Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Cyntia M. Palacio"'
Autor:
Henriëtte J. Rozeboom, Marleen Otzen, Elisa Lanfranchi, Dick B. Janssen, Cyntia M. Palacio, Qinglong Meng
Publikováno v:
The FEBS Journal, 286(20):14950, 4086-4102. NLM (Medline)
The biodegradation of the nylon-6 precursor caprolactam by a strain of Pseudomonas jessenii proceeds via ATP-dependent hydrolytic ring-opening to 6-aminohexanoate. This non-natural ω-amino acid is converted to 6-oxohexanoic acid by an aminotransfera
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::848a636fac0db7b3c5e966494765ad1f
https://research.rug.nl/en/publications/5a47474f-4365-4a3b-bb61-238713f699cd
https://research.rug.nl/en/publications/5a47474f-4365-4a3b-bb61-238713f699cd
Autor:
Bian Wu, Rohana Abu, Cyntia M. Palacio, Sebastian Bartsch, Ciprian G. Crismaru, Vaidotas Navickas, Kai Baldenius, Dick B. Janssen, John M. Woodley, Klaus Ditrich, Michael Breuer
Publikováno v:
Biotechnology and Bioengineering. 113:1853-1861
We constructed an enzymatic network composed of three different enzymes for the synthesis of valuable ether amines. The enzymatic reactions are interconnected to catalyze the oxidation and subsequent transamination of the substrate and to provide cof
Publikováno v:
Applied Microbiology and Biotechnology
Applied Microbiology and Biotechnology, 15, 6699-6711. SPRINGER
Applied Microbiology and Biotechnology, 15, 6699-6711. SPRINGER
Some bacterial cultures are capable of growth on caprolactam as sole carbon and nitrogen source, but the enzymes of the catabolic pathway have not been described. We isolated a caprolactam-degrading strain of Pseudomonas jessenii from soil and identi
Autor:
Cyntia M, Palacio, Ciprian G, Crismaru, Sebastian, Bartsch, Vaidotas, Navickas, Klaus, Ditrich, Michael, Breuer, Rohana, Abu, John M, Woodley, Kai, Baldenius, Bian, Wu, Dick B, Janssen
Publikováno v:
Biotechnology and bioengineering. 113(9)
We constructed an enzymatic network composed of three different enzymes for the synthesis of valuable ether amines. The enzymatic reactions are interconnected to catalyze the oxidation and subsequent transamination of the substrate and to provide cof
N-Monoacetylated derivatives of ribo- (adenosine, guanosine) and 2′-deoxyribonucleosides (2′-deoxyadenosine and 2′-deoxyguanosine), useful as oligonucleotide building blocks, were obtained in 88–100% by enzymatic chemoselective hydrolysis of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dab49279a1c29f204abbf6d6c823bec7
http://www.sciencedirect.com/science/article/pii/S0168165613001399
http://www.sciencedirect.com/science/article/pii/S0168165613001399
Autor:
Nikolas Capra, Henriëtte J. Rozeboom, Elisa Lanfranchi, Qinglong Meng, Hein J. Wijma, Cyntia M. Palacio, Luc Z. Van Schie, Marleen Otzen, Dick B. Janssen, Andy-Mark W. H. Thunnissen
Publikováno v:
ACS Catalysis, 10(5), 2915-2928. AMER CHEMICAL SOC
ACS Catalysis
ACS Catalysis
Transaminases are attractive catalysts for the production of enantiopure amines. However, the poor stability of these enzymes often limits their application in biocatalysis. Here, we used a framework for enzyme stability engineering by computational