ArticleActa crystallographica. Section F, Structural biology communications2017
3,6-Anhydro-L-galactonate cycloisomerase from Vibrio sp. strain EJY3: crystallization and X-ray crystallographic analysis.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Agaro-Oligosaccharide Supplementation Alters the Gut Microbiota, Revealing Potential Agaro-Oligosaccharide-Utilizing Taxa in Healthy Japanese Adults.Biomedicines · 2026Article
- Identification of the enantiomeric nature of 2-keto-3-deoxy-galactonate in the catabolic pathway of 3,6-anhydro-L-galactose.Applied microbiology and biotechnology · 2023Article
- NADPJournal of microbiology and biotechnology · 2021Article
- Application-Oriented Marine Isomerases in Biocatalysis.Marine drugs · 2020Review
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Authors and funding
5 authors.
Funding
Abstract
3,6-Anhydro-L-galactonate cycloisomerase (ACI), which is found in the marine bacterium Vibrio sp. strain EJY3, converts 3,6-anhydro-L-galactonate into 2-keto-3-deoxygalactonate. ACI is a key enzyme in the metabolic pathway of 3,6-anhydro-L-galactose (AHG). Study of AHG metabolism is important for the efficient fermentation of agar and biofuel production, because AHG is a sugar that is non-fermentable by commercial microorganisms. The aci gene from Vibrio sp. strain EJY3 was cloned, and the recombinant protein was overexpressed and crystallized in order to determine the structure and understand the function of the protein. The crystals diffracted to 2.2 Å resolution and belonged to space group P4
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