2.4.2.2: pyrimidine-nucleoside phosphorylase

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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

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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]

General Stability

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General Stability on EC 2.4.2.2 - pyrimidine-nucleoside phosphorylase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

Escherichia coli uridine phosphorylase is destabilized in the presence of ATP. ATP alters protein folding and function of the enzyme. ATP specifically accelerates the unfolding rate of uridine phosphorylase with no observable effects on the refolding process, ATP binding mechanism analysis. Purified UPase remains folded following treatment with 0 to about 4 M urea, and unfolding occurred from 4 to 6 M urea in the absence of ATP. Partially unfolded intermediate states of UPase accumulate in the presence of ATP. ATP interacts with a transition state close to the folded state.

Escherichia coli

P0C037

758699

repeated cycles of freezing and thawing inactivate the enzyme if phosphate is absent

Haemophilus influenzae

-

639640

the enzyme is quite labile during the course of purification, dithiothreitol and glycerol are required for stability

Haemophilus influenzae

-

639640