533-48-2Relevant articles and documents
Designing Selectivity in Dirhodium Metallopeptide Catalysts for Protein Modification
Martin, Samuel C.,Vohidov, Farrukh,Wang, Haopei,Knudsen, Sarah E.,Marzec, Alex A.,Ball, Zachary T.
, p. 659 - 665 (2017)
The ability to chemically alter proteins is important for broad areas of chemical biology, biophysics, and medicine. Chemical catalysts for protein modification, and particularly rhodium(II) conjugates, represent an important new approach to protein modification that develops novel functionalization approaches while shedding light on the development of selective chemistries in complex environments. Here, we elucidate the reaction parameters that allow selective catalysis and even discrimination among highly similar proteins. Furthermore, we show that quantifying modification allows the measurement of competitive ligand affinity, permitting straightforward measurement of protein-peptide interactions and inhibitors thereof. Taken as a whole, rhodium(II) conjugates replicate many features of enzymes in an entirely chemical construct.
The Mechanism of Escherichia coli Dethiobiotin Synthetase-the Closure of the ureido Ring of Dethiobiotin involves Formation of a Carbamic-phosphate Mixed Anhydride
Baxter, Robert L.,Baxter, Helen C.
, p. 759 - 760 (1994)
The final intermediate in the enzymatic synthesis of the ureido ring of D-dethiobiotin 1 from (7R,8S)-7,8-diaminononanoate 2 catalysed by E. coli dethiobiotin sunthetase is the phosphoric acid anhydride 4 of the carbamate 3.
-
Kuzuhara,H. et al.
, p. 1185 - 1188 (1970)
-
A Vinylogous Photocleavage Strategy Allows Direct Photocaging of Backbone Amide Structure
Mangubat-Medina, Alicia E.,Martin, Samuel C.,Hanaya, Kengo,Ball, Zachary T.
supporting information, p. 8401 - 8404 (2018/06/29)
Side-chain modifications that respond to external stimuli provide a convenient approach to control macromolecular structure and function. Responsive modification of backbone amide structure represents a direct and powerful alternative to impact folding and function. Here, we describe a new photocaging method using histidine-directed backbone modification to selectively modify peptides and proteins at the amide N-H bond. A new vinylogous photocleavage method allows photorelease of the backbone modification and, with it, restoration of function.
The design and synthesis of inhibitors of dethiobiotin synthetase as potential herbicides
Rendina,Taylor,Gibson,Lorimer,Rayner,Lockett,Kranis,Wexler,Marcovici-Mizrahi,Nudelman,Nudelman,Marsilii,Chi,Wawrzak,Calabrese,Huang,Jia,Schneider,Lindqvist,Yang
, p. 236 - 247 (2007/10/03)
Dethiobiotin synthetase (DTBS; E.C. 6.6.6.6), the penultimate enzyme in the biosynthesis of the essential vitamin biotin, is a new potential target for novel herbicides. Inhibitors were designed based on mechanistic and structural information. The in-vitro activities of these potential inhibitors versus the bacterial enzyme are reported here. Mimics of 7,8- diaminopelargonic acid (DAPA) or the DAPA carbamate reaction intermediate were substrates or partial substrates for the enzyme. Synergistic binding with ATP was noted with compounds which contained an amino functionality. NMR studies and X-ray structures confirmed that the inhibitors could be phosphorylated by the enzyme. Several series of potential inhibitors were designed to take advantage of this partial substrate activity by generating potentially more tightly bound phosphorylated inhibitors in situ. Structure- activity relationships for these series based on both substrate and inhibitory activity are described herein. An X-ray structure for one of these inhibitors is also discussed. Although considerable potential for inhibitors of this type was demonstrated, none of the compounds reported showed sufficient herbicidal activity to be a commercial proposition.
