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Literature summary for 2.1.1.34 extracted from

  • Pleshe, E.; Truesdell, J.; Batey, R.T.
    Structure of a class II TrmH tRNA-modifying enzyme from Aquifex aeolicus (2005), Acta Crystallogr. Sect. F, 61, 722-728.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
analysis reveals a fold typical of members of the SpoU clan of proteins, a subfamily of the alpha/beta-knot superfamily, with alpha-helical extensions at the N- and C-termini that are likely to be involved in tRNA binding Aquifex aeolicus

Cloned(Commentary)

Cloned (Comment) Organism
into vector pThioHisB and transformed into Escherichia coli strain DH5alpha, overexpressed in Escherichia coli Rosetta(DE3)/pLysS cells Aquifex aeolicus

Crystallization (Commentary)

Crystallization (Comment) Organism
by the hanging-drop method, at 1.85 A resolution, diffraction-quality crystals in the pH range 4.0–4.5, enzyme can not be crystallized with S-adenosyl-L-methionine or an analog in the active site Aquifex aeolicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
54000
-
gel filtration Aquifex aeolicus

Organism

Organism UniProt Comment Textmining
Aquifex aeolicus O67577
-
-

Purification (Commentary)

Purification (Comment) Organism
gel filtration, more than 99% pure Aquifex aeolicus

Subunits

Subunits Comment Organism
homodimer gel filtration Aquifex aeolicus

Synonyms

Synonyms Comment Organism
TrmH
-
Aquifex aeolicus