Asset Details
Do you wish to reserve the book?
Structural and biochemical characterisation of a novel alginate lyase from Paenibacillus sp. str. FPU-7
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?
Structural and biochemical characterisation of a novel alginate lyase from Paenibacillus sp. str. FPU-7
Do you wish to request the book?
Structural and biochemical characterisation of a novel alginate lyase from Paenibacillus sp. str. FPU-7
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
Structural and biochemical characterisation of a novel alginate lyase from Paenibacillus sp. str. FPU-7
2019
Overview
A novel alginate lyase, PsAly, with a molecular mass of 33 kDa and whose amino acid sequence shares no significant similarity to other known proteins, was biochemically and structurally characterised from
Paenibacillus
sp. str. FPU-7. The maximum PsAly activity was obtained at 65 °C, with an optimum pH of pH 7–7.5. The activity was enhanced by divalent cations, such as Mg
2+
, Mn
2+
, or Co
2+
, and inhibited by a metal chelator, ethylenediaminetetraacetic acid. The reaction products indicated that PsAly is an endolytic enzyme with a preference for polymannuronate. Herein, we report a detailed crystal structure of PsAly at a resolution of 0.89 Å, which possesses a β-helix fold that creates a long cleft. The catalytic site was different from that of other polysaccharide lyases. Site-directed mutational analysis of conserved residues predicted Tyr184 and Lys221 as catalytic residues, abstracting from the C5 proton and providing a proton to the glycoside bond, respectively. One cation was found to bind to the bottom of the cleft and neutralise the carboxy group of the substrate, decreasing the p
K
a
of the C5 proton to promote catalysis. Our study provides an insight into the structural basis for the catalysis of alginate lyases and β-helix polysaccharide lyases.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Cations
/ Cobalt
/ Escherichia coli - metabolism
/ Genetic Vectors - metabolism
/ Humanities and Social Sciences
/ Kinetics
/ Molecular Docking Simulation
/ Polysaccharide-Lyases - chemistry
/ Polysaccharide-Lyases - genetics
/ Polysaccharide-Lyases - metabolism
/ Protein Conformation, alpha-Helical
/ Protein Conformation, beta-Strand
/ Protein Interaction Domains and Motifs
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Science
