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Information on EC 3.1.1.64 - retinoid isomerohydrolase and Organism(s) Mus musculus and UniProt Accession Q91ZQ5
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3.1.1.64 retinoid isomerohydrolaseIUBMB 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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Word Map
- 3.1.1.64
- retinal
- epithelium
- photoreceptors
- amaurosis
- leber
- degeneration
-
vision
-
retinoids
- dystrophy
-
blind
- cone
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subretinal
-
macular
- rhodopsin
- chromophore
- 11-cis-retinal
-
adeno-associated
- pigmentosa
- erg
- opsin
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electroretinogram
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fundus
-
gucy2d
-
electroretinography
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rpe-specific
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acuity
-
epithelium-specific
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cralbp
-
goldmann
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phototransduction
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full-field
-
rpgrip1
-
rpe-like
- recoverin
-
cone-specific
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cone-dominant
-
retinaldehyde-binding
-
bruch
-
perimetry
- all-trans-retinal
-
mertk
-
cone-rod
- stargardt
-
rod-cone
- choroideremia
-
cone-mediated
- nyctalopia
-
bestrophin
-
s-cones
- retinaldehyde
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
rpe65, isomerohydrolase, retinoid isomerase, retinoid isomerohydrolase, retinol isomerase, rpe65c, 13cimh, rpe65a, all-trans-reh, retinol isomerohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
esterase, all-trans-retinol palmitate
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-
-
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Rpe65
Rpe65
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of carboxylic ester
hydrolysis of carboxylic ester
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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
106389-24-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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-
Rpe65 presents retinyl esters as substrate to the isomerase for synthesis of visual chromophore
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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in vitro, the dark-adapted form of RGR (retinal pigment epithelium-retinal G protein receptor-opsin) inhibits, but the light-adapted form has no effect on all-trans-REH
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
MYO7A protein
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the Usher 1B protein MYO7A is required for normal localization and function of the visual retinoid cycle enzyme RPE65. RPE65 normally undergoes a light-dependent translocation to become more concentrated in the central region of the RPE cells. This translocation requires MYO7A
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additional information
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enzyme activity is dependent upon the presence of Rpe65
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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activity is 2.2fold higher in light- versus dark-adapted RPE homogenates from wild-type mice
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
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in the dark, RPE65 is distributed more extensively throughout the cell, but upon exposure to light (about 100 lux, 2 h), it becomes concentrated more in the central region
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
-
outer segment discs of rod photoreceptors in Rpe65-deficient mice are disorganized, rod function is abolished although cone function remains. Rpe65-deficient mice lack rhodopsin, but not opsin apoprotein
physiological function
physiological function
deletion of RPE65 partially suppresses cone dark adaptation. Transgenic mice expressing human RPE65 in the cones reveal no morphological or functional changes between control (RPE65-deficient) and transgenic cones, with only a slight delay in dark adaptation, possibly caused by the buffering of retinoids by RPE65
physiological function
large amounts of esters accumulate in Rpe65-/- mice. Retinyl ester levels in Sv/129 wild type mice that are dark adapted for various intervals are similar to those in mice raised in cyclic light. In C57BL/6 mice, which contain less Rpe65 protein, dark adaptation is accompanied by an increase in ester levels compared to cyclic light controls. Retinyl ester levels are much higher in Rpe65-/- mice compared to wild type and keep increasing with age
physiological function
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Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle
physiological function
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the enzyme is essential for the synthesis by isomerohydrolase of 11-cis-retinal, the chromophore of rod and cone opsins
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RPE65_MOUSE
533
0
61085
Swiss-Prot
other Location (Reliability: 2)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
2 h exposure to light effects a 25% increase over dark-adapted RPE65 levels in wild type retinas
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Radu, R.A.; Hu, J.; Peng, J.; Bok, D.; Mata, N.L.; Travis, G.H.
Retinal pigment epithelium-retinal G protein receptor-opsin mediates light-dependent translocation of all-trans-retinyl esters for synthesis of visual chromophore in retinal pigment epithelial cells
J. Biol. Chem.
283
19730-19738
2008
Mus musculus
Moiseyev, G.; Crouch, R.K.; Goletz, P.; Oatis, J.; Redmond, T.M.; Ma, J.X.
Retinyl esters are the substrate for isomerohydrolase
Biochemistry
42
2229-2238
2003
Bos taurus, Mus musculus
Lyubarsky, A.L.; Savchenko, A.B.; Morocco, S.B.; Daniele, L.L.; Redmond, T.M.; Pugh, E.N.
Mole quantity of RPE65 and its productivity in the generation of 11-cis-retinal from retinyl esters in the living mouse eye
Biochemistry
44
9880-9888
2005
Mus musculus
Lopes, V.S.; Gibbs, D.; Libby, R.T.; Aleman, T.S.; Welch, D.L.; Lillo, C.; Jacobson, S.G.; Radu, R.A.; Steel, K.P.; Williams, D.S.
The Usher 1B protein, MYO7A, is required for normal localization and function of the visual retinoid cycle enzyme, RPE65
Hum. Mol. Genet.
20
2560-2570
2011
Mus musculus
Mata, N.L.; Moghrabi, W.N.; Lee, J.S.; Bui, T.V.; Radu, R.A.; Horwitz, J.; Travis, G.H.
Rpe65 is a retinyl ester binding protein that presents insoluble substrate to the isomerase in retinal pigment epithelial cells
J. Biol. Chem.
279
635-643
2004
Mus musculus
Redmond, T.M.; Yu, S.; Lee, E.; Bok, D.; Hamasaki, D.; Chen, N.; Goletz, P.; Ma, J.X.; Crouch, R.K.; Pfeifer, K.
Rpe65 is necessary for production of 11-cis-vitamin A in the retinal visual cycle
Nat. Genet.
20
344-351
1998
Mus musculus
Sheridan, C.; Boyer, N.P.; Crouch, R.K.; Koutalos, Y.
RPE65 and the accumulation of retinyl esters in mouse retinal pigment epithelium
Photochem. Photobiol.
93
844-848
2017
Mus musculus (Q91ZQ5), Mus musculus
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