ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009
Crystallization and preliminary X-ray analysis of neoagarobiose hydrolase from Saccharophagus degradans 2-40.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. 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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4 citing papers in PubMed, 23 citations in OpenAlex.
- Dual Agarolytic Pathways in a Marine Bacterium,Applied and environmental microbiology · 2020Article
- Characterization of a Novel α-Neoagarobiose Hydrolase Capable of Preparation of Medium- and Long-Chain Agarooligosaccharides.Frontiers in bioengineering and biotechnology · 2019Article
- Analysis of keystone enzyme in Agar hydrolysis provides insight into the degradation (of a polysaccharide from) red seaweeds.The Journal of biological chemistry · 2012Article
- Carbohydrase systems of Saccharophagus degradans degrading marine complex polysaccharides.Marine drugs · 2011Review
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
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Abstract
Many agarolytic bacteria degrade agar polysaccharide into the disaccharide unit neoagarobiose [O-3,6-anhydro-alpha-L-galactopyranosyl-(1-->3)-D-galactose] using various beta-agarases. Neoagarobiose hydrolase is an enzyme that acts on the alpha-1,3 linkage in neoagarobiose to yield D-galactose and 3,6-anhydro-L-galactose. This activity is essential in both the metabolism of agar by agarolytic bacteria and the production of fermentable sugars from agar biomass for bioenergy production. Neoagarobiose hydrolase from the marine bacterium Saccharophagus degradans 2-40 was overexpressed in Escherichia coli and crystallized in the monoclinic space group C2, with unit-cell parameters a = 129.83, b = 76.81, c = 90.11 A, beta = 101.86 degrees . The crystals diffracted to 1.98 A resolution and possibly contains two molecules in the asymmetric unit.
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