3.2.1.171: rhamnogalacturonan hydrolase
This is an abbreviated version!
For detailed information about rhamnogalacturonan hydrolase, go to the full flat file.
Word Map on EC 3.2.1.171
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3.2.1.171
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aspergillus
-
aculeatus
-
pectic
-
rgases
-
galacturonic
-
galactan
-
homogalacturonans
-
right-handed
-
endo-polygalacturonase
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polygalacturonase
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irpex
-
pectate
-
lacteus
- 3.2.1.171
- aspergillus
- aculeatus
-
pectic
-
rgases
-
galacturonic
- galactan
- homogalacturonans
-
right-handed
- endo-polygalacturonase
- polygalacturonase
- irpex
- pectate
- lacteus
Reaction
Endohydrolysis of alpha-D-GalA-(1->2)-alpha-L-Rha glycosidic bond in the rhamnogalacturonan I backbone with initial inversion of anomeric configuration releasing oligosaccharides with beta-D-GalA at the reducing end =
Synonyms
endo-rhamnogalacturonase, HIRHG, RG hydrolase, RG-hydrolase, RGase A, RGH, RGI endo-hydrolase, RGI hydrolase, rhamnogalacturonan hydrolase, rhamnogalacturonase A, RhgA, RhgA_An, RhgB, RhgB_An
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.2.1.171 - rhamnogalacturonan hydrolase
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glycoprotein
a significant amount of glycan structures is attached to the enzyme. Three potential sites for N-linked glycosylation are present in the primary structure of RGase A (amino acid positions 50, 235, and 317). Recombinant RGase A is overglycosylated by approximately 3 kDa compared with native RGase A
glycoprotein
the enzyme is highly glycosylated corresponding to 5.9 kDa
glycoprotein
the enzyme is highly glycosylated: two N-linked and eighteen O-linked glycosylation sites in the structure. The glycan groups bound to RGase A are important to the stability of the crystal