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Literature summary extracted from

  • Jahng, W.J.; Cheung, E.; Rando, R.R.
    Lecithin retinol acyltransferase forms functional homodimers (2002), Biochemistry, 41, 6311-6319.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.135 0.00046
-
all-trans-retinol with dipalmitoylphosphatidylcholine, chemically dimerized enzyme Bos taurus
2.3.1.135 0.00052
-
all-trans-retinol with dipalmitoylphosphatidylcholine Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.135 phosphatidylcholine + all-trans-retinol Bos taurus
-
all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.135 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.135 solubilization, centrifugation and dialysis Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.135 phosphatidylcholine + all-trans-retinol
-
Bos taurus all-trans-retinyl acyl esters + 2-acylglycerophosphocholine
-
?

Subunits

EC Number Subunits Comment Organism
2.3.1.135 homodimer SDS-PAGE in absence of 2-mercaptoethanol Bos taurus
2.3.1.135 homodimer 2 × 25300, SDS-PAGE in presence of 2-mercaptoethanol Bos taurus
2.3.1.135 monomer
-
Bos taurus
2.3.1.135 More LRAT monomer interact in membranes and form functional homodimers, the dimer formation is mediated by disulfide bond formation and protein-protein interactions Bos taurus