3.2.1.51: alpha-L-fucosidase

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

Reaction

Synonyms

acid hydrolase, Afc2, Afc3, AFU, Alf1_Wf, alfA, alfB, alfC, alpha-fuc, alpha-fucosidase, alpha-L fucosidase, alpha-L-fucosidase, alpha-L-fucosidase 1, alpha-L-fucosidase 2, alpha-L-fucosidase I, alpha-L-fucosidase iso2, alpha-L-fucosidase isoenzyme 1, Alpha-L-fucoside fucohydrolase, alpha-L-fucoside fucohydrolase 2, alphafuc, bfo_2737, BgFUC, Eo0918, Eo3066, Eo3812, FpFucA, FucA, Fuca1, Fuca2, Fuca3, FucFA, fucosidase, alpha-L-1, tissue, h-Fuc, mfuc1, mfuc2, mfuc3, mfuc4, mfuc5, mfuc6, mfuc7, Pap-Alf, serum AFU, serum alpha-L-fucosidase, TfFuc1, TMalphafuc

ECTree

     3 Hydrolases

         3.2 Glycosylases

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

                3.2.1.51 alpha-L-fucosidase

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Results	in table
18	Activating Compound
7083	AA Sequence
24	Application
1	CAS Registry Number
22	Cloned(Commentary)
6	Crystallization (Commentary)
1295	Disease/ Diagnostics
1	Expression
11	General Information
6	General Stability
7	IC50 Value
177	Inhibitors
4	kcat/KM [mM/s]
76	Ki Value [mM]
206	KM Value [mM]
42	Localization
27	Metals/Ions
96	Molecular Weight [Da]
118	Natural Substrates/ Products (Substrates)
8	Organic Solvent Stability
243	Organism
4	Pathway
68	PDB ID
102	pH Optimum
23	pH Range
30	pH Stability
11	pI Value
32	Posttranslational Modification
61	Protein Variants
70	Purification (Commentary)
5	Reaction
4	Reaction Type
214	Reference
175	Source Tissue
82	Specific Activity [micromol/min/mg]
31	Storage Stability
378	Substrates and Products (Substrate)
52	Subunits
93	Synonyms
1	Systematic Name
27	Temperature Optimum [°C]
7	Temperature Range [°C]
76	Temperature Stability [°C]
107	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.51 - alpha-L-fucosidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystals of mutant D229 soaked with aryl glycoside substrate 4-nitrophenyl alpha-L-fucoside. X-ray data at 1.95 A resolution reveal an unambiguous electron density for the unhydrolysed substrate, which is in the 1C4 conformation. Trapping of fucosyl-enzyme intermediate on the E288Q variant and analysis at 2.1 A. Again, the observed electron density reveals the trapped beta-L-fucosyl enzyme intermediate, here in the 3S1 conformation with the beta-linkage to the nucleophile Asp229

Bacteroides thetaiotaomicron

-

708881

-

Paenibacillus thiaminolyticus

E3PQQ9

750714

recombinant enzyme, vapor diffusion method

Saccharolobus solfataricus

-

663840

-

Thermotoga maritima

-

679718

in complex with iminocyclitol inhibitors. Compounds show time-dependent, slow-binding inhibition. Inhibitors that have an extra substituent at C1 residing at the beta position adopt a product-like 1C4 chair conformation rather than the transition-state 3H4 half-chair conformation

Thermotoga maritima

-

707139

the crystal structure of enzyme is determined at 2.5 A resolution by the MAD method

Thermotoga maritima

-

656203