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Literature summary for 2.3.1.135 extracted from

  • Bussieres, S.; Cantin, L.; Salesse, C.
    Lecithin retinol acyltransferase and its S175R mutant have a similar secondary structure content and maximum insertion pressure but different enzyme activities (2011), Exp. Eye Res., 93, 778-781.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of the truncated tLRAT and its S175R mutant Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information construction of a truncated enzyme version, tLRAT, that shows enzyme activity, but leads to physiological dysfunction of the protein by causing retinis pigmentosa Homo sapiens
S175R site-directed mutagenesis, the mutation in the truncated LRAT results in an inactive enzyme. The S175R mutation has no effect on the membrane binding properties of tLRAT, the global secondary structure of tLRAT remains almost unchanged with the S175R mutation. The loss of enzymatic activity associated with the S175R mutant is related to loss of an essential nucleophile near the active site, or alternatively to steric obstruction of the active site that impedes substrate binding Homo sapiens

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of truncated tLRAT Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphatidylcholine + retinol-[cellular-retinol-binding-protein] Homo sapiens
-
2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant truncated tLRAT and its S175R mutant Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme performs formation of all-trans retinyl heptanoate from all-trans-retinol and 1,2-diheptanoyl-sn-glycero-3-phosphocholine, DHPC Homo sapiens ?
-
?
phosphatidylcholine + retinol-[cellular-retinol-binding-protein]
-
Homo sapiens 2-acylglycerophosphocholine + retinyl-ester-[cellular-retinol-binding-protein]
-
?

Synonyms

Synonyms Comment Organism
lecithin retinol acyltransferase
-
Homo sapiens
lecithin:retinol acyltransferase
-
Homo sapiens
LRAT
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
20
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Homo sapiens

General Information

General Information Comment Organism
malfunction a truncated form of LRAT as well as its S175R mutant lead to retinis pigmentosa, a severe form of retinal dystrophy Homo sapiens
additional information the catalytic triad includes histidine 60, tyrosine 154 and cysteine 161 in the LRAT structure Homo sapiens