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pro vyhledávání: '"Elisa M, Woolridge"'
Autor:
Annemarie A. Lee, Esabelle D. Gervasio, Riley O. Hughes, Alexandra A. Maalouf, Samantha A. Musso, Alicia M. Crisalli, Elisa M. Woolridge
Publikováno v:
Applied Biochemistry and Biotechnology. 195:3311-3326
Autor:
Elisa M. Woolridge
Publikováno v:
Catalysts, Vol 4, Iss 1, Pp 1-35 (2014)
The application of enzymes such as laccase and xylanase for the preparation of cellulose from lignocellulosic material is an option for those industries seeking to reduce the use of chlorine-containing bleach agents, thus minimizing the environmental
Externí odkaz:
https://doaj.org/article/8bc93923dc6a4cd1b1e84e36a2ad567f
Publikováno v:
Enzyme and Microbial Technology. 43:149-156
The biomass-processing enzymes laccase and xylanase can each be used to moderately reduce the amount of chlorine dioxide required for bleached pulp production. Although combined enzyme treatment is anticipated to be appealing to biomass-converting in
Autor:
Stephen C. Ransom, John W. Kozarich, Suzanne E. Williams, Patricia C. Babbitt, Elisa M. Woolridge, James A. Landro
Publikováno v:
Biochemistry. 31:9768-9776
The gene (pcaB) for 3-carboxymuconate lactonizing enzyme (CMLE; 3-carboxymuconate cycloisomerase; EC 5.5.1.2) from Pseudomonas putida has been cloned into pMG27NS, a temperature-sensitive expression vector, and expressed in Escherichia coli N4830. Th
Autor:
Gregory A. Petsko, John W. Kozarich, Yi Wang, Jian Yang, Elisa M. Woolridge, Vandana Arora, Dagmar Ringe
Publikováno v:
Biochemistry. 43(32)
3-Carboxy-cis,cis-muconate lactonizing enzymes (CMLEs), the key enzymes in the protocatechuate branch of the beta-ketoadipate pathway in microorganisms, catalyze the conversion of 3-carboxy-cis,cis-muconate to muconolactones. We have determined the c
Autor:
Elisa M. Woolridge, Margaret M. McGowen, Gregory A. Petsko, Ilme Schlichting, Dagmar Ringe, John W. Kozarich, Miriam S. Hasson
Publikováno v:
Acta Crystallographica. Section D: Biological Crystallography (Copenhagen)
Two crystal forms of 3-carboxy-cis,cis-muconate lactonizing enzyme from Pseudomonas putida have been characterized. Form A is in space group P6, with unit-cell dimensions a = b = 232, c = 79 A, alpha = beta = 90, gamma = 120 degrees. Form B is orthor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::741b00c2f5d09caeb72c9a0bc5ce6eb7
https://www.ncbi.nlm.nih.gov/pubmed/15299946
https://www.ncbi.nlm.nih.gov/pubmed/15299946
Autor:
Elisa M. Woolridge, Steven E. Rokita
Publikováno v:
Archives of biochemistry and biophysics. 286(2)
6-(Difluoromethyl)indole has been characterized and developed as a probe for the turnover of indole by the bifunctional enzyme, tryptophan synthase (alpha 2 beta 2). The neutral form of the indolyl species undergoes a slow and spontaneous hydrolysis
Autor:
Elisa M. Woolridge, Steven E. Rokita
Publikováno v:
Biochemistry. 30(7)
A substrate analogue, 6-(difluoromethyl)tryptophan, was developed and characterized for mechanistic investigation of tryptophanase. The utility of this derivative was based on its ability to partition between fluoride elimination and carbon-carbon bo
ChemInform Abstract: Synthesis and Reactivity of 6-(Fluoromethyl)indole and 6-(Difluoromethyl)indole
Autor:
Steven E. Rokita, Elisa M. Woolridge
Publikováno v:
ChemInform. 21
The N-1 BOC protected precursors of 6-(fluoromethyl)indole and 6-(difluoromethyl)indole were prepared and deprotected via flash vacuum thermolysis. The stability of these newly prepared, unprotected indole derivatives has been characterized and compa
Autor:
Elisa M. Woolridge, Steven E. Rokita
Publikováno v:
Tetrahedron Letters. 30:6117-6120
The N-1 BOC protected precursors of 6-(fluoromethyl)indole and 6-(difluoromethyl)indole were prepared and deprotected via flash vacuum thermolysis. The stability of these newly prepared, unprotected indole derivatives has been characterized and compa