2.4.2.2: pyrimidine-nucleoside phosphorylase

This is an abbreviated version!
For detailed information about pyrimidine-nucleoside phosphorylase, go to the full flat file.

Reaction

Synonyms

AmPyNP, BbPyNP, BfPyNP, BsPyNP, deoA, EC 2.4.2.23, GsPyNP, GtPyNP, LpPyNP, nucleoside phosphorylase, PDP, phosphorylase, pyrimidine nucleoside, Py-NPase, PYNP, pynpase, pyrimidine nucleoside phosphorylase, pyrimidine ribonucleoside phosphorylase, pyrimidine-nucleoside phosphorylase, pyrimidine/purine nucleoside phosphorylase, TTHA1771, TtPyNP, udp, UPase

ECTree

     2 Transferases

         2.4 Glycosyltransferases

             2.4.2 Pentosyltransferases

                2.4.2.2 pyrimidine-nucleoside phosphorylase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
1	Activating Compound
13423	AA Sequence
8	Application
1	CAS Registry Number
18	Cloned(Commentary)
6	Crystallization (Commentary)
85	Disease/ Diagnostics
1	Expression
9	General Information
3	General Stability
10	IC50 Value
7	Inhibitors
12	kcat/KM [mM/s]
2	Ki Value [mM]
50	KM Value [mM]
7	Molecular Weight [Da]
71	Natural Substrates/ Products (Substrates)
136	Organism
1	Oxidation Stability
5	Pathway
10	PDB ID
19	pH Optimum
3	pH Range
2	pH Stability
6	Protein Variants
11	Purification (Commentary)
4	Reaction
5	Reaction Type
45	Reference
1	Renatured (Commentary)
2	Source Tissue
15	Specific Activity [micromol/min/mg]
2	Storage Stability
194	Substrates and Products (Substrate)
11	Subunits
62	Synonyms
1	Systematic Name
15	Temperature Optimum [°C]
5	Temperature Range [°C]
19	Temperature Stability [°C]
20	Turnover Number [1/s]

Renatured

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

Renatured on EC 2.4.2.2 - pyrimidine-nucleoside phosphorylase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to Renatured Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

RENATURED/Commentary

ORGANISM

UNIPROT

LITERATURE

recombinant enzyme, unfolding equilibrium of UPase in 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, 5.0 mM MgCl2, 1.0 mM Tris(2-carboxyethyl)phosphine hydrochloride (TCEP), and 10 M urea at pH 8.0, 25°C overnight. Monitoring by pulse proteolysis. Cm values are measured by fitting the band intensities on SDS-PAGE with varying urea concentrations to a simple two-state model. Data are fitted to the two-state model in the absence of ATP and to a three-state model in the presence of ATP. Purified UPase remains folded following treatment with 0 to about 4 M urea, and unfolding occurs from 4 to 6 M urea in the absence of ATP. For refolding experiments, 0.4 mg/ml UPase are initially incubated overnight in 20 mM Tris-HCl buffer, pH 8.0, containing 50 mM NaCl, 5.0 mM MgCl2, 1.0 mM TCEP, and 7.5 M urea to induce the unfolded state. Refolding is then performed by diluting samples five times into refolding buffer to reach the following final conditions: 0.08 mg/ml UPase, 20 mM Tris-HCl, pH 8.0, 50 mM NaCl, 5.0 MgCl2, 1.0 mM TCEP, and 1.5 M urea with or without 2.0 mM ATP. Partially unfolded intermediate states of UPase accumulate in the presence of ATP

Escherichia coli

P0C037

758699