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pro vyhledávání: '"35"'
Autor:
Frank M. Raushel, Leisha S. Mullins
Publikováno v:
Journal of the American Chemical Society. 121:3803-3804
Ammonia can replace glutamine as the ultimate source for the nitrogen requirement in the reaction presented above.3 A chemical mechanism for the enzymatic transformation is presented below in Scheme 1. The first ATP phosphorylates bicarbonate to form
Autor:
Matthew O. Ross, Igor D. Petrik, Pierre Moënne-Loccoz, Yelu Shi, Yi Lu, Qianhong Zhu, Ambika Bhagi-Damodaran, Julian Reed, Yong Zhang, Saumen Chakraborty, Evan N. Mirts
Publikováno v:
Journal of the American Chemical Society. 139(35)
The presence of nonheme metal, such as copper and iron, in the heme-copper oxidase (HCO) superfamily is critical to the enzymatic activity of reducing O2 to H2O, but the exact mechanism the nonheme metal ion uses to confer and fine-tune the activity
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
Publikováno v:
Journal of the American Chemical Society. 125:14728-14732
The description of reaction regulation in enzymes responsible for activating and catalyzing small molecules (O(2), NO) requires identification of ligand movement into the binding site and out of the enzyme through specific channels and docking sites.
Publikováno v:
Journal of the American Chemical Society, 125(35), 10570-10579. AMER CHEMICAL SOC
The binding of a series of p-alkylbenzamidinium chloride inhibitors to the serine proteinase trypsin over a range of temperatures has been studied using isothermal titration (micro)calorimetry and molecular dynamics simulation techniques. The inhibit
Autor:
Richard N. Armstrong, Christopher L. Rife, Stoyan K. Smoukov, Joshua Telser, Brian M. Hoffman, Bryan A Bernat
Publikováno v:
Journal of the American Chemical Society. 124(10)
FosA is a manganese metalloglutathione transferase that confers resistance to the broad-spectrum antibiotic fosfomycin, (1R,2S)-epoxypropylphosphonic acid. The reaction catalyzed by FosA involves the attack by glutathione on fosfomycin to yield the p