3.2.1.172: unsaturated rhamnogalacturonyl hydrolase
This is an abbreviated version!
For detailed information about unsaturated rhamnogalacturonyl hydrolase, go to the full flat file.
Reaction
Synonyms
CA_C0359, More, RGI hydrolase, unsaturated rhamnogalacturonyl hydrolase, URGH, URH, YesR, YteR
ECTree
Advanced search results
General Information
General Information on EC 3.2.1.172 - unsaturated rhamnogalacturonyl hydrolase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
additional information
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
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
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
in the active site of YesR Asp135 is most likely functioning as proton donor
additional information
in the active site of YesR Asp135 is most likely functioning as proton donor
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
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
additional information
substrate-bound enzyme structure modeling, overview