3.2.1.171: rhamnogalacturonan hydrolase

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For detailed information about rhamnogalacturonan hydrolase, go to the full flat file.

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

     3 Hydrolases

         3.2 Glycosylases

             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds

                3.2.1.171 rhamnogalacturonan hydrolase

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Results	in table
17	AA Sequence
6	Cloned(Commentary)
2	Crystallization (Commentary)
2	Expression
8	General Information
2	Localization
6	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
13	Organism
5	pH Optimum
1	pH Range
2	pH Stability
6	pI Value
3	Posttranslational Modification
2	Protein Variants
1	Purification (Commentary)
3	Reaction
12	Reference
2	Source Tissue
5	Specific Activity [micromol/min/mg]
18	Substrates and Products (Substrate)
10	Subunits
30	Synonyms
1	Systematic Name
3	Temperature Optimum [°C]
1	Temperature Range [°C]
2	Temperature Stability [°C]

Crystallization

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Crystallization on EC 3.2.1.171 - rhamnogalacturonan hydrolase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

hanging-drop vapour-diffusion technique, crystals diffract beyond 2.0 A resolution and belong to one of the orthorhombic space groups 12(1)2(1)2 or I222, with the unit-cell parameters a = 62.9, b = 125.4 and c = 137.0 A

Aspergillus aculeatus

Q00001

706944

structure solved by the single isomorphous replacement method including anomalous scattering to 2.0 A resolution. The enzyme folds into a large right-handed parallel beta helix, with a core composed of 13 turns of b strands. Four parallel beta sheets (PB1, PB1a, PB2 and PB3), formed by the consecutive turns, are typically separated by a residue in the conformation of a left-handed a helix

Aspergillus aculeatus

Q00001

710581