Literature summary for 2.4.2.3 extracted from

Mordkovich, N.; Safonova, T.; Antipov, A.; Manuvera, V.; Polyakov, K.; Okorokova, N.; Veiko, V.
Study of structural-functional organization of nucleoside phosphorylases of gammaproteobacteria. Special aspects of functioning of uridine phosphorylase phosphate-binding site (2018), Appl. Biochem. Microbiol., 54, 12-20 .

No PubMed abstract available

Search for more literature for 2.4.2.3

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression in constructed Escherichia coli strain C600DELTAudpRecA-	Shewanella oneidensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure analysis of the active center of enzyme UDP from Shewanella oneidensis strain MR-1 in complex with uridine and sulfate (PDB ID 4R2W)	Shewanella oneidensis

Protein Variants

Protein Variants	Comment	Organism
C212S	site-directed mutagenesis, the replacement has no significant effect on the loop (217-227 ARs)	Shewanella oneidensis
G23A	site-directed mutagenesis	Shewanella oneidensis
L211Q	site-directed mutagenesis	Shewanella oneidensis
L211Q/C206S	site-directed mutagenesis, the double mutant is characterized not only by lower values of KM for phosphate with a slight increase in KM for uridine but also by the increased specific activity compared to the wild-type enzyme	Shewanella oneidensis
R27K	site-directed mutagenesis	Shewanella oneidensis
R45K	site-directed mutagenesis	Shewanella oneidensis
R88K	site-directed mutagenesis	Shewanella oneidensis
T91A	site-directed mutagenesis, the replacement is nonsynonymous and leads to significant replacement of the side radical	Shewanella oneidensis
T91S	site-directed mutagenesis	Shewanella oneidensis

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	Michaelis-Menten kinetics and Lineweaver-Burk plots	Shewanella oneidensis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
uridine + phosphate	Shewanella oneidensis	-	uracil + alpha-D-ribose 1-phosphate	-	r

Organism

Organism	UniProt	Comment	Textmining
Shewanella oneidensis	Q8E927	pyrimidine/purine nucleoside phosphorylase	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
uridine + phosphate	-	Shewanella oneidensis	uracil + alpha-D-ribose 1-phosphate	-	r

Subunits

Subunits	Comment	Organism
homohexamer	-	Shewanella oneidensis
More	some loop regions of the polypeptide chain (88-93 and 212-219 ARs) have a pronounced fluctuation motility occupying different positions relative to the protein globule in various subunits. Moreover, the C212 residue is in vicinity of the SoUDP phosphate-binding region and is a part of the 212-219 AR fluctuation region	Shewanella oneidensis

Synonyms

Synonyms	Comment	Organism
pyrimidine/purine nucleoside phosphorylase	UniProt	Shewanella oneidensis
udp	-	Shewanella oneidensis

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Shewanella oneidensis

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Shewanella oneidensis

General Information

General Information	Comment	Organism
additional information	structure of the active center of enzyme UDP from Shewanella oneidensis strain MR-1 (SoUDP) in complex with uridine and sulfate (code PDB 4R2W), structure-function analysis. In the SoUDP active center, uridine is in high-energy syn-conformation, and the ribose residue acquires a conformation close to planar	Shewanella oneidensis

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)