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Literature summary extracted from

  • Kadziola, A.; Neuhard, J.; Larsen, S.
    Structure of product-bound Bacillus caldolyticus uracil phosphoribosyltransferase confirms ordered sequential substrate binding (2002), Acta Crystallogr. Sect. D, 58, 936-945.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.4.2.9 pharmacology potential target for the development of new antibiotics [Bacillus] caldolyticus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.2.9 DNA and amino acid sequence determination and analysis, overexpression in enzyme-deficient Escherichia coli [Bacillus] caldolyticus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.2.9 vapour diffusion using hanging or sitting drops, room temperature, protein solution 20 mg/ml, pH 7.0, 5 mM phosphate, 0.003 ml + 0.003 ml reservoir solution, pH 7.5, 6-10% polyethylene glycol 4000, 0.1 M HEPES, crystals appeared after 3 weeks, structure determination and analysis [Bacillus] caldolyticus

Organism

EC Number Organism UniProt Comment Textmining
2.4.2.9 [Bacillus] caldolyticus P70881 gene upp
-
2.4.2.9 [Bacillus] caldolyticus P70881 strain DSM 405
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.4.2.9 UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate modelling of enzyme-5-phospho-alpha-D-ribose 1-diphosphate complex [Bacillus] caldolyticus
a
2.4.2.9 UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate active sites pointing away from each other, a long arm from each monomer subunit wraps around the other subunit [Bacillus] caldolyticus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.2.9 uracil + 5-phospho-alpha-D-ribose 1-diphosphate 5-phospho-alpha-D-ribose 1-diphosphate binding site [Bacillus] caldolyticus UMP + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.4.2.9 dimer
-
 [Bacillus] caldolyticus
2.4.2.9 More three-dimensional structure [Bacillus] caldolyticus
2.4.2.9 More monomer subunit fold with UMP [Bacillus] caldolyticus
2.4.2.9 More 2 conserved sequences: Asp131-Ser139 contains the 5-phosphoribose 1-diphosphate binding motif and binds the ribose 5'-phosphate part of UMP, Tyr193-Ala201 is specific for uracil phosphoribosyltransferases and binds the uracil part of UMP [Bacillus] caldolyticus