Zobrazeno 1 - 10
of 24
pro vyhledávání: '"35"'
Autor:
Kenneth M. Merz
Publikováno v:
Journal of the American Chemical Society. 113:3572-3575
Publikováno v:
Journal of the American Chemical Society. 133(25)
In this study, mono- and pentacyclic C(35) terpenes from Bacillus subtilis were biosynthesized via the cyclization of C(35) isoprenoid using purified enzymes, including the first identified new terpene cyclase that shows no sequence homology to any o
Autor:
Dominique Florentin, Michel Azoulay, Jean-Claude Tabet, Georges Guillerm, François Frappier, Andrée Marquet
Publikováno v:
Journal of the American Chemical Society. 115:2139-2145
Previous results led to the conclusion that the last step of biotin biosynthesis, the sulfuur insertion into dethiobiotin should involve a thiol as intermediate. The three possible thiols have been synthesized and their biological activity was evalua
Publikováno v:
Journal of the American Chemical Society. 140:15744-15752
Class Ia ribonucleotide reductase (RNR) of Escherichia coli contains an unusually stable tyrosyl radical cofactor in the β2 subunit (Y122•) necessary for nucleotide reductase activity. Upon binding the cognate α2 subunit, loaded with nucleoside d
Publikováno v:
Journal of the American Chemical Society. 139:16657-16665
Ribonucleotide reductases (RNR) catalyze the reduction of nucleotides to deoxynucleotides through a mechanism involving an essential cysteine based thiyl radical. In the E. coli class 1a RNR the thiyl radical (C439•) is a transient species generate
Autor:
John F. Quinn, Michael R. Whittaker, Phillip J. Hogg, Paul Wilson, Thomas P. Davis, Kristian Kempe, Sarah Mann, Athina Anastasaki, Angus P. R. Johnston, David M. Haddleton, Matthew R. Owen
Publikováno v:
Journal of the American Chemical Society. 137:4215-4222
The entropy-driven affinity of trivalent (in)organic arsenicals for closely spaced dithiols has been exploited to develop a novel route to peptide/protein-polymer conjugation. A trivalent arsenous acid (As(III)) derivative (1) obtained from p-arsanil
Autor:
Alexey Silakov, Denise A. Conner, Wei Jiang, Mohammad R. Seyedsayamdost, Bigna Wörsdörfer, Kenichi Yokoyama, J. Martin Bollinger, JoAnne Stubbe, Carsten Krebs, Jovan Livada
Publikováno v:
Journal of the American Chemical Society. 135:8585-8593
The class Ia ribonucleotide reductase (RNR) from Escherichia coli (Ec) employs a free-radical mechanism, which involves bidirectional translocation of a radical equivalent or “hole” over a distance of ∼35 Å from the stable diferric/tyrosyl-rad
Autor:
Michal Avital-Shmilovici, Kalyaneswar Mandal, Nelson B. Phillips, Michael A. Weiss, Zachary P. Gates, Stephen B. H. Kent
Publikováno v:
Journal of the American Chemical Society. 135:3173-3185
Efficient total synthesis of insulin is important to enable the application of medicinal chemistry to the optimization of the properties of this important protein molecule. Recently we described "ester insulin"--a novel form of insulin in which the f
Publikováno v:
Journal of the American Chemical Society. 134:2520-2523
The reaction of a class I ribonucleotide reductase (RNR) begins when a cofactor in the β subunit oxidizes a cysteine residue ~35 Å away in the α subunit, generating a thiyl radical. In the class Ic enzyme from Chlamydia trachomatis (Ct), the cyste
Publikováno v:
Journal of the American Chemical Society. 133:19807-19815
S-adenosylhomocysteine hydrolase (SAHH), a cellular enzyme that plays a key role in methylation reactions including those required for maturation of viral mRNA, is an important drug target in the discovery of antiviral agents. While targeting the act