Literature summary for 2.4.2.1 extracted from

Bertosa, B.; Mikleusevic, G.; Wielgus-Kutrowska, B.; Narczyk, M.; Hajnic, M.; Lescic Asler, I.; Tomic, S.; Luic, M.; Bzowska, A.
Homooligomerization is needed for stability: a molecular modelling and solution study of Escherichia coli purine nucleoside phosphorylase (2014), FEBS J., 281, 1860-1871.

Search for more literature for 2.4.2.1

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
R117E/K121E/D139R	the mutant shows greater stability compared with the wild type dimer and changes in its structures compared with the wild type dimer in a hexamer	Escherichia coli
R117E/K121E/D139R/F120D	the mutant shows greater stability compared with the wild type dimer and changes in its structures compared with the wild type dimer in a hexamer	Escherichia coli
R117E/K121E/D139R/F120D/I128S/F131G	the mutant shows greater stability compared with the wild type dimer and changes in its structures compared with the wild type dimer in a hexamer	Escherichia coli
R117E/K121E/D139R/Y173S	the mutant shows greater stability compared with the wild type dimer and changes in its structures compared with the wild type dimer in a hexamer	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABP8	-	-

Purification (Commentary)

Purification (Comment)	Organism
Q-Sepharose column chromatography and Sephacryl S-200 gel filtration	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
7-methylguanosine + phosphate	-	Escherichia coli	7-methylguanine + alpha-D-ribose 1-phosphate	-	?
adenosine + phosphate	-	Escherichia coli	adenine + alpha-D-ribose 1-phosphate	-	?
inosine + phosphate	highest activity	Escherichia coli	hypoxanthine + alpha-D-ribose 1-phosphate	-	r

Subunits

Subunits	Comment	Organism
homohexamer	-	Escherichia coli

Synonyms

Synonyms	Comment	Organism
PNP	-	Escherichia coli
purine nucleoside phosphorylase	-	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)