Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Mark S. Payne"'
Autor:
Walter R. P. Novak, Jeffrey N. Agar, Mary Jo Ondrechen, Dagmar Ringe, J. Alejandro D’Aquino, Gregory A. Petsko, N. M. Karabacak, Mark S. Payne, Heather R. Brodkin, Amy C. Milne, Ilana G. Goldberg
Publikováno v:
Biochemistry. 50:4923-4935
Active sites may be regarded as layers of residues, whereby the residues that interact directly with substrate also interact with residues in a second shell and these in turn interact with residues in a third shell. These residues in the second and t
Publikováno v:
British Journal of Medical and Surgical Urology. 3:52-58
Introduction: Gelatine is a setting agent used by the food and drug industries whose consumption is forbidden by religious and other faith groups. Gelatine-containing drugs are found in most of the drug classifications in Section 7.4 of the British N
Autor:
Lawrence J. Mersinger, Kelly L. Petrillo, Mark S. Payne, Frederick B. Cooling, John E. Gavagan, Arie Ben-Bassat, Eugenia C. Hann, Shijun Wu, Robert DiCosimo
Publikováno v:
Advanced Synthesis & Catalysis. 347:1125-1131
A thermally-stable nitrile hydratase produced by Comamonas testosteroni 5-MGAM-4D has been expressed in Escherichia coli, and the alginate-immobilized transformant evaluated as catalyst for the conversion of acrylonitrile to acrylamide. In batch reac
Autor:
Eugenia Costa Hann, Kelly L. Petrillo, Mark S. Payne, John E. Gavagan, Frederick B. Cooling, Robert DiCosimo, Arie Ben-Bassat, Shijun Wu
Publikováno v:
Applied Microbiology and Biotechnology. 67:664-670
The genes encoding a thermally stable and regio-selective nitrile hydratase (NHase) and an amidase from Comamonas testosteroni 5-MGAM-4D have been cloned and sequenced, and active NHase has been over-produced in Escherichia coli. Maximal activity req
Autor:
Amy E. Sigmund, Frederick B. Cooling, Mark S. Payne, Michael G. Bramucci, Susan K. Fager, John E. Gavagan, Robert DiCosimo, Eugenia C. Hann, Sarita Chauhan
Publikováno v:
Tetrahedron. 60:577-581
Acidovorax facilis 72W nitrilase catalyzed the regioselective hydrolysis of (E,Z)-2-methyl-2-butenenitrile, producing only (E)-2-methyl-2-butenoic acid with no detectable conversion of (Z)-2-methyl-2-butenenitrile. (E)-2-Methyl-2-butenoic acid, produ
Autor:
Frederick B. Cooling, Amy E. Sigmund, Arie Ben-Bassat, John E. Gavagan, Eugenia C. Hann, Sarita Chauhan, Susan K. Fager, Robert DiCosimo, Mark S. Payne, Susan Marie Hennessey
Publikováno v:
Advanced Synthesis & Catalysis. 345:775-782
Microbial catalysts having a combination of nitrile hydratase and amidase activities had a significantly-higher specific activity for hydrolysis of 3-hydroxyalkanenitriles than microbial nitrilase catalysts. Comamonas testosteroni 22–1, Dietzia sp.
Autor:
Sarita Chauhan, David R. Short, Eugenia Costa Hann, Susan Marie Hennessey, John E. Gavagan, Robert DiCosimo, Amy E. Sigmund, Arie Ben-Bassat, Mark S. Payne, Robert D. Fallon
Publikováno v:
Organic Process Research & Development. 6:492-496
Optimization of microbial cell immobilization, catalyst specific activity, and volumetric productivity were required for scale-up of the nitrilase-catalyzed hydrolysis of 2-methylglutaronitrile to ...
Publikováno v:
DNA and Cell Biology. 17:915-920
Amidases are a class of enzymes which convert amides to acids and have potential value in the development of commercial bioprocesses for the production of useful chemicals. A gene encoding an amidase in Pseudomonas putida 5B has been cloned, sequence
Autor:
John E. Gavagan, Susan K. Fager, Robert DiCosimo, John E. Seip, David Leroy Anton, Mark S. Payne, Dawn S. Clark
Publikováno v:
The Journal of Organic Chemistry. 62:5419-5427
Permeabilized, metabolically-inactive transformants of the methylotrophic yeasts Hansenula polymorpha and Pichia pastoris which contain significant quantities of the enzymes spinach glycolate oxidase ((S)-2-hydroxyacid oxidase, EC 1.1.3.15), Saccharo
Autor:
Ivan M. Turner, Mark S. Payne, Robert D. Fallon, Shijun Wu, Gabriela Tudor, Mark J. Nelson, Barry Stieglitz
Publikováno v:
Biochemistry. 36:5447-5454
Nitrile hydratase from Pseudomonas putida NRRL-18668 has been purified and characterized. The purified enzyme catalyzes the hydration of 2(S)-(4'-chlorophenyl)-3-methylbutyronitrile at least fifty times faster than that of 2(R)-(4'-chlorophenyl)-3-me