3.2.1.40: alpha-L-rhamnosidase

This is an abbreviated version!
For detailed information about alpha-L-rhamnosidase, go to the full flat file.

Reaction

Synonyms

alpha-L-rhamnosidase, alpha-L-rhamnosidase A, alpha-L-rhamnosidase B, alpha-L-rhamnosidase N, alpha-L-rhamnosidase Ram A, alpha-L-rhamnosidase T, alpha-RHA, AoRha, AorhaA, BtRha, BtRha78A, DtRha, EC 3.2.1.66, GH106 alpha-L-rhamnosidase, gypenoside-alpha-L-rhamnosidase, KoRha, L-rhamnosidase, More, naringinase, pnp-rhamnohydrolase, RamA, RHA-P, RhaA, RhaB, RhaB1, RhaB2, RhaL1, Rham, rhamnosidase, alpha -L-, RhmA, saponin-alpha-L-rhamnosidase

ECTree

     3 Hydrolases

         3.2 Glycosylases

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

                3.2.1.40 alpha-L-rhamnosidase

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Results	in table
3	Activating Compound
14294	AA Sequence
37	Application
1	CAS Registry Number
23	Cloned(Commentary)
4	Crystallization (Commentary)
6	Expression
4	General Stability
6	IC50 Value
146	Inhibitors
29	kcat/KM [mM/s]
22	Ki Value [mM]
81	KM Value [mM]
13	Localization
31	Metals/Ions
39	Molecular Weight [Da]
30	Natural Substrates/ Products (Substrates)
9	Organic Solvent Stability
135	Organism
1	Pathway
7	PDB ID
55	pH Optimum
24	pH Range
21	pH Stability
10	pI Value
12	Posttranslational Modification
50	Protein Variants
39	Purification (Commentary)
1	Reaction
1	Reaction Type
103	Reference
22	Source Tissue
30	Specific Activity [micromol/min/mg]
4	Storage Stability
309	Substrates and Products (Substrate)
42	Subunits
51	Synonyms
1	Systematic Name
47	Temperature Optimum [°C]
23	Temperature Range [°C]
68	Temperature Stability [°C]
31	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.40 - alpha-L-rhamnosidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

X-ray structure of the GH78 family alpha-L-rhamnosidase from Aspergillus terreus has been determined at 1.38 A resolution using the sulfur single-wavelength anomalous dispersion phasing method

Aspergillus terreus

I0AZ41

749499

native and selenomethionine-derivaties, 1.9 A resolution with a final R-factor of 18.2%, hanging-drop method, data-collection and statistics indicated, overall structure shown, quaternary structure, catalytic domain and active cleft determined, complex with the reaction product rhamnose determined and refined at 2.1 A with a final R-factor of 19.5%

Bacillus sp. (in: Bacteria)

Q93RE7

681462

native and selenomethionine-derivaties, crystallized at 293 K, hanging-drop vapour diffusion with PEG 8000 as a precipitant, data collection and statistics indicated

Bacillus sp. (in: Bacteria)

Q93RE7

677351

hanging drop vapor diffusion method, crystal structure is determined at 2.7 A resolution with rhamnose bound in the active site of the catalytic domain. The homodimeric structure is significantly smaller than those of the other previously determined GH78 structures. Nevertheless, the enzyme displays alpha-rhamnosidase activity when assayed in vitro, suggesting that the additional structural domains found in the related enzymes are dispensible for function

Klebsiella oxytoca

A0A0J9X262

752138