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Literature summary 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

Cloned(Commentary)

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.3 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

EC Number Protein Variants Comment Organism
2.4.2.3 C212S site-directed mutagenesis, the replacement has no significant effect on the loop (217-227 ARs) Shewanella oneidensis
2.4.2.3 G23A site-directed mutagenesis Shewanella oneidensis
2.4.2.3 L211Q site-directed mutagenesis Shewanella oneidensis
2.4.2.3 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
2.4.2.3 R27K site-directed mutagenesis Shewanella oneidensis
2.4.2.3 R45K site-directed mutagenesis Shewanella oneidensis
2.4.2.3 R88K site-directed mutagenesis Shewanella oneidensis
2.4.2.3 T91A site-directed mutagenesis, the replacement is nonsynonymous and leads to significant replacement of the side radical Shewanella oneidensis
2.4.2.3 T91S site-directed mutagenesis Shewanella oneidensis

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

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

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.4.2.3 homohexamer
-
 Shewanella oneidensis
2.4.2.3 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

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.2.3 37
-
 assay at Shewanella oneidensis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.2.3 7.4
-
 assay at Shewanella oneidensis

General Information

EC Number General Information Comment Organism
2.4.2.3 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