ArticleBiochemistry2023
Energetics of the Glycosyl Transfer Reactions of Sucrose Phosphorylase.
Article in Biochemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Analysis of the Atypical Temperature Dependence and Conformational Changes During Turnover of a Lactobacillus Chlorogenic Acid Esterase.Biochemistry · 2026Article
- The P134Q Sucrose Phosphorylase: Subtle Changes in the Catalytic Properties Benefit the Production of 2-O-α-Glucosyl Glycerol.Biotechnology and bioengineering · 2025Article
- Development of Sucrose-UtilizingMetabolites · 2025Article
- Keeping the Distance: Activity Control in Solid-Supported Sucrose Phosphorylase by a Rigid α-Helical Linker of Tunable Spacer Length.ACS catalysis · 2024Article
- 2-O-α-D-glucosyl glycerol production by whole-cell biocatalyst of lactobacilli encapsulating sucrose phosphorylase with improved glycerol affinity and conversion rate.Microbial cell factories · 2024Article
Corrections and comments
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Authors and funding
2 authors.
Funding
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Abstract
From its structure and mechanism, sucrose phosphorylase is a specialized glycoside hydrolase that uses phosphate ions instead of water as the nucleophile of the reaction. Unlike the hydrolysis reaction, the phosphate reaction is readily reversible and, here, this has enabled the study of temperature effects on kinetic parameters to map the energetic profile of the complete catalytic process via a covalent glycosyl enzyme intermediate. Enzyme glycosylation from sucrose and α-glucose 1-phosphate (Glc1P) is rate-limiting in the forward (
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