Asset Details
Do you wish to reserve the book?
First bacterial chalcone isomerase isolated from Eubacterium ramulus
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
First bacterial chalcone isomerase isolated from Eubacterium ramulus
Do you wish to request the book?
First bacterial chalcone isomerase isolated from Eubacterium ramulus
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
First bacterial chalcone isomerase isolated from Eubacterium ramulus
2004
Overview
The human fecal anaerobe Eubacterium ramulus is capable of degrading various flavonoids, including the flavone naringenin. The first step in the proposed degradation pathway is the isomerization of naringenin to the corresponding chalcone. Cell-free extracts of E. ramulus displayed chalcone isomerase activity. The enzyme from E. ramulus was purified to homogeneity. Its apparent molecular mass was estimated to be 136 and 129 kDa according to gel filtration and native polyacrylamide gel electrophoresis, respectively. Chalcone isomerase is composed of one type of subunit of 30 kDa. The purified enzyme catalyzed the isomerization of naringenin chalcone, isoliquiritigenin, and butein, three chalcones that differ in their hydroxylation pattern. N-bromosuccinimide, but also naringenin and phloretin, inhibited the purified enzyme considerably. This is the first report on a bacterial chalcone isomerase. The physiological function of the purified enzyme is unclear, but an involvement in the conversion of the flavanone naringenin to the chalcone is proposed.
Publisher
Springer,Springer Nature B.V
Subject
/ analysis
/ Bacteria
/ Biological and medical sciences
/ Bromosuccinimide - pharmacology
/ chalcone
/ Chalcone - analogs & derivatives
/ Electrophoresis, Polyacrylamide Gel
/ Enzyme Inhibitors - pharmacology
/ Enzymes
/ Fundamental and applied biological sciences. Psychology
/ humans
/ Intramolecular Lyases - chemistry
/ Intramolecular Lyases - isolation & purification
/ Intramolecular Lyases - metabolism
