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Literature summary for 3.2.1.174 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 Aspergillus aculeatus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
rhamnogalacturonan I + H2O Aspergillus aculeatus 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
Aspergillus aculeatus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
Exohydrolysis of the alpha-L-Rha-(1->4)-alpha-D-GalA bond in rhamnogalacturonan oligosaccharides with initial inversion of configuration releasing beta-L-rhamnose from the non-reducing end of rhamnogalacturonan oligosaccharides mode of action and site of action, overview Aspergillus aculeatus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12.9
-
substrate MHR-S, pH 5.0, 60°C Aspergillus aculeatus
57.6
-
substrate degalactosylated MHR-S, pH 5.0, 60°C Aspergillus aculeatus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
degalactosylated MHR-S + H2O degalactosylated saponified modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, galactosyl residues removed. The activity increases 78% when tested with MHR-S without galactose substitutions, and in essence the activity of this enzyme is thus hindered by galactose substitutions Aspergillus aculeatus beta-L-rhamnose + ?
-
?
MHR + H2O i.e. modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, the enzyme is active towards MHR-S as well as unsaponified MHR Aspergillus aculeatus beta-L-rhamnose + ?
-
?
MHR-S + H2O i.e. saponified modified hairy regions of xylogalacturonan, from apple pectin, residue remaining after enzymatic liquefaction of pectin, the enzyme is active towards MHR-S as well as unsaponified MHR Aspergillus aculeatus beta-L-rhamnose + ?
-
?
additional information RGRH exo-enzyme catalyses the cleavage of the alpha-(1->4) glycosidic bonds between L-Rhap and D-GalpA in the non-reducing terminus, releasing single beta-L-Rhap. Enzyme RGRH requires Rhap at the non-reducing end for action Aspergillus aculeatus ?
-
?
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 Aspergillus aculeatus beta-L-rhamnose + ?
-
?
rhamnogalacturonan I + H2O Aspergillus aculeatus RGRH is active on the nonreducing end Rhap-linkage in RGI fragments Aspergillus aculeatus L-rhamnose + ?
-
?

Subunits

Subunits Comment Organism
? x * 84000 Aspergillus aculeatus

Synonyms

Synonyms Comment Organism
RGI exo-hydrolase
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Aspergillus aculeatus
RGI hydrolase
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Aspergillus aculeatus
RGI rhamnohydrolase
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Aspergillus aculeatus
RGRH
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Aspergillus aculeatus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Aspergillus aculeatus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
60
-
pH 5.0, 1 h, stable Aspergillus aculeatus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
4
-
-
Aspergillus aculeatus

pH Stability

pH Stability pH Stability Maximum Comment Organism
3 5 stable at, unstable below and above that range Aspergillus aculeatus

pI Value

Organism Comment pI Value Maximum pI Value
Aspergillus aculeatus
-
5.4 4.9

General Information

General Information Comment Organism
evolution phylogenetic and structural traits of RGI hydrolases, overview. The enzyme belongs to the glycosyl hydrolase family 28, GH28 Aspergillus aculeatus