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Information on EC 3.1.1.64 - retinoid isomerohydrolase and Organism(s) Danio rerio and UniProt Accession A9C3R8

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.1 Carboxylic-ester hydrolases
                3.1.1.64 retinoid isomerohydrolase
IUBMB Comments
This enzyme, which operates in the retinal pigment epithelium (RPE), catalyses the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol, a key step in the regeneration of the visual chromophore in the vertebrate visual cycle . Interaction of the enzyme with the membrane is critical for its enzymic activity .
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This record set is specific for:
Danio rerio
UNIPROT: A9C3R8
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Word Map
The taxonomic range for the selected organisms is: Danio rerio
The enzyme appears in selected viruses and cellular organisms
Synonyms
rpe65, isomerohydrolase, retinoid isomerase, retinoid isomerohydrolase, retinol isomerase, rpe65c, 13cimh, rpe65a, all-trans-reh, 13-cis isomerohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
RPE65c
isoform
13-cis isomerohydrolase
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esterase, all-trans-retinol palmitate
-
-
-
-
isomerohydrolase
-
-
Rpe65
RPE65a
isoform
RPE65c
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of carboxylic ester
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
all-trans-retinyl ester acylhydrolase, 11-cis retinol forming
This enzyme, which operates in the retinal pigment epithelium (RPE), catalyses the cleavage and isomerization of all-trans-retinyl fatty acid esters to 11-cis-retinol, a key step in the regeneration of the visual chromophore in the vertebrate visual cycle [4]. Interaction of the enzyme with the membrane is critical for its enzymic activity [6].
CAS REGISTRY NUMBER
COMMENTARY hide
106389-24-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 all-trans-retinyl ester + 2 H2O
11-cis-retinol + 13-cis-retinol + 2 a fatty acid
show the reaction diagram
intrinsic substrate for isoform RPE65c
-
-
?
all-trans-retinyl ester + H2O
11-cis-retinol + a fatty acid
show the reaction diagram
-
-
-
?
an all-trans retinyl ester + H2O
13-cis-retinol + a fatty acid
show the reaction diagram
specific substrate
-
-
?
an all-trans-retinyl ester + H2O
11-cis-retinol + a fatty acid
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an all-trans-retinyl ester + H2O
11-cis-retinol + a fatty acid
show the reaction diagram
-
the enzyme generates predominantly 11-cis-retinol and a minor amount of 13-cis-retinol, from all-trans-retinyl ester
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
isoform RPE65c requires iron for its enzymatic activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bipyridine
in the presence of 1 mM of the metal chelator bipyridine the enzymatic activity of isoform RPE65c is almost completely abolished
bipyridine
the addition of 6 mM FeSO4 into the iron chelator reaction restores partial enzyme activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026
an all-trans retinyl ester
pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00044
an all-trans retinyl ester
pH and temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform RPE65c
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
13cIMH expression is detected in the periventricular grey zone of the optic tectum and torus longitudinalis, at the fasciculus longitudinalis medialis in the medulla oblongata, and at the periventricular pretectum
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
isoform RPE65c is the alternative isomerohydrolase in the intra-retinal visual cycle, providing 11-cis retinal to cone photoreceptors in cone-dominant species
evolution
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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
physiological function
additional information
-
key residues determining the isomerization product specificity of the enzyme are Tyr58, Phe103, and Leu133
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
RP65C_DANRE
532
0
60879
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61000
x * 61000, estimated from SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 61000, estimated from SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA resin column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in 293A cells
expressed in 293A cells
expressed in 293A-lecithin retinol acyltransferase cells
expression of wild-type enzyme and mutants in HEK-293A cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takahashi, Y.; Moiseyev, G.; Chen, Y.; Nikolaeva, O.; Ma, J.X.
An alternative isomerohydrolase in the retinal Mueller cells of a cone-dominant species
FEBS J.
278
2913-2926
2011
Danio rerio (A9C3R8), Danio rerio (Q6PBW5), Danio rerio
Manually annotated by BRENDA team
Takahashi, Y.; Moiseyev, G.; Chen, Y.; Farjo, K.; Nikolaeva, O.; Ma, J.X.
An enzymatic mechanism for generating the precursor of endogenous 13-cis retinoic acid in the brain
FEBS J.
278
973-987
2011
Danio rerio (A9C3R9), Danio rerio
Manually annotated by BRENDA team
Takahashi, Y.; Moiseyev, G.; Nikolaeva, O.; Ma, J.X.
Identification of the key residues determining the product specificity of isomerohydrolase
Biochemistry
51
4217-4225
2012
Danio rerio, Gallus gallus
Manually annotated by BRENDA team