Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.1.64 extracted from

  • Takahashi, Y.; Moiseyev, G.; Nikolaeva, O.; Ma, J.X.
    Identification of the key residues determining the product specificity of isomerohydrolase (2012), Biochemistry, 51, 4217-4225.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type enzyme and mutants in HEK-293A cells Danio rerio
recombinant expression in HEK-293A cells Gallus gallus

Protein Variants

Protein Variants Comment Organism
F103L site-directed mutagenesis, the mutation reverses the enzyme isomerization product specificity from formation of 11-cis-retinol to 13-cis-retinol, product of EC 3.1.1.90. Formation of 95.7% 13-cis-retinol and 4.3% 11-cis-retinol Danio rerio
K222M site-directed mutagenesis, the mutation reverses the enzyme isomerization product specificity from formation of 11-cis-retinol to 13-cis-retinol, product of EC 3.1.1.90. Formation of 55.1% 13-cis-retinol and 44.9% 11-cis-retinol Danio rerio
L133S site-directed mutagenesis, the mutation reverses the enzyme isomerization product specificity from formation of 11-cis-retinol to 13-cis-retinol, product of EC 3.1.1.90. Formation of 71-3% 13-cis-retinol and 28.7% 11-cis-retinol Danio rerio
Y58N site-directed mutagenesis, the mutation completely reverses the enzyme isomerization product specificity from formation of 11-cis-retinol to 13-cis-retinol, product of EC 3.1.1.90. Exclusive formation of 13-cis-retinol Danio rerio

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
an all-trans-retinyl ester + H2O Gallus gallus the enzyme generates predominantly 11-cis-retinol and a minor amount of 13-cis-retinol, from all-trans-retinyl ester 11-cis-retinol + a fatty acid
-
?
an all-trans-retinyl ester + H2O Danio rerio the enzyme generates predominantly 11-cis-retinol and a minor amount of 13-cis-retinol, from all-trans-retinyl ester 11-cis-retinol + a fatty acid
-
?

Organism

Organism UniProt Comment Textmining
Danio rerio
-
homologue RPE65c
-
Gallus gallus
-
homologue RPE65
-

Source Tissue

Source Tissue Comment Organism Textmining
epithelium
-
Gallus gallus
-
epithelium
-
Danio rerio
-
additional information enzyme homologue RPE65c is expressed in retinal Müller cells, not in the retinal pigment epithelium. Zebrafish is a cone-dominant species with 79% cones and 21% rods Danio rerio
-
Mueller cell
-
Danio rerio
-
retina
-
Gallus gallus
-
retina inner Danio rerio
-
retinal pigment epithelium
-
Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
an all-trans-retinyl ester + H2O the enzyme generates predominantly 11-cis-retinol and a minor amount of 13-cis-retinol, from all-trans-retinyl ester Gallus gallus 11-cis-retinol + a fatty acid
-
?
an all-trans-retinyl ester + H2O the enzyme generates predominantly 11-cis-retinol and a minor amount of 13-cis-retinol, from all-trans-retinyl ester Danio rerio 11-cis-retinol + a fatty acid
-
?
an all-trans-retinyl ester + H2O the enzyme generates predominantly 11-cis-retinol (72.2%) and a minor amount of 13-cis-retinol (27.8%), from all-trans-retinyl ester Danio rerio 11-cis-retinol + a fatty acid
-
?
an all-trans-retinyl ester + H2O the enzyme generates predominantly 11-cis-retinol (87.3%) and a minor amount of 13-cis-retinol (12.7%), from all-trans-retinyl ester Gallus gallus 11-cis-retinol + a fatty acid
-
?

Synonyms

Synonyms Comment Organism
isomerohydrolase
-
Gallus gallus
isomerohydrolase
-
Danio rerio
Rpe65
-
Gallus gallus
Rpe65
-
Danio rerio
RPE65c
-
Danio rerio

General Information

General Information Comment Organism
evolution it is likely that the two novel homologues of RPE65 (13cIMH and RPE65c, EC 3.1.1.90 and EC 3.1.1.64, respectively) are generated through gene duplication after the separation of fish RPE65 from the ancestral RPE65, because they exhibit an extremely high level of sequence identity (97%) and are located in the same chromosome, but on a different chromosome from RPE65 Danio rerio
additional information key residues determining the isomerization product specificity of the enzyme are Tyr58, Phe103, and Leu133 Danio rerio
physiological function the efficient recycling of the chromophore of visual pigments, 11-cis-retinal, through the retinoid visual cycle is an essential process for maintaining normal vision. RPE65 is the isomerohydrolase in retinal pigment epithelium and generates predominantly 11-cis-retinol and a minor amount of 13-cis-retinol, from all-trans-retinyl ester Gallus gallus
physiological function the efficient recycling of the chromophore of visual pigments, 11-cis-retinal, through the retinoid visual cycle is an essential process for maintaining normal vision. RPE65 is the isomerohydrolase in retinal pigment epithelium and generates predominantly 11-cis-retinol and a minor amount of 13-cis-retinol, from all-trans-retinyl ester. Enzyme homologue RPE65c expressed in the inner retina may serve as an alternative isomerohydrolase in the inner retinal visual cycle to meet the high demand for recycling of the chromophore in the cone-dominant retina Danio rerio