Search

Your search keyword '"Fink, Michael J."' showing total 9 results
Start Over Author "Fink, Michael J." Publisher american chemical society (acs)
9 results on '"Fink, Michael J."'

2. Mutations Increasing Cofactor Affinity, Improve Stability and Activity of a Baeyer–Villiger Monooxygenase

Author

Mansouri, Hamid R., primary, Gracia Carmona, Oriol, additional, Jodlbauer, Julia, additional, Schweiger, Lorenz, additional, Fink, Michael J., additional, Breslmayr, Erik, additional, Laurent, Christophe, additional, Feroz, Saima, additional, P. Goncalves, Leticia C., additional, Rial, Daniela V., additional, Mihovilovic, Marko D., additional, Bommarius, Andreas S., additional, Ludwig, Roland, additional, Oostenbrink, Chris, additional, and Rudroff, Florian, additional

Published
2022
Full Text
View/download PDF

4. A Click-Flipped Enzyme Substrate Boosts the Performance of the Diagnostic Screening for Hunter Syndrome

Author

Schwarz, Markus, Skrinjar, Philipp, Fink, Michael J., Kronister, Stefan, Mechtler, Thomas, Koukos, Panagiotis I., Bonvin, Alexandre M. J. J., Kasper, David C., Mikula, Hannes, Sub NMR Spectroscopy, NMR Spectroscopy, Sub NMR Spectroscopy, and NMR Spectroscopy

Subjects
chemistry.chemical_classification, 010405 organic chemistry, Triazole, Substrate (chemistry), Hunter syndrome, General Chemistry, 010402 general chemistry, medicine.disease, 01 natural sciences, Early initiation, 0104 chemical sciences, chemistry.chemical_compound, Chemistry, Enzyme, Pyranose, chemistry, Biochemistry, Flip, medicine, Diagnostic screening
Abstract

We report on the unexpected finding that click modification of iduronyl azides results in a conformational flip of the pyranose ring, which led to the development of a new strategy for the design of superior enzyme substrates for the diagnostic assaying of iduronate-2-sulfatase (I2S), a lysosomal enzyme related to Hunter syndrome. Synthetic substrates are essential in testing newborns for metabolic disorders to enable early initiation of therapy. Our click-flipped iduronyl triazole showed a remarkably better performance with I2S than commonly used O-iduronates. We found that both O- and triazole-linked substrates are accepted by the enzyme, irrespective of their different conformations, but only the O-linked product inhibits the activity of I2S. Thus, in the long reaction times required for clinical assays, the triazole substrate substantially outperforms the O-iduronate. Applying our click-flipped substrate to assay I2S in dried blood spots sampled from affected patients and random newborns significantly increased the confidence in discriminating between these groups, clearly indicating the potential of the click-flip strategy to control the biomolecular function of carbohydrates., Click-triggered flip of the conformation of a sulfated iduronyl azide afforded a superior enzyme substrate to screen for Hunter syndrome.

Published
2020

7. A Common Mechanism Links Activities of Butyrate in the Colon

Author

Verma, Mohit S., primary, Fink, Michael J., additional, Salmon, Gabriel L., additional, Fornelos, Nadine, additional, Ohara, Takahiro E., additional, Ryu, Stacy H., additional, Vlamakis, Hera, additional, Xavier, Ramnik J., additional, Stappenbeck, Thaddeus S., additional, and Whitesides, George M., additional

Published
2018
Full Text
View/download PDF

9. A common mechanism links activities of butyrate in the colon

Author

S. Verma, Mohit, primary, Fink, Michael J., primary, Salmon, Gabriel L, primary, Fornelos, Nadine, primary, Ohara, Takahiro E., primary, Ryu, Stacy S., primary, Vlamakis, Hera, primary, Xavier, Ramnik J., primary, S. Stappenbeck, Thaddeus, primary, and Whitesides, George M., primary

Published
2017
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results