نتائج البحث

Structural Insights into the Very Low Activity of the Homocoenzyme B 12 Adenosylmethylcobalamin in Coenzyme B 12 -Dependent Diol Dehydratase and Ethanolamine Ammonia-Lyase.

• Authors : Shibata N; Department of Life Science, Graduate School of Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo, 678-1297, Japan.; Higuchi Y

Subjects: Ethanolamine Ammonia-Lyase*/Ethanolamine Ammonia-Lyase*/Ethanolamine Ammonia-Lyase*/chemistry ; Ethanolamine Ammonia-Lyase*/Ethanolamine Ammonia-Lyase*/Ethanolamine Ammonia-Lyase*/metabolism ; Propanediol Dehydratase*/Propanediol Dehydratase*/Propanediol Dehydratase*/chemistry

• Source: Chemistry (Weinheim an der Bergstrasse, Germany) [Chemistry] 2022 Nov 21; Vol. 28 (65), pp. e202202196. Date of Electronic Publication: 2022 Sep 19.Publisher: Wiley-VCH Country of Publication: Germany NLM ID: 9513783 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1521-3765

تفاصيل العنوان

Resolution and characterization of contributions of select protein and coupled solvent configurational fluctuations to radical rearrangement catalysis in coenzyme B(12)-dependent ethanolamine ammonia-lyase

• Authors : Meghan Kohne; Wei Li; Alina Ionescu

Subjects: Salmonella typhimurium; Phosphothreonine; Solvents

• Source: Methods EnzymolMethods in Enzymology ISBN: 9780323955577

تفاصيل العنوان

Electron spin-labelling of the EutC subunit in B 12 -dependent ethanolamine ammonia-lyase reveals dynamics and a two-state conformational equilibrium in the N-terminal, signal-sequence-associated domain.

• Authors : Nforneh B; a Department of Physics , Emory University , Atlanta , GA , USA.; Bovell AM

Subjects: Spin Labels*; Ethanolamine Ammonia-Lyase/Ethanolamine Ammonia-Lyase/Ethanolamine Ammonia-Lyase/*chemistry ; Salmonella typhimurium/Salmonella typhimurium/Salmonella typhimurium/*chemistry

• Source: Free radical research [Free Radic Res] 2018 Mar; Vol. 52 (3), pp. 307-318. Date of Electronic Publication: 2017 Dec 18.Publisher: Informa Healthcare Country of Publication: England NLM ID: 9423872 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

تفاصيل العنوان

Electron spin-labelling of the EutC subunit in B12-dependent ethanolamine ammonia-lyase reveals dynamics and a two-state conformational equilibrium in the N-terminal, signal-sequence-associated domain.

• Authors : Nforneh, Benjamen¹; Bovell, Adonis M.¹; Warncke, Kurt¹

Subjects: *ENZYME kinetics; *ELECTRON spin; *GENE clusters

• Source: Free Radical Research. Mar2018, Vol. 52 Issue 3, p307-318. 12p. 2 Diagrams, 2 Charts, 4 Graphs.

تفاصيل العنوان

Purification and some properties of wild-type and N-terminal-truncated ethanolamine ammonia-lyase of Escherichia coli.

• Authors : Akita K; Department of Bioscience and Biotechnology, Graduate School of Natural Science and Technology, Okayama University, Tsushima-naka, Kita-ku, Okayama 700-8530, Japan.; Hieda N

Subjects: Escherichia coli/Escherichia coli/Escherichia coli/*enzymology ; Ethanolamine Ammonia-Lyase/Ethanolamine Ammonia-Lyase/Ethanolamine Ammonia-Lyase/*isolation & purification ; Ethanolamine Ammonia-Lyase/Ethanolamine Ammonia-Lyase/Ethanolamine Ammonia-Lyase/*metabolism

• Source: Journal of biochemistry [J Biochem] 2010 Jan; Vol. 147 (1), pp. 83-93. Date of Electronic Publication: 2009 Sep 16.Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

تفاصيل العنوان

Control of Solvent Dynamics around the B12-Dependent Ethanolamine Ammonia-Lyase Enzyme in Frozen Aqueous Solution by Using Dimethyl Sulfoxide Modulation of Mesodomain Volume

• Authors : Kurt Warncke; Benjamen Nforneh

Subjects: Salmonella typhimurium; 010402 general chemistry; 01 natural sciences

• Source: J Phys Chem B

تفاصيل العنوان

Native and nonnative reactions in ethanolamine ammonia-lyase are actuated by different dynamics

• Authors : Li, Wei; Warncke, Kurt;

• Source: Biophysical Journal ; volume 122, issue 19, page 3976-3985 ; ISSN 0006-3495

تفاصيل العنوان

Functions of the D-ribosyl moiety and the lower axial ligand of the nucleotide loop of coenzyme B(12) in diol dehydratase and ethanolamine ammonia-lyase reactions.

• Authors : Fukuoka M; Department of Bioscience and Biotechnology, Faculty of Engineering, Okayama University, Tsushima-naka, Okayama 700-8530, Japan.; Yamada S

Subjects: Ligands* ; Nucleic Acid Conformation*; Cobamides/Cobamides/Cobamides/*chemistry

• Source: Journal of biochemistry [J Biochem] 2002 Dec; Vol. 132 (6), pp. 935-43.Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print Cited Medium: Print ISSN: 0021-924X

تفاصيل العنوان

Homoadenosylcobalamins as probes for exploring the active sites of coenzyme B12-dependent diol dehydratase and ethanolamine ammonia-lyase.

• Authors : Fukuoka, Masaki¹; Nakanishi, Yuka¹; Hannak, Renate B.²

Subjects: *COENZYMES; *ENZYMES; *ETHANOLAMINES

• Source: FEBS Journal. Sep2005, Vol. 272 Issue 18, p4787-4796. 10p.

تفاصيل العنوان

Magnetic Field Effects on B$_{12}$ Ethanolamine Ammonia Lyase: Evidence for a Radical Mechanism

• Authors : Harkins, Timothy T.; Grissom, Charles B.

• Source: Science, 1994 Feb . 263(5149), 958-960.

تفاصيل العنوان