Unsaturated Glucuronyl Hydrolase of Bacillus sp. GL1: Novel Enzyme Prerequisite for Metabolism of Unsaturated Oligosaccharides Produced by Polysaccharide Lyases

Hashimoto, Wataru; Kobayashi, Eizaburo; Nankai, Hirokazu; Sato, Nobuyuki; Miya, Toyofumi; Kawai, Shigeyuki; Murata, Kousaku

doi:10.1006/abbi.1999.1305

Cited by 41 publications

(52 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…GL1 is a monomeric enzyme with a molecular mass of about 43 kDa (377 amino acid residues) (9). A UGL crystal (0.1 ϫ 0.1 ϫ 0.5 mm) was obtained by sitting-drop vapor diffusion as described elsewhere (21).…”

Section: Resultsmentioning

confidence: 99%

“…Enzyme activity was measured by monitoring the decrease in absorbance at 235 nm, corresponding to the loss of the CϭC double bond of the substrate because the pyranose ring of the released ⌬GlcA readily opens so that it is nonenzymatically converted to ␣-keto acid through the loss of the double bond ( Fig. 1d) (7,9). Enzyme concentration was determined by UV spectrophotometry using theoretical molar extinction coefficient ⑀ 280 ϭ 99,570 (M Ϫ1 cm Ϫ1 ).…”

Section: Methodsmentioning

confidence: 99%

“…Unsaturated glucuronyl hydrolase (UGL) catalyzes the hydrolysis of unsaturated disaccharides to an amino sugar and an unsaturated GlcA (⌬GlcA), which is nonenzymatically converted immediately to ␣-keto acid ( Fig. 1) (9). The enzyme is thus thought to be another virulent factor responsible for the complete degradation of glycosaminoglycans.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å Resolution

Itoh

Akao

Hashimoto

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Unsaturated glucuronyl hydrolase (UGL) is a novel glycosaminoglycan hydrolase that releases unsaturated D-glucuronic acid from oligosaccharides produced by polysaccharide lyases. The x-ray crystallographic structure of UGL from Bacillus sp. GL1 was first determined by multiple isomorphous replacement (mir) and refined at 1.8 Å resolution with a final R-factor of 16.8% for 25 to 1.8 Å resolution data. The refined UGL structure consists of 377 amino acid residues and 478 water molecules, four glycine molecules, two dithiothreitol (DTT) molecules, and one 2-methyl-2,4-pentanediol (MPD) molecule. UGL includes an ␣ 6 /␣ 6 -barrel, whose structure is found in the six-hairpin enzyme superfamily of an ␣/␣-toroidal fold. One side of the UGL ␣ 6 /␣ 6 -barrel structure consists of long loops containing three short ␤-sheets and contributes to the formation of a deep pocket. One glycine molecule and two DTT molecules surrounded by highly conserved amino acid residues in UGLs were found in the pocket, suggesting that catalytic and substrate-binding sites are located in this pocket. The overall UGL structure, with the exception of some loops, very much resembled that of the Bacillus subtilis hypothetical protein Yter, whose function is unknown and which exhibits little amino acid sequence identity with UGL. In the active pocket, residues possibly involved in substrate recognition and catalysis by UGL are conserved in UGLs and Yter. The most likely candidate catalytic residues for glycosyl hydrolysis are Asp 88 and Asp 149 . This was supported by site-directed mutagenesis studies in Asp 88 and Asp 149 .

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å Resolution

Itoh

Akao

Hashimoto

et al. 2004

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

show abstract

“…We found two novel hydrolases, unsaturated glucuronyl hydrolase (UGL) in Bacillus sp. GL1 74,75) and unsaturated galacturonyl hydrolase (UGH) in B. subtilis. 58,76) These enzymes show an ability to hydrolyze host-cell surface matrices, including unsaturated oligosaccharides formed from mammalian glycosaminoglycans, such as chondroitin, hyaluronan, heparin, and plant cell-wall pectin and rhamnogalacturonan, and are thought to be another virulence factor facilitating invasion by pathogenic bacteria of mammalian and plant cells in cooperation with polysaccharide lyases.…”

Section: Alginate Biofilms and Bacterial Infectionmentioning

confidence: 99%

Superchannel of Bacteria: Biological Significance and New Horizons

Murata

Kawai

Mikami

et al. 2008

Bioscience, Biotechnology, and Biochemistry

Self Cite

View full text Add to dashboard Cite

“…We have identified unsaturated glucuronyl hydrolase (UGL), which is essential for degrading unsaturated disaccharides to constituent monosaccharides (i.e. unsaturated uronic acids and amino sugars) in bacteria, including streptococci (8,9), and found that a genome segment termed the UGL genetic cluster is responsible for the depolymerization, import, and degradation of glycosaminoglycans in streptococci, such as Streptococcus agalactiae, Streptococcus pneumoniae, and Streptococcus pyogenes (10) (see Fig. 2A).…”

mentioning

confidence: 99%

Metabolic Fate of Unsaturated Glucuronic/Iduronic Acids from Glycosaminoglycans

Maruyama¹,

Oiki²,

Takase³

et al. 2015

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background: Some streptococci target host extracellular matrix glycosaminoglycans for infection. Results: The streptococcal metabolic pathway of glycosaminoglycan-derived unsaturated uronates was identified. The crystal structures of its isomerase and dehydrogenase were determined. Conclusion: Streptococci include an assembled genetic cluster for depolymerization, import, degradation, and metabolism of glycosaminoglycans. Significance: This study contributes to understanding of the streptococcal degradation/metabolism mechanism of glycosaminoglycans.

show abstract

Unsaturated Glucuronyl Hydrolase of Bacillus sp. GL1: Novel Enzyme Prerequisite for Metabolism of Unsaturated Oligosaccharides Produced by Polysaccharide Lyases

Cited by 41 publications

References 19 publications

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å Resolution

Crystal Structure of Unsaturated Glucuronyl Hydrolase, Responsible for the Degradation of Glycosaminoglycan, from Bacillus sp. GL1 at 1.8 Å Resolution

Superchannel of Bacteria: Biological Significance and New Horizons

Metabolic Fate of Unsaturated Glucuronic/Iduronic Acids from Glycosaminoglycans

Contact Info

Product

Resources

About