Zobrazeno 1 - 10
of 77
pro vyhledávání: '"Coenzyme analog"'
A templated RNA synthesis is characterized in which G5′pp5′G accelerates synthesis of A5′pp5′A from pA and chemically activated ImpA precursors. Similar acceleration is not observable in the presence of UppU, CppC, AppG, AppA, or pG alone. Th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::115e3bdc27c3681edcd9e308779c1697
https://europepmc.org/articles/PMC5733574/
https://europepmc.org/articles/PMC5733574/
Publikováno v:
The Journal of Physical Chemistry C. 115:310-316
Polarization modulation infrared reflection absorption spectroscopy (PM-IRRAS) and (in situ) surface-enhanced (resonant) Raman scattering (SE(R)RS) were used as “quality control” tools during the construction of a model biofuel cell anode. The mo
Publikováno v:
FEBS Journal. 275:5960-5968
Adenosylcobalamin (AdoCbl)-dependent glutamate mutase from Clostridium tetanomorphum comprises two weakly-associating subunits, MutS and MutE, which combine with AdoCbl to form the active holo-enzyme. Three coenzyme analogs, methylcobinamide (MeCbi),
Autor:
van den Heuvel, R.H.H., Tahallah, N., Kamerbeek, N.M, Fraaije, M.W., Berkel, W.J.H., Janssen, D.B., Heck, A.J.R., van Berkel, WJH
Publikováno v:
The Journal of Biological Chemistry, 280(37), 32115-32121. AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280 (37), pp.32115-21. ⟨10.1074/jbc.M503758200⟩
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2005, 280 (37), pp.32115-21. ⟨10.1074/jbc.M503758200⟩
International audience; The NADPH-dependent dimeric flavoenzyme 4-hydroxyacetophenone monooxygenase (HAPMO) catalyzes Baeyer-Villiger oxidations of a wide range of ketones, thereby generating esters or lactones. In the current work, we probed HAPMO-c
Autor:
C. R. Lowe, Richard J. Ansell
Publikováno v:
Applied Microbiology and Biotechnology. 51:703-710
A range of biomimetic analogues of the nicotinamide nucleotide coenzymes NAD(P)(H) have been developed based on the structure of a triazine dye template. These biomimetic redox coenzymes are relatively straightforward and inexpensive to synthesise an
Publikováno v:
Journal of Molecular Catalysis B: Enzymatic. 6:111-123
The interactions of CL4, a biomimetic analogue of NAD + comprising a nicotinamide functionality coupled via a triazine ring to a dibenzenesulphonic acid unit, and of a series of analogues, with HLADH and other dehydrogenases have been compared to tho
Publikováno v:
Hardman, S J O, Pudney, C R, Hay, S & Scrutton, N S 2013, ' Excited state dynamics can be used to probe donor-acceptor distances for H-tunneling reactions catalyzed by flavoproteins ', BIOPHYSICAL JOURNAL, vol. 105, no. 11, pp. 2549-2558 . https://doi.org/10.1016/j.bpj.2013.10.015
In enzyme systems where fast motions are thought to contribute to H-transfer efficiency, the distance between hydrogen donor and acceptor is a very important factor. Sub-ångstrom changes in donor-acceptor distance can have a large effect on the rate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d44ecc83bfc52b0fc48d8787f831e266
Publikováno v:
Tetrahedron. 52:14787-14800
The Knoevenagel condensation product of pyridoxal 5′-phosphate (1) with rhodanine (2) was prepared and identified as (Z)-5-[[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-4-pyridinyl]methylene]-2-thioxo-4-thiazolidinone (3). The labile (E)-stereoisom
Publikováno v:
Enzyme and Microbial Technology. 18:570-580
A series of nicotinamide-containing compounds based on the structure of a triazine dye, C.I. Reactive Blue 2, which is known to interact at the coenzyme-binding sites of several NAD(P)(H)-dependent dehydrogenases,1,2 were designed, synthesized, and c
Autor:
Atsuyoshi Ohno, Yuji Mikata, Norimasa Yamazaki, Yasushi Kawai, Akihiro Tsutsumi, Masayuki Fujii, Mutsuo Okamura
Publikováno v:
Bulletin of the Chemical Society of Japan. 69:1093-1098
The molecular structure of an enantiomer of nicotinamide coenzyme analog 1 has been determined by X-ray crystallography with the absolute configuration being established by the anomalous dispersion effects of all non-hydrogen atoms: (+)-1 exhibits (S