2.4.2.3: uridine phosphorylase
This is an abbreviated version!
For detailed information about uridine phosphorylase, go to the full flat file.
Word Map on EC 2.4.2.3
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2.4.2.3
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pyrimidine
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nucleoside
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thymidine
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uracil
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5-fluorouracil
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phosphorolysis
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salvage
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orotate
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phosphoribosyltransferase
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phosphorylases
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thymidylate
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fluoropyrimidine
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udp
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5'-deoxy-5-fluorouridine
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5-fluoro-2'-deoxyuridine
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dihydropyrimidine
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acyclonucleoside
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5-fluorouridine
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ribose-1-phosphate
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capecitabine
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5-methyluridine
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dthdpase
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fdurd
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orotidine
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dihydrouracil
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uridine-cytidine
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mete
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diagnostics
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medicine
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synthesis
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drug development
- 2.4.2.3
- pyrimidine
- nucleoside
- thymidine
- uracil
- 5-fluorouracil
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phosphorolysis
-
salvage
- orotate
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phosphoribosyltransferase
- phosphorylases
- thymidylate
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fluoropyrimidine
- udp
- 5'-deoxy-5-fluorouridine
- 5-fluoro-2'-deoxyuridine
- dihydropyrimidine
- acyclonucleoside
- 5-fluorouridine
- ribose-1-phosphate
- capecitabine
- 5-methyluridine
- dthdpase
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fdurd
- orotidine
- dihydrouracil
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uridine-cytidine
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mete
- diagnostics
- medicine
- synthesis
- drug development
Reaction
Synonyms
apUP, EC 2.4.2.23, L-UrdPase, More, PcUP1, PcUP2, phosphorylase, uridine, pynpase, pyrimidine nucleoside phosphorylase, pyrimidine phosphorylase, pyrimidine/purine nucleoside phosphorylase, StUPh, udp, UDRPase
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Subunits
Subunits on EC 2.4.2.3 - uridine phosphorylase
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dimer
isozyme UPP1, the N-terminus of the protein forms a strand-turn-strand structure bracketed by two short helices, structure, overview
hexamer
homodimer
homohexamer
monomer
tetramer
additional information
homodimer
although the homodimer's conformation of PcUP1 is equivalent to the dimer unit in the typical NP-I subfamily, it is not possible to assemble three PcUP1 dimers into the canonical hexamer as a result of a 16-amino-acid insertion in the sequence of PcUP1. This Phytophthora capsici-specific insert creates an additional secondary structural element, that protrudes into the space that would be occupied by the neighboring dimer of the canonical NP-1 hexamer, thus sterically blocking trimerization of the dimers. Trypanosoma brucei TbUP and human HsUPP1 also harbor hexamer-blocking insertions. The strictly ear-shaped conserved catalytic pocket with positive charge of PcUP1 is located on the monomer-monomer hydrophobic interface
homodimer
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although the homodimer's conformation of PcUP1 is equivalent to the dimer unit in the typical NP-I subfamily, it is not possible to assemble three PcUP1 dimers into the canonical hexamer as a result of a 16-amino-acid insertion in the sequence of PcUP1. This Phytophthora capsici-specific insert creates an additional secondary structural element, that protrudes into the space that would be occupied by the neighboring dimer of the canonical NP-1 hexamer, thus sterically blocking trimerization of the dimers. Trypanosoma brucei TbUP and human HsUPP1 also harbor hexamer-blocking insertions. The strictly ear-shaped conserved catalytic pocket with positive charge of PcUP1 is located on the monomer-monomer hydrophobic interface
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homodimer
each monomer is composed of a central 11-stranded mixed beta-sheet surrounded by 14 alpha-helices and two peripheral short, 2-stranded antiparallel beta-sheets
homohexamer
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6 * 27500, recombinant enzyme, SDS-PAGE, the quaternary structure of the VchUPh complex is a toroidal homohexamer composed of three homodimers (AB, CD, and EF), structure analysis, overview
tetramer
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4 * 26000, SDS-PAGE in presence of 4 M urea and 0.5% 2-mercaptoethanol
tetramer
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4 * 26000, SDS-PAGE in presence of 6 M urea, without 2-mercaptoethanol
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
additional information
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spatial organization of the AB homodimer of the VchUPh complex containing thymidine (THM) at the enzyme active site and a sodium ion (Na+) at the intersubunit interface. Hydrophobic residues are distributed throughout the subunit and play a key role in the formation of the structural core of the molecule. Detailed enzyme structure analysis, overview
additional information
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the VchUPh monomer consists of eight beta-strands (28% residues) and eight alpha-helices (32% residues). The arrangement of the secondary-structure elements of the subunits is characterized by a Rossmann fold with a three-layer alphabetaalpha sandwich architecture. The beta-stands form three different beta-sheets: the antiparallel sheet comprising beta2-, beta3-, and beta4-strands, the parallel sheet consisting of beta1-, beta5-, and beta8-strands, and the parallel sheet composed of beta6- and beta7-strands