2.3.1.135: phosphatidylcholine-retinol O-acyltransferase

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For detailed information about phosphatidylcholine-retinol O-acyltransferase, go to the full flat file.

Reaction

Synonyms

11-cis-acyl-CoA:retinol O-acyltransferase, acyltransferase, lecithin-retinol, EC 5.2.1.3, lecithin retinol acyl transferase, lecithin retinol acyltransferase, lecithin-retinol acyltransferase, lecithin/retinol acyltransferase, lecithin: retinol acyltransferase, lecithin:retinol acyl transferase, lecithin:retinol acyltransferase, LRAT, More, retinyl ester synthase, retinyl-ester synthase

ECTree

     2 Transferases

         2.3 Acyltransferases

             2.3.1 Transferring groups other than aminoacyl groups

                2.3.1.135 phosphatidylcholine-retinol O-acyltransferase

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Results	in table
19	Activating Compound
16	AA Sequence
7	Application
1	CAS Registry Number
26	Cloned(Commentary)
1	Crystallization (Commentary)
89	Disease/ Diagnostics
2	Expression
22	General Information
4	General Stability
28	Inhibitors
1	kcat/KM [mM/s]
39	KM Value [mM]
25	Localization
4	Metals/Ions
9	Molecular Weight [Da]
54	Natural Substrates/ Products (Substrates)
1	Organic Solvent Stability
136	Organism
4	Pathway
4	PDB ID
12	pH Optimum
2	pH Range
1	pH Stability
36	Protein Variants
20	Purification (Commentary)
4	Reaction
1	Reaction Type
76	Reference
139	Source Tissue
21	Specific Activity [micromol/min/mg]
3	Storage Stability
165	Substrates and Products (Substrate)
19	Subunits
86	Synonyms
1	Systematic Name
16	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
1	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.3.1.135 - phosphatidylcholine-retinol O-acyltransferase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

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

Q9JI60

736858