Zobrazeno 1 - 10
of 139
pro vyhledávání: '"Lars G. Ljungdahl"'
Publikováno v:
Chemistry and Biochemistry of Flavoenzymes ISBN: 9781351070577
5,10-Methylenetetrahydrofolate reductase catalyzes the two electron reduction of 5,10-niethylenetetrahydrofolate (CH2-H4folate) to 5-methyltetrahydrofolate (CH3-H4folate). Methylene-H4folate reductases have been purified from two acetogenic bacteria,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0a09a7f7f1a790b0053e8c2da4d27107
https://doi.org/10.1201/9781351070577-17
https://doi.org/10.1201/9781351070577-17
Autor:
Lars G. Ljungdahl
Publikováno v:
Annual Review of Microbiology. 63:1-25
Frankly, I was surprised to receive an invitation to write a prefatory chapter for the Annual Review of Microbiology. I have read several such chapters written by outstanding researchers, many of whom I know and admire. I did not think I belonged to
Autor:
Ravi D. Barabote, Elizabeth Saunders, Stephen W. Ragsdale, Gary Xie, Lars G. Ljungdahl, Thomas Brettin, John C. Detter, Paul D. Richardson, Cliff Han, Elizabeth Pierce, Amaresh Das
Publikováno v:
Environmental Microbiology. 10:2550-2573
Summary This paper describes the genome sequence of M. thermoacetica (f. Clostridium thermoaceticum), which is the model acetogenic bacterium that has been widely used for elucidating the WoodLjungdahl pathway of CO and CO2 fixation. This pathway, wh
Autor:
Lars G. Ljungdahl
Publikováno v:
Annals of the New York Academy of Sciences. 1125:308-321
Anaerobic fungi, first described in 1975 by Orpin, live in close contact with bacteria and other microorganisms in the rumen and caecum of herbivorous animals, where they digest ingested plant food. Seventeen distinct anaerobic fungi belonging to fiv
Publikováno v:
FEBS Letters. 579:4367-4373
Cellobiohydrolase A (CbhA) from Clostridium thermocellum is composed of an N-terminal carbohydrate-binding domain 4 (CBD4), an immunoglobulin-like domain (Ig), a glycoside hydrolase 9 (GH9), X1(1) and X1(2) domains, a CBD3, and a dockerin domain. All
Publikováno v:
Biochemistry. 44:6492-6501
Several members of a widespread class of bacterial and archaeal metalloflavoproteins, called FprA, likely function as scavenging nitric oxide reductases (S-NORs). However, the only published X-ray crystal structure of an FprA is for a protein charact
Publikováno v:
Journal of Bacteriology. 187:2020-2029
The gram-positive, thermophilic, acetogenic bacterium Moorella thermoacetica can reduce CO 2 to acetate via the Wood-Ljungdahl (acetyl coenzyme A synthesis) pathway. This report demonstrates that, despite its classification as a strict anaerobe, M. t
Publikováno v:
European Journal of Biochemistry. 124:397-404
Formyltetrahydrofolate synthetase (EC 6.3.4.3) from Clostridium thermoaceticum is a 240 000-molecular-weight, tetrameric enzyme composed of identical subunits. When negatively stained with uranyl acetate or sodium phosphotungstate the enzyme appears
Autor:
Lars G. Ljungdahl, Irina Kataeva, John Rose, Bi-Cheng Wang, Vladimir N. Uversky, Florian D. Schubot, John M. Brewer
Publikováno v:
Protein Engineering Design and Selection. 17:759-769
Cellobiohydrolase CbhA from Clostridium thermocellum cellulosome is a multi-modular protein composed starting from the N-terminus of a carbohydrate-binding module (CBM) of family 4, an immunoglobulin(Ig)-like module, a catalytic module of family 9 gl
Autor:
Carlos Roberto Felix, Michael A. Cotta, Bruce S. Dien, Xin-Liang Li, Lars G. Ljungdahl, Eduardo Ximenes, Huizhong Chen
Publikováno v:
Applied Biochemistry and Biotechnology. 113:233-250
A beta-glucosidase (BglA, EC 3.2.1.21) gene from the polycentric anaerobic fungus Orpinomyces PC-2 was cloned and sequenced. The enzyme containing 657 amino acid residues was homologous to certain animal, plant, and bacterial beta-glucosidases but la