Asset Details
Do you wish to reserve the book?
L-rhamnose isomerase: a crucial enzyme for rhamnose catabolism and conversion of rare sugars
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?
L-rhamnose isomerase: a crucial enzyme for rhamnose catabolism and conversion of rare sugars
Do you wish to request the book?
L-rhamnose isomerase: a crucial enzyme for rhamnose catabolism and conversion of rare sugars
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
L-rhamnose isomerase: a crucial enzyme for rhamnose catabolism and conversion of rare sugars
2024
Overview
L-rhamnose isomerase (L-RhI) plays a key role in the microbial L-rhamnose metabolism by catalyzing the reversible isomerization of L-rhamnose to L-rhamnulose. Additionally, the enzyme exhibits activity on various other aldoses and ketoses, and its broad substrate specificity has attracted attention for its potential application in the production of rare sugars; however, improvement of the enzyme properties is desirable, such as thermal stability, enzymatic activity, and a pH optimum suitable for industrial usage. This review summarizes our current insights into L-RhIs with respect to their substrate recognition mechanism and their relationship with D-xylose isomerase (D-XI) based on structural and phylogenetic analyses. These two enzymes are inherently different, but recognize distinctly different substrates, and share common features that may be phylogenetically related. For example, they both have a flexible loop region that is involved in shaping active sites, and this region may also be responsible for various enzymatic properties of L-RhIs, such as substrate specificity and thermal stability.
Key points
•
L-RhIs share structural features with D-XI.
•
There are two types of L-RhIs: E. coli L-RhI-type and D-XI-type.
•
Flexible loop regions are involved in the specific enzyme properties.
Publisher
Springer Berlin Heidelberg,Springer,Springer Nature B.V
Subject
Aldose-Ketose Isomerases - chemistry
/ Aldose-Ketose Isomerases - genetics
/ Aldose-Ketose Isomerases - metabolism
/ aldoses
/ Biomedical and Life Sciences
/ E coli
/ Enzymes
/ Escherichia coli - enzymology
/ Escherichia coli - metabolism
/ ketoses
/ Microbial Genetics and Genomics
/ rhamnose
/ Sugar
/ xylose
