2.4.1.20: cellobiose phosphorylase

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For detailed information about cellobiose phosphorylase, go to the full flat file.

Reaction

Synonyms

Cbp, CbpA, cellobiose phosphorylase A, cellobiose:orthophosphate alpha-D-glucosyltransferase, CPase, CuCbP, GH94 cellobiose phosphorylase, lactose phosphorylase, ra2122, THA_1941, Tm_1848

ECTree

     2 Transferases

         2.4 Glycosyltransferases

             2.4.1 Hexosyltransferases

                2.4.1.20 cellobiose phosphorylase

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Results	in table
1	Activating Compound
146	AA Sequence
8	Application
1	CAS Registry Number
32	Cloned(Commentary)
3	Crystallization (Commentary)
2	Expression
2	General Information
3	General Stability
30	Inhibitors
58	kcat/KM [mM/s]
10	Ki Value [mM]
124	KM Value [mM]
7	Metals/Ions
19	Molecular Weight [Da]
49	Natural Substrates/ Products (Substrates)
6	Organic Solvent Stability
112	Organism
4	Pathway
28	PDB ID
19	pH Optimum
6	pH Range
3	pH Stability
26	Protein Variants
21	Purification (Commentary)
4	Reaction
1	Reaction Type
65	Reference
32	Specific Activity [micromol/min/mg]
205	Substrates and Products (Substrate)
18	Subunits
35	Synonyms
1	Systematic Name
14	Temperature Optimum [°C]
4	Temperature Range [°C]
15	Temperature Stability [°C]
91	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.4.1.20 - cellobiose phosphorylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

in complex with phosphate, to 2.4 A resolution. Enzyme is composed of four distinct domains, an N-terminal domain with residues 1-279, a helical linker with residues 280-314, an (alpha/beta)6-barrel domain with residues 321-734, and a C-terminal beta-sandwich domain with residues 315-320 and 735-811. The side chains of His653, Gln699 and Thr718 and the backbone N-atom of Gly719 coordinate the phosphate bound in the interior of the (alpha/beta)6-barrel domain. Two short helical extensions, residues 158-169, from the N-terminal domain of the adjacent subunit extend into the cleft which runs along the face of the (alpha/beta)6-barrel domain, forming an active-site pocket. An additional loop, residues 488-507, lays on top of the active-site pocket, forming a restrictive active-site pocket that is large enough to bind a disaccharide but not large enough to bind an oligosaccharide

Acetivibrio thermocellus

Q8VP44

718502

at 25°C using the sitting-drop vapour diffusion method. Cellobiose phosphorylase-SO4 and cellobiose phosphorylase-PO4 structures are determined at 2.0 and 2.1 A resolution to R factor (Rfree) of 17.6% (21.3%) and 18.0% (22%) respectively. The pH values for crystallization are pH 8.2 for cellobiose phosphorylase-PO4 and pH 6.5 for cellobiose phosphorylase-SO4.

Cellulomonas gilvus

-

671874

crystallization of recombinant enzyme by the sitting-drop vapour-diffusion method using 10 mg/ml purified enzyme, 1.5 M ammonium sulfate, 0.1 M MES buffer pH 7.0 and 5 mM glucose. A suitable crystal is obtained after 10 d incubation at 298 K. The crystal belongs to space group P2(1), with unit-cell parameters a = 84.77, b = 98.31, c = 104.04 A, beta = 102.73°. X-ray diffraction data to 2.1 A resolution collected at KEK-PF BL-5A

Cellulomonas gilvus

-

657459