3.2.1.B28: Pyrococcus furiosus beta-glycosidase

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For detailed information about Pyrococcus furiosus beta-glycosidase, go to the full flat file.

Reaction

The enzyme produces mannose and glucose mainly from mannooligosaccharides and cellobiose by hydrolyzing them from the reducing end. It can not hydrolyze alpha-form substrates and bulk polymers like mannan and starch =

Synonyms

beta-glycosidase, Bgl, BGLPf, CelB, PFTG

ECTree

3 Hydrolases

3.2 Glycosylases

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

3.2.1.B28 Pyrococcus furiosus beta-glycosidase

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Results	in table
1	Activating Compound
2	AA Sequence
17	Application
17	Cloned(Commentary)
3	Crystallization (Commentary)
2	Expression
5	General Stability
18	Inhibitors
89	kcat/KM [mM/s]
9	Ki Value [mM]
127	KM Value [mM]
1	Localization
2	Metals/Ions
13	Molecular Weight [Da]
1	Organic Solvent Stability
38	Organism
17	pH Optimum
4	pH Range
1	pH Stability
1	pI Value
26	Protein Variants
10	Purification (Commentary)
1	Reaction
38	Reference
40	Specific Activity [micromol/min/mg]
103	Substrates and Products (Substrate)
13	Subunits
20	Synonyms
15	Temperature Optimum [°C]
4	Temperature Range [°C]
45	Temperature Stability [°C]
109	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.2.1.B28 - Pyrococcus furiosus beta-glycosidase

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3.3 A resolution structural model. CelB shows a homo-tetramer configuration, with subunits having a typical (betaalpha)8-barrel fold

Pyrococcus furiosus

Q51723

326270

hanging-drop vapour-diffusion method, a monomeric form of the enzyme is constructed by removing the C-terminal region (the mutant lacks the C-terminal 23 residues and includes six substitutive mutations R170A, R220A, Y227F, F447S, R448V and E449K) of the enzyme and its crystal structure is solved at a resolution of 2.8 A in space group

Pyrococcus furiosus

Q51723

726640

to 2.35 A resolution. There is one tetramer in the asymmetric unit and the dimeric molecule exhibits a structure that is stable towards sodium dodecyl sulfate even after boiling at 368 K. The elongation at the C-terminal end forms a hydrophobic patch at the dimer interface that might contribute to hyperthermostability

Pyrococcus furiosus

Q51723

735377