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Literature summary for 5.4.99.12 extracted from

  • Gu, X.; Liu, Y.; Santi, D.V.
    The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA (1999), Proc. Natl. Acad. Sci. USA, 96, 14270-14275.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
5-fluorouracil tRNAPhe enzyme forms a covalent adduct with 5-fluorouracil-tRNA to form a putative analog of a steady-state intermediate in the normal reaction pathway. The putative Asp nucleophile is attached to the 6-position of the target 5-fluorouracil-tRNA to form a stable covalent adduct, which can undergo O-acyl hydrolytic cleavage, and the intermediate contains an intact N-glycosidic bond linking the modified base to the polynucleotide chain Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Escherichia coli P07649
-
-
Saccharomyces cerevisiae
-
-
-

Reaction

Reaction Comment Organism Reaction ID
tRNA uridine38-40 = tRNA pseudouridine38-40 the mechanism of pseudouridine synthase I is deduced from its interaction with 5-fluorouracil-tRNA. The covalent complex formed between pseudouridine synthase I and 5-fluorouracil-tRNA involves Michael adduct formation between Asp60 of pseudouridine synthase I and the 6-carbon of 5-fluorouracil39 of tRNA to form a covalent pseudouridine synthase I-5-fluorouracil-tRNA complex Escherichia coli
a

Synonyms

Synonyms Comment Organism
pseudouridine synthase I
-
 Saccharomyces cerevisiae
pseudouridine synthase I
-
 Escherichia coli