Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.172 extracted from

  • Silva, I.R.; Jers, C.; Meyer, A.S.; Mikkelsen, J.D.
    Rhamnogalacturonan I modifying enzymes an update (2016), New Biotechnol., 33, 41-54 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis Bacillus subtilis

KM Value [mM]

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/ Products (Substrates)

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

Organism UniProt Comment Textmining
Bacillus subtilis O31521
-
-
Bacillus subtilis O34559
-
-

Reaction

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 and Products (Substrate)

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

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

Synonyms Comment Organism
RGI hydrolase
-
Bacillus subtilis
URGH
-
Bacillus subtilis
YesR
-
Bacillus subtilis
YteR
-
Bacillus subtilis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
-
Bacillus subtilis

pH Optimum

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

pI Value

Organism Comment pI Value Maximum pI Value
Bacillus subtilis
-
-
4.9
Bacillus subtilis
-
-
5.9

General Information

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