Exploring Multifunctional Residues of Ribose-5-phosphate Isomerase B from Ochrobactrum sp. CSL1 Enhancing Isomerization of d-Allose
Author:
Affiliation:
1. School of Chemistry, Biology, and Material Engineering, Suzhou University of Science and Technology, Suzhou 215009, P.R. China
2. Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University, Fujian 350116, P.R. China
Funder
Jiangsu Provincial Department of Education
Natural Science Foundation of Fujian Province
National Natural Science Foundation of China
Publisher
American Chemical Society (ACS)
Subject
General Agricultural and Biological Sciences,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jafc.9b07855
Reference37 articles.
1. Structure of Escherichia coli Ribose-5-Phosphate Isomerase
2. The return of metabolism: biochemistry and physiology of the pentose phosphate pathway
3. Ribose catabolism of Escherichia coli: characterization of the rpiB gene encoding ribose phosphate isomerase B and of the rpiR gene, which is involved in regulation of rpiB expression
4. Two Ribose-5-Phosphate Isomerases from Escherichia coli K12: Partial Characterisation of the Enzymes and Consideration of Their Possible Physiological Roles
5. Erythritol feeds the pentose phosphate pathway via three new isomerases leading to D-erythrose-4-phosphate inBrucella
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