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Literature summary for 2.3.1.135 extracted from

  • Bussieres, S.; Buffeteau, T.; Desbat, B.; Breton, R.; Salesse, C.
    Secondary structure of a truncated form of lecithin retinol acyltransferase in solution and evidence for its binding and hydrolytic action in monolayers (2008), Biochim. Biophys. Acta, 1778, 1324-1334.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
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Escherichia coli BL21

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane membrane-associated protein Escherichia coli BL21 16020
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Organic Solvent Stability

Organic Solvent Comment Organism
Triton X-100 the high similarity between the secondary structure of tLRAT in the absence and the presence of Triton X-100 suggests that this detergent has no detectable effect on the structure of this protein Escherichia coli BL21

Organism

Organism UniProt Comment Textmining
Escherichia coli BL21
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-
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Purification (Commentary)

Purification (Comment) Organism
histidine-tagged truncated LRAT Escherichia coli BL21

Synonyms

Synonyms Comment Organism
lecithin retinol acyltransferase
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Escherichia coli BL21
LRAT
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Escherichia coli BL21