Asset Details
Do you wish to reserve the book?
Bifidobacterial GH146 -l-arabinofuranosidase for the removal of 1,3-l-arabinofuranosides on plant glycans
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?
Bifidobacterial GH146 -l-arabinofuranosidase for the removal of 1,3-l-arabinofuranosides on plant glycans
Do you wish to request the book?
Bifidobacterial GH146 -l-arabinofuranosidase for the removal of 1,3-l-arabinofuranosides on plant glycans
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
Bifidobacterial GH146 -l-arabinofuranosidase for the removal of 1,3-l-arabinofuranosides on plant glycans
2024
Overview
l-Arabinofuranosides with -linkages are present in several plant molecules, such as arabinogalactan proteins (AGPs), extensin, arabinan, and rhamnogalacturonan-II. We previously characterized a -l-arabinofuranosidase from Bifidobacterium longum subsp. longum JCM 1217, Bll1HypBA1, which was found to belong to the glycoside hydrolase (GH) family 127. This strain encodes two GH127 genes and two GH146 genes. In the present study, we characterized a GH146 -l-arabinofuranosidase, Bll3HypBA1 (BLLJ₁848), which was found to constitute a gene cluster with AGP-degrading enzymes. This recombinant enzyme degraded AGPs and arabinan, which contain Araf-1,3-Araf structures. In addition, the recombinant enzyme hydrolyzed oligosaccharides containing Araf-1,3-Araf structures but not those containing Araf-1,2-Araf and Araf-1,5-Araf structures. The crystal structures of Bll3HypBA1 were determined at resolutions up to 1.7 Å. The monomeric structure of Bll3HypBA1 comprised a catalytic ([alpha]/[alpha]).sub.6 barrel and two -sandwich domains. A hairpin structure with two -strands was observed in Bll3HypBA1, to extend from a -sandwich domain and partially cover the active site. The active site contains a Zn.sup.2+ ion coordinated by Cys.sub.3-Glu and exhibits structural conservation of the GH127 cysteine glycosidase Bll1HypBA1. This is the first study to report on a 1,3-specific -l-arabinofuranosidase.
Publisher
Springer
We currently cannot retrieve any items related to this title. Kindly check back at a later time.