3.2.1.179: gellan tetrasaccharide unsaturated glucuronosyl hydrolase
This is an abbreviated version!
For detailed information about gellan tetrasaccharide unsaturated glucuronosyl hydrolase, go to the full flat file.
Word Map on EC 3.2.1.179
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3.2.1.179
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disaccharide
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polysaccharide
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glycosaminoglycans
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lyases
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chondroitin
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glycoside
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streptococcal
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glucuronic
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depolymerization
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agalactiae
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oligosaccharides
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matrices
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hyaluronate
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hydrolases
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phosphotransferase
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xanthan
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nonreducing
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heteropolysaccharide
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perfringens
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rhamnogalacturonan
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galacturonic
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n-acetyl-d-galactosamine
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pyogenes
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vinyl
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beta-d-glucosidase
- 3.2.1.179
- disaccharide
- polysaccharide
- glycosaminoglycans
- lyases
- chondroitin
- glycoside
- streptococcal
-
glucuronic
-
depolymerization
- agalactiae
- oligosaccharides
-
matrices
- hyaluronate
- hydrolases
-
phosphotransferase
- xanthan
-
nonreducing
- heteropolysaccharide
- perfringens
- rhamnogalacturonan
-
galacturonic
- n-acetyl-d-galactosamine
- pyogenes
-
vinyl
- beta-d-glucosidase
Reaction
Synonyms
CaUGL, CA_C0359, More, SagUGL, UGL, unsaturated glucuronyl hydrolase
ECTree
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Substrates Products
Substrates Products on EC 3.2.1.179 - gellan tetrasaccharide unsaturated glucuronosyl hydrolase
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REACTION DIAGRAM
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-N-acetylgalactosamine
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc6S
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-N-acetylgalactosamine-6-O-sulfate
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GlcNAc + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GlcNAc
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116% of the activity with beta-D-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
beta-D-4-deoxy-DELTA4,5-GlcAp2S-(1->3)-beta-D-GalNAc + H2O
? + beta-D-GalNAc
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23.5% of the activity with beta-D-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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-
?
beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp + H2O
5-dehydro-4-deoxy-D-glucuronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
enzyme activity is measured by monitoring the decrease in absorbance at 235 nm, corresponding to the loss of the C=C double bond of the substrate because the pyranose ring of the released DELTAGlcA readily opens so that it is nonenzymatically converted to alpha-keto acid through the loss of the double bond
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-
?
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
the enzyme strongly recognizes DELTA-4,5-GlcA at subsite -1 through the formation of hydrogen bonds and stacking interactions, and prefers N-acetyl-D-galactosamine and glucose rather than N-acetyl-D-glucosamine as a residue accommodated in subsite +1, due to the steric hindrance
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-
?
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
the enzyme strongly recognizes DELTA-4,5-GlcA at subsite -1 through the formation of hydrogen bonds and stacking interactions, and prefers N-acetyl-D-galactosamine and glucose rather than N-acetyl-D-glucosamine as a residue accommodated in subsite +1, due to the steric hindrance
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-
?
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
enzyme activity is measured by monitoring the decrease in absorbance at 235 nm, corresponding to the loss of the C=C double bond of the substrate because the pyranose ring of the released DELTAGlcA readily opens so that it is nonenzymatically converted to alpha-keto acid through the loss of the double bond
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-
?
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc
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114% of the activity with beta-D-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc
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114% of the activity with beta-D-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
-
-
?
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-N-acetylgalactosamine
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-
-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-N-acetylgalactosamine
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-
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?
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc6S
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25.5% of the activity with beta-D-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc6S
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25.5% of the activity with beta-D-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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-
?
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-N-acetylgalactosamine-6-O-sulfate
kcat/Km is 8% of the kcat/KM value for the unsulfated substrate beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
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-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-N-acetylgalactosamine-6-O-sulfate
kcat/Km is 8% of the kcat/KM value for the unsulfated substrate beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
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?
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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degradation of oligosaccharides with unsaturated uronic acid at the nonreducing terminal produced by polysaccharide lyases
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-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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-
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-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
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degradation of oligosaccharides with unsaturated uronic acid at the nonreducing terminal produced by polysaccharide lyases
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-
?
5-dehydro-4-deoxy-D-glucuronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp
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?
beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp + H2O
5-dehydro-4-deoxy-D-glucuronate + beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp
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?
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the enzyme is specific for unsaturated glucuronides and inert to saturated glucuronides. The enzyme fails to liberate nitrophenol from p-nitrophenyl-beta-D-glucuronide. The enzyme prefers unsaturated chondroitin disaccharide without sulfate to those with sulfate
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additional information
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the enzyme is specific for unsaturated glucuronides and inert to saturated glucuronides. The enzyme fails to liberate nitrophenol from p-nitrophenyl-beta-D-glucuronide. The enzyme prefers unsaturated chondroitin disaccharide without sulfate to those with sulfate
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?
additional information
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the degradation of the polygalacturonan (PGA) and rhamnogalacturonan-I (RG-I) backbones of pectin. In both instances the unsaturated GalA may spontaneously open to 4-deoxy-L-threo-5-hexosulose-uronate, reaction pathways, overview. The suggested mechanism for both families, the unsaturated rhamnogalacturonyl hydrolase (EC 3.2.1.172) and the unsaturated glucuronyl hydrolase (EC 3.2.1.179), requires hydration at the C=C bond of the unsaturated sugar, resulting in glycosidic cleavage. Substrate specificity in the GH105 family correlates with the loops surrounding the active site
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additional information
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glycosaminoglycans such as hyaluronan and heparin are depolymerized by polysaccharide lyase and the resulting unsaturated disaccharides are degraded to unsaturated uronic acids and amino sugars by enzyme UG, reaction mechanism of UGL, overview. Gellan gum, xanthan gum, hyaluronan, chondroitin sulfate C, and heparin are used as glucuronate-containing polysaccharides. SagUGL preferentially degrades unsaturated hyaluronan and chondroitin sulfate disaccharides with 1,3-glycosidic bonds
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additional information
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glycosaminoglycans such as hyaluronan and heparin are depolymerized by polysaccharide lyase and the resulting unsaturated disaccharides are degraded to unsaturated uronic acids and amino sugars by enzyme UG, reaction mechanism of UGL, overview. Gellan gum, xanthan gum, hyaluronan, chondroitin sulfate C, and heparin are used as glucuronate-containing polysaccharides. SagUGL preferentially degrades unsaturated hyaluronan and chondroitin sulfate disaccharides with 1,3-glycosidic bonds
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