrome P450 or nitric oxide synthase. Catalase-related allene oxide synthase (cAOS) fro
Publikováno v:
Journal of Biological Chemistry. 285:20615-20624
In the aerobic metabolism of aromatic substrates, oxygenases use molecular oxygen to hydroxylate and finally cleave the aromatic ring. In the case of the common intermediate benzoate, the ring cleavage substrates are either catechol (in bacteria) or
Publikováno v:
Journal of Biological Chemistry. 284:21856-21862
Thermotoga maritima is a Gram-negative, hyperthermophilic bacterium whose peptidoglycan contains comparable amounts of L- and D-lysine. We have determined the fine structure of this cell-wall polymer. The muropeptides resulting from the digestion of
Autor:
Bärbel Thiele, Michael Müller, Oliver Rieder, Nico Jehmlich, Martin von Bergen, Matthias Boll
Publikováno v:
Journal of Biological Chemistry. 283:20713-20721
Benzoyl-CoA reductases (BCRs) are key enzymes of anaerobic aromatic metabolism in facultatively anaerobic bacteria. The highly oxygen-sensitive enzymes catalyze the ATP-dependent reductive dearomatization of the substrate, yielding cyclohexa-1,5-dien
Publikováno v:
Journal of Biological Chemistry. 281:27-35
The ActVA-ActVB system from Streptomyces coelicolor isatwo-component flavin-dependent monooxygenase that belongs to an emerging class of enzymes involved in various oxidation reactions in microorganisms. The ActVB component is a NADH:flavin oxidoredu
Autor:
David Marçal, Maria Arménia Carrondo, Francisco J. Enguita, Peter F. Lindley, Rosa Grenha, Adriano O. Henriques, Lígia O. Martins
Publikováno v:
Journal of Biological Chemistry. 279:23472-23476
The CotA laccase from the endospore coat of Bacillus subtilis has been crystallized in the presence of the non-catalytic co-oxidant 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonate) (ABTS), and the structure was determined using synchrotron radiatio