Cloned (Comment) | Organism |
---|---|
phylogenetic analysis | Bacillus subtilis |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.1 | - |
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose | pH 4.0, 30°C | Bacillus subtilis | |
0.719 | - |
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose | pH 6.0, 30°C | Bacillus subtilis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H2O | Bacillus subtilis | - |
5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose | - |
? | |
rhamnogalacturonan I + H2O | Bacillus subtilis | RGI, degrading enzymes are active on the RGI backbone of pectin and are thus strictly specific for cleaving bonds in the repetitive [(1->2)-alpha-L-Rhap-(1->4)-alpha-D-GalpA-(1->2)] structure | beta-L-rhamnose + ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus subtilis | O31521 | - |
- |
Bacillus subtilis | O34559 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H2O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose | mode of action and site of action, overview. In the active site of YesR Asp135 is most likely functioning as proton donor | Bacillus subtilis | |
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H2O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose | mode of action and site of action, overview. In the active site of YteR Asp143 is most likely functioning as proton donor | Bacillus subtilis |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H2O | - |
Bacillus subtilis | 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose | - |
? | |
additional information | URGH is active only on RGI oligomers with alpha-DELTA4,5-unsaturated-GalpA (i.e. 2-O-(4-deoxy-beta-L-threo-hex-4-enopyra-nuronosyl)) at the non-reducing end. The URGH activity catalyses the cleavage of the alpha-(1->2) glycosidic bond between the DELTA4,5-unsaturated-GalpA and L-Rhap releasing single unsaturated DELTAGalpA (5-dehydro-4-deoxy-D-galacturonate) | Bacillus subtilis | ? | - |
? | |
rhamnogalacturonan I + H2O | RGI, degrading enzymes are active on the RGI backbone of pectin and are thus strictly specific for cleaving bonds in the repetitive [(1->2)-alpha-L-Rhap-(1->4)-alpha-D-GalpA-(1->2)] structure | Bacillus subtilis | beta-L-rhamnose + ? | - |
? | |
rhamnogalacturonan I + H2O | - |
Bacillus subtilis | L-rhamnose + ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 43000 | Bacillus subtilis |
? | x * 39000 | Bacillus subtilis |
More | enzyme URGH from GH105 has a alpha/alpha double toroid structure with six-a-hairpins arranged in a double helical barrel | Bacillus subtilis |
More | enzyme URGH from GH105 has a alpha/alpha double toroid structure with six-alpha-hairpins arranged in a double helical barrel, overview | Bacillus subtilis |
Synonyms | Comment | Organism |
---|---|---|
RGI hydrolase | - |
Bacillus subtilis |
URGH | - |
Bacillus subtilis |
YesR | - |
Bacillus subtilis |
YteR | - |
Bacillus subtilis |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
50 | - |
- |
Bacillus subtilis |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
additional information | - |
residues Asp88 and Tyr41 may modulate the pKa of Asp143 in YteR thereby inducing the lower pH optimum of this enzyme | Bacillus subtilis |
4 | - |
- |
Bacillus subtilis |
6 | - |
- |
Bacillus subtilis |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Bacillus subtilis | - |
- |
4.9 |
Bacillus subtilis | - |
- |
5.9 |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic and structural traits of RGI hydrolases, overview. The enzyme belongs to the glycosyl hydrolase family 105, GH105. Enzyme URGH from GH105 has a alpha/alpha double toroid structure with six-a-hairpins arranged in a double helical barrel | Bacillus subtilis |
evolution | phylogenetic and structural traits of RGI hydrolases, overview. The enzyme belongs to the glycosyl hydrolase family 105, GH105. The URGH from GH105 has a alpha/alpha double toroid structure with six-a-hairpins arranged in a double helical barrel | Bacillus subtilis |
additional information | in the active site of YesR Asp135 is most likely functioning as proton donor | Bacillus subtilis |
additional information | in the active site of YteR Asp143 is most likely functioning as proton donor. Residues Asp88 and Tyr41 may modulate the pKa of Asp143 in YteR thereby inducing the lower pH optimum of this enzyme | Bacillus subtilis |