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Literature summary for 5.4.99.12 extracted from

  • Kammen, H.; Marvel, C.; Hardy, L.; Penhoet, E.
    Purification structure and properties of Escherichia coli tRNA pseudouridine synthase I (1988), J. Biol. Chem., 263, 2255-2263.
    View publication on PubMed
Search for more literature for 5.4.99.12

Inhibitors

Inhibitors Comment Organism Structure
Dithionitrobenzoate irreversibly inactivates Escherichia coli
iodoacetate irreversibly inactivates Escherichia coli
p-chloromercuribenzoate irreversibly inactivates Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
 x * 31000, SDS-PAGE Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
isolation of virtually homogeneous tRNA pseudouridine synthase I from strains of Escherichia coli transformed with plasmid in which the production of tRNA pseudouridine synthase I is amplified 20fold Escherichia coli

Storage Stability

Storage Stability Organism
-20°C or 2°C, 50% w/v glycerol, 50% loss of activity after 2 years Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tRNA uridine38-40 purified tRNA pseudouridine synthase I modifies all of the hisT isoacceptors of tRNAHis, tRNATyr, and tRNALeu to products which are chromatographically indistinguishable from the respective wild-type species. These three groups of isoacceptors contain all the known topological sites for pseudouridine modification of residues 38,39, and 40 Escherichia coli tRNA pseudouridine38-40
-
 ?

Subunits

Subunits Comment Organism
? x * 31000, SDS-PAGE Escherichia coli

Synonyms

Synonyms Comment Organism
hisT
-
 Escherichia coli
pseudouridine synthase I
-
 Escherichia coli