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Literature summary for 3.1.1.29 extracted from

  • Fukunaga, R.; Yokoyama, S.
    Structure of the AlaX-M trans-editing enzyme from Pyrococcus horikoshii (2007), Acta Crystallogr. Sect. D, 63, 390-400.
    View publication on PubMed
Search for more literature for 3.1.1.29

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus horikoshii

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapour-diffusion method at 20°C, crystal structure is determined at 2.7 A resolution Pyrococcus horikoshii

Protein Variants

Protein Variants Comment Organism
C703A mutation abolishes editing activity Pyrococcus horikoshii

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ a zinc ion is coordinated by the conserved zinc-binding cluster in the C-domain, which is expected to be the enzymatic active site Pyrococcus horikoshii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
25000
-
 gel filtration Pyrococcus horikoshii
25300
-
 1 * 25300, calculated from sequence Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O57848
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Gly-tRNAAla + H2O
-
 Pyrococcus horikoshii Gly + tRNAAla
-
 ?
Ser-tRNAAla + H2O
-
 Pyrococcus horikoshii Ser + tRNAAla
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 25300, calculated from sequence Pyrococcus horikoshii

Synonyms

Synonyms Comment Organism
alanyl-tRNA editing protein AlaX-M
-
 Pyrococcus horikoshii
AlaX-M trans-editing enzyme
-
 Pyrococcus horikoshii
PH0108
-
 Pyrococcus horikoshii