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Information on EC 3.2.1.179 - gellan tetrasaccharide unsaturated glucuronosyl hydrolase
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EC Tree
3.2.1.179 gellan tetrasaccharide unsaturated glucuronosyl hydrolaseIUBMB Comments
The enzyme releases 4-deoxy-4(5)-unsaturated D-glucuronic acid from oligosaccharides produced by polysaccharide lyases, e.g. the tetrasaccharide beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp produced by EC 4.2.2.25, gellan lyase. The enzyme can also hydrolyse unsaturated chondroitin and hyaluronate disaccharides (beta-D-4-deoxy-Delta4-GlcAp-(1->3)-D-GalNAc, beta-D-4-deoxy-Delta4-GlcAp-(1->3)-D-GalNAc6S, beta-D-4-deoxy-Delta4-GlcAp2S-(1->3)-D-GalNAc, beta-D-4-deoxy-Delta4-GlcAp-(1->3)-D-GlcNAc), preferring the unsulfated disaccharides to the sulfated disaccharides.
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Word Map
- 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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
unsaturated glucuronyl hydrolase, sagugl, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
UGL
unsaturated glucuronyl hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
-
-
-
-
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
the enzyme triggers a hydration reaction acting on the C-C double bond between the C-4 and C-5 positions of the unsaturated uronic acid residue in GAG disaccharide using the catalytic Asp residue (Asp-II) as a general acid and base catalyst to protonate the C-4 atom of unsaturated uronic acid residue and to deprotonate the water molecule. The deprotonated water molecule attacks the C-5 atom of the unsaturated uronic acid residue to yield unstable hemiketal, followed by its spontaneous conversion to 4-deoxy-L-threo-5-hexosulose-uronic acid and an amino sugar via hemiacetal formation and cleavage of the glycoside bond
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SYSTEMATIC NAME
IUBMB Comments
beta-D-4-deoxy-DELTA4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp beta-D-4-deoxy-DELTA4-GlcAp hydrolase
The enzyme releases 4-deoxy-4(5)-unsaturated D-glucuronic acid from oligosaccharides produced by polysaccharide lyases, e.g. the tetrasaccharide beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-D-Glcp produced by EC 4.2.2.25, gellan lyase. The enzyme can also hydrolyse unsaturated chondroitin and hyaluronate disaccharides (beta-D-4-deoxy-Delta4-GlcAp-(1->3)-D-GalNAc, beta-D-4-deoxy-Delta4-GlcAp-(1->3)-D-GalNAc6S, beta-D-4-deoxy-Delta4-GlcAp2S-(1->3)-D-GalNAc, beta-D-4-deoxy-Delta4-GlcAp-(1->3)-D-GlcNAc), preferring the unsulfated disaccharides to the sulfated disaccharides.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
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
-
-
?
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
-
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
-
-
?
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
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc
-
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
-
-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc
-
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
-
-
?
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-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
-
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
-
-
?
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S + H2O
4-deoxy-L-threo-5-hexosulose-uronate + beta-D-GalNAc6S
-
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
-
-
?
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
-
-
?
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
-
-
?
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-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
-
degradation of oligosaccharides with unsaturated uronic acid at the nonreducing terminal produced by polysaccharide lyases
-
-
?
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-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
-
degradation of oligosaccharides with unsaturated uronic acid at the nonreducing terminal produced by polysaccharide lyases
-
-
?
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
-
-
-
?
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
-
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-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
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
-
degradation of oligosaccharides with unsaturated uronic acid at the nonreducing terminal produced by polysaccharide lyases
-
-
?
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
-
degradation of oligosaccharides with unsaturated uronic acid at the nonreducing terminal produced by polysaccharide lyases
-
-
?
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
-
-
-
?
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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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
poor effects by gellan, xanthan, and heparin
-
additional information
-
poor effects by gellan, xanthan, and heparin
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.06 - 0.2
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
0.06
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, mutant enzyme E149N
0.09
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, wild-type enzyme
0.2
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, mutant enzyme E88N
0.381
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, wild-type enzyme
0.504
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme G342S
0.566
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme K370I
0.861
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme H339S
2.2
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme K370I
7
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme G342S
7.19
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme H339S
18.6
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, wild-type enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00057 - 7.3
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
0.00057
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, mutant enzyme E88N
0.0059
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, mutant enzyme E149N
7.3
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, wild-type enzyme
14.1
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, wild-type enzyme
16.9
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme H339S
18.2
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme G342S
23.8
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme K370I
20.9
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme G342S
24.5
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme H339S
39.8
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme K370I
54.9
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0029 - 81
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
0.0029
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, mutant enzyme E88N
0.098
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, mutant enzyme E149N
81
beta-D-4-deoxy-DELTA-4,5-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp
pH 6.5, 30°C, wild-type enzyme
19.6
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme H339S
36.1
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme G342S
36.8
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, wild-type enzyme
42
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
pH 7.5, 30°C, mutant enzyme K370I
2.95
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, wild-type enzyme
2.99
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme G342S
3.41
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme H339S
18.1
beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S
pH 7.5, 30°C, mutant enzyme K370I
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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
additional information
-
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
45
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
30°C: about 90% of maximal activity, 55°C: about 35% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
the enzyme expression is induced threefold and sixfold during growth on pectin and polygalacturonic acid, respectively, when compared with growth on glucose
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
Clostridium acetobutylicum ATCC 824 gene CA_C0359 encodes a putative unsaturated rhamnogalacturonyl hydrolase (URH) with distant amino-acid sequence homology to YteR of Bacillus subtilis strain 168. YteR, like other URHs, has core structural homology to unsaturated glucuronyl hydrolases, but hydrolyzes the unsaturated disaccharide derivative of rhamnogalacturonan I. There is a conserved aspartic acid residue in both structures, which has been shown to be important for hydration of the C=C bond during the release of unsaturated galacturonic acid by YteR. A surface electrostatic potential comparison of CA_C0359 and proteins from CAZy families GH88 and GH105 reveals the make-up of the active site to be a combination of the unsaturated rhamnogalacturonyl hydrolase (EC 3.2.1.172) and the unsaturated glucuronyl hydrolase (EC 3.2.1.179) from Bacillus subtilis strain 168. Structural and electrostatic comparisons suggest that the enzyme may have a slightly different substrate specificity from that of YteR
malfunction
SagUGL mutants D115N and D115N/K370S show negligible enzyme activity. The side chain of Asn115 is drastically shifted in both mutants owing to the interaction with several residues, including Asp175, by formation of hydrogen bonds. This interaction between Asn115 and Asp175 probably prevents the mutants from triggering the enzyme reaction using Asp175 as an acid catalyst
additional information
additional information
substrate-bound enzyme structure modeling, overview
additional information
two Asp residues, Asp115 and Asp175 of Streptococcus agalactiae UGL (SagUGL), are completely conserved in other bacterial UGLs, one of which (Asp175 of SagUGL) acts as a general acid and base catalyst. The other Asp (Asp115 of SagUGL) also affects the enzyme activity
additional information
-
two Asp residues, Asp115 and Asp175 of Streptococcus agalactiae UGL (SagUGL), are completely conserved in other bacterial UGLs, one of which (Asp175 of SagUGL) acts as a general acid and base catalyst. The other Asp (Asp115 of SagUGL) also affects the enzyme activity
Show AA Sequence and Transmembrane Helices (369 entries)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
the protein adopts a six-(alpha/alpha)-hairpin barrel fold with a small two-stranded beta-sheet and helix overlaying the end of the barrel near the active pocket. The CA_C0359 structure closely adopts the fold of family GH105 proteins
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallized at 20°C from a droplet containing 56% 2-methyl-2,4-pentanediol, 0.1 M NaCl, 0.1 M glycine/NaOH pH 8.2 and 0.1 M dithiothreitol using the hanging-drop vapour-diffusion method. The crystals are hexagonal and belonged to space group P6122 or P6522, with unit-cell parameters a = b = 102.8, c = 223.4 A. Diffraction data to 2.4 A are collected from a single crystal
crystals are obtained by using hanging drop vapor diffusion and microseeding, wild-type enzyme, mutant enzyme D88N and mutant enzyme D88N in complex with beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc
sitting-drop vapor duffusion method, X-ray crystallographic structure of the enzyme at 1.8 A resolution
vapor diffusion method, demonstration of substrate recognition mechanism of the unsaturated glucuronyl hydrolase by determining the X-ray crystallographic structure of its substrate-enzyme complexes (D88N/DELTAGlcA-Glc-Pha-Glc and D99N/DELTAGlcA-GlcNAc). The tetrasaccharide-enzyme complex demonstrates that at least four subsites are present in the active pocket
partially purified recombinnat enzyme, hanging-drop vapor-diffusion method, mixing 0.002 ml 7.5 mg/ml protein solution with 0.002 ml reservoir solution consisting of 0.1 M Tris, pH 7.75, 16% w/v PEG 4000, 21°C, X-ray diffraction structure determination and analysis at 1.6 A resolution, modelling
purified recombinant enzyme mutants D115N and D115N/K370S, sitting drop vapor diffusion, 20 mg/ml and 40 mg/ml protein solution, respectively, is mixed with an equal volumes of reservoir solution. The reservoir solution for mutant D115N crystallization contains 1.5 M ammonium sulfate and 0.1 M Tris-HCl, pH 9.0, D115N crystals are grown at 20°C for a week. The reservoir solution for mutant D115N/K370S crystallization contains 40% ethylene glycol, 0.5 mM dithiothreitol, and 0.1 M Tris-HCl, pH 7.0, D115N/K370S is crystallized at 20°C for 2 months. X-ray diffraction structure determination and analysis at 2.00 A and 1.79 A resolution, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D149N
almost inactive mutant enzyme, kcat/Km is significantly lower than that of the wild-type enzyme for gellan tetrasaccharide
D88N
almost inactive mutant enzyme, kcat/Km is significantly lower than that of the wild-type enzyme for gellan tetrasaccharide
G342S
kcat/KM for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S is similar to the wild-type value, kcat/Km for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc is similar to wild-type value
H339S
kcat/KM for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S is 1.2fold higher than the kcat/Km-value for the wild-type enzyme, kcat/Km for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc is 53% of the wild-type value
I344K
kcat/KM for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S is 6.1fold higher than the wild-type value, kcat/Km for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc is similar to the wild-type value
D149N
-
almost inactive mutant enzyme, kcat/Km is significantly lower than that of the wild-type enzyme for gellan tetrasaccharide
-
D88N
-
almost inactive mutant enzyme, kcat/Km is significantly lower than that of the wild-type enzyme for gellan tetrasaccharide
-
G342S
-
kcat/KM for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S is similar to the wild-type value, kcat/Km for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc is similar to wild-type value
-
H339S
-
kcat/KM for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S is 1.2fold higher than the kcat/Km-value for the wild-type enzyme, kcat/Km for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc is 53% of the wild-type value
-
I344K
-
kcat/KM for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc6S is 6.1fold higher than the wild-type value, kcat/Km for beta-D-4-deoxy-DELTA4,5-GlcAp-(1->3)-beta-D-GalNAc is similar to the wild-type value
-
D115N
site-directed mutagenesis, the mutant shows only negligible enzyme activity
D115N/K370S
site-directed mutagenesis, the mutant shows only negligible enzyme activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by ultrafiltration and gel filtration
recombinant wild-type enzyme and enzyme mutants from Escherichia coli strain HMS174(DE3)pLysS
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene CA_C0359, recombinant expression of the intein-fused enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli TOP10, transcriptional analysis using quantitative PCR
gene ugl, recombinant expression of wild-type enzyme and enzyme mutants in Escherichia coli strain HMS174(DE3)pLysS
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induced in the bacterial cells grown on either gellan or xanthan. Expression levels of unsaturated glucuronyl hydrolase in the bacterium grown on gellan and xanthan are 20.7 and 16.4 mU/mg protein, respectively, while the bacterium grown in the glucose, pectin, or LB medium fails to produce the enzyme
the enzyme expression is induced threefold and sixfold during growth on pectin and polygalacturonic acid, respectively, when compared with growth on glucose
induced in the bacterial cells grown on either gellan or xanthan. Expression levels of unsaturated glucuronyl hydrolase in the bacterium grown on gellan and xanthan are 20.7 and 16.4 mU/mg protein, respectively, while the bacterium grown in the glucose, pectin, or LB medium fails to produce the enzyme
-
induced in the bacterial cells grown on either gellan or xanthan. Expression levels of unsaturated glucuronyl hydrolase in the bacterium grown on gellan and xanthan are 20.7 and 16.4 mU/mg protein, respectively, while the bacterium grown in the glucose, pectin, or LB medium fails to produce the enzyme
-
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mori, S.; Akao, S.; Miyake, O.; Nankai, H.; Hashimoto, W.; Mikami, B.; Murata, K.
Crystallization and preliminary X-ray analysis of a novel unsaturated glucuronyl hydrolase from Bacillus sp. GL1
Acta Crystallogr. Sect. D
59
946-949
2003
Bacillus sp. (in: Bacteria) (Q9RC92), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) GL1 (Q9RC92)
brenda
Hashimoto, W.; Kobayashi, E.; Nankai, H.; Sato, N.; Miya, T.; Kawai, S.; Murata, K.
Unsaturated glucuronyl hydrolase of Bacillus sp. GL1: novel enzyme prerequisite for metabolism of unsaturated oligosaccharides produced by polysaccharide lyases
Arch. Biochem. Biophys.
368
367-374
1999
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) GL1
brenda
Itoh, T.; Hashimoto, W.; Mikami, B.; Murata, K.
Substrate recognition by unsaturated glucuronyl hydrolase from Bacillus sp. GL1
Biochem. Biophys. Res. Commun.
344
253-262
2006
Bacillus sp. (in: Bacteria) (Q9RC92), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) GL1 (Q9RC92)
brenda
Itoh, T.; Akao, S.; Hashimoto, W.; Mikami, B.; Murata, K.
Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A resolution
J. Biol. Chem.
279
31804-31812
2004
Bacillus sp. (in: Bacteria) (Q9RC92), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) GL1 (Q9RC92)
brenda
Itoh, T.; Hashimoto, W.; Mikami, B.; Murata, K.
Crystal structure of unsaturated glucuronyl hydrolase complexed with substrate: molecular insights into its catalytic reaction mechanism
J. Biol. Chem.
281
29807-29816
2006
Bacillus sp. (in: Bacteria) (Q9RC92), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) GL1 (Q9RC92)
brenda
Nakamichi, Y.; Maruyama, Y.; Mikami, B.; Hashimoto, W.; Murata, K.
Structural determinants in streptococcal unsaturated glucuronyl hydrolase for recognition of glycosaminoglycan sulfate groups
J. Biol. Chem.
286
6262-6271
2011
Bacillus sp. (in: Bacteria) (Q9RC92), Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) GL1 (Q9RC92)
brenda
Germane, K.L.; Servinsky, M.D.; Gerlach, E.S.; Sund, C.J.; Hurley, M.M.
Structural analysis of Clostridium acetobutylicum ATCC 824 glycoside hydrolase from CAZy family GH105
Acta Crystallogr. Sect. F
71
1100-1108
2015
Clostridium acetobutylicum (Q97M41)
brenda
Nakamichi, Y.; Oiki, S.; Mikami, B.; Murata, K.; Hashimoto, W.
Conformational change in the active site of streptococcal unsaturated glucuronyl hydrolase through site-directed mutagenesis at Asp-115
Protein J.
35
300-309
2016
Streptococcus agalactiae (A0A0E1EQ72), Streptococcus agalactiae
brenda
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Release 2023.1 (January 2023)
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