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Literature summary for 2.3.1.135 extracted from

  • Golczak, M.; Sears, A.E.; Kiser, P.D.; Palczewski, K.
    LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3 (2015), Nat. Chem. Biol., 11, 26-32.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
2.2 A crystal structure of HRAS-like tumor suppressor 3 /LRAT chimeric enzyme in a thioester catalytic intermediate state reveals a major structural rearrangement accompanied by 3D-domain swapping dimerization not observed in native HRASLS proteins. Structural changes affecting the active site environment contribute to slower hydrolysis of the catalytic intermediate supporting efficient acyl transfer Mus musculus

Protein Variants

Protein Variants Comment Organism
additional information construction of chimeric proteins between LRAT and human HRASLS2, HRASLS3 and HRASLS4 by by replacing the native sequence of HRASLS2, 3, and 4 (residues 39-57) with the 30 aa mouse LRAT sequence 76DILLALTNDKERTQKVVSNKRLLLGVICKV106 Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q9JI60
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Synonyms

Synonyms Comment Organism
LRAT
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Mus musculus