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6HPD

The structure of a beta-glucuronidase from glycoside hydrolase family 2

Summary for 6HPD
Entry DOI10.2210/pdb6hpd/pdb
DescriptorBeta-galactosidase (GH2), BROMIDE ION, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordsgh2, glycoside hydrolase, glucuronidase, hydrolase
Biological sourceFormosa agariphila KMM 3901
Total number of polymer chains1
Total formula weight112959.53
Authors
Robb, C.S.,Gerlach, N.,Reisky, L.,Bornshoeru, U.,Hehemann, J.H. (deposition date: 2018-09-20, release date: 2019-07-24, Last modification date: 2024-01-24)
Primary citationReisky, L.,Prechoux, A.,Zuhlke, M.K.,Baumgen, M.,Robb, C.S.,Gerlach, N.,Roret, T.,Stanetty, C.,Larocque, R.,Michel, G.,Song, T.,Markert, S.,Unfried, F.,Mihovilovic, M.D.,Trautwein-Schult, A.,Becher, D.,Schweder, T.,Bornscheuer, U.T.,Hehemann, J.H.
A marine bacterial enzymatic cascade degrades the algal polysaccharide ulvan.
Nat.Chem.Biol., 15:803-812, 2019
Cited by
PubMed Abstract: Marine seaweeds increasingly grow into extensive algal blooms, which are detrimental to coastal ecosystems, tourism and aquaculture. However, algal biomass is also emerging as a sustainable raw material for the bioeconomy. The potential exploitation of algae is hindered by our limited knowledge of the microbial pathways-and hence the distinct biochemical functions of the enzymes involved-that convert algal polysaccharides into oligo- and monosaccharides. Understanding these processes would be essential, however, for applications such as the fermentation of algal biomass into bioethanol or other value-added compounds. Here, we describe the metabolic pathway that enables the marine flavobacterium Formosa agariphila to degrade ulvan, the main cell wall polysaccharide of bloom-forming Ulva species. The pathway involves 12 biochemically characterized carbohydrate-active enzymes, including two polysaccharide lyases, three sulfatases and seven glycoside hydrolases that sequentially break down ulvan into fermentable monosaccharides. This way, the enzymes turn a previously unexploited renewable into a valuable and ecologically sustainable bioresource.
PubMed: 31285597
DOI: 10.1038/s41589-019-0311-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.43 Å)
Structure validation

237992

数据于2025-06-25公开中

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