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EC Tree
IUBMB Comments All-trans-retinyl esters, which are a storage form of vitamin A, are generated by the activity of EC 2.3.1.135, phosphatidylcholine---retinol O-acyltransferase (LRAT). They can be hydrolysed to 11-cis-retinol by EC 3.1.1.64, retinoid isomerohydrolase (RPE65), or to 13-cis-retinol by this enzyme.
The enzyme appears in viruses and cellular organisms
Synonyms
13-cis-isomerohydrolase,
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13-cis isomerohydrolase
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13-cis retinoid-specific isomerohydrolase
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13-cis-isomerohydrolase
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13-cis-specific isomerohydrolase
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an all-trans-retinyl fatty acyl ester + H2O = 13-cis-retinol + a fatty acid
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all-trans-retinyl ester acylhydrolase, 13-cis retinol forming
All-trans-retinyl esters, which are a storage form of vitamin A, are generated by the activity of EC 2.3.1.135, phosphatidylcholine---retinol O-acyltransferase (LRAT). They can be hydrolysed to 11-cis-retinol by EC 3.1.1.64, retinoid isomerohydrolase (RPE65), or to 13-cis-retinol by this enzyme.
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all-trans retinyl ester + H2O
11-cis retinol + ?
all-trans retinyl ester + H2O
13-cis retinol + ?
an all-trans-retinyl ester + H2O
13-cis-retinol + a fatty acid
all-trans retinyl ester + H2O
11-cis retinol + ?
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RPE65c generates predominatly 11-cis retinol and only little 13-cis retinol
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all-trans retinyl ester + H2O
11-cis retinol + ?
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all-trans retinyl ester + H2O
13-cis retinol + ?
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all-trans retinyl ester + H2O
13-cis retinol + ?
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13cIMH generates exclusively 13-cis retinol
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all-trans retinyl ester + H2O
13-cis retinol + ?
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an all-trans-retinyl ester + H2O
13-cis-retinol + a fatty acid
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the enzyme generates exclusively 13-cis-retinol
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an all-trans-retinyl ester + H2O
13-cis-retinol + a fatty acid
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the enzyme generates exclusively 13-cis-retinol, no formation of 11-cis-retinol
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an all-trans-retinyl ester + H2O
13-cis-retinol + a fatty acid
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the enzyme generates exclusively 13-cis-retinol
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?
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bipyridine
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complete inhibition at 1 mM
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0.0026
all-trans retinyl ester
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pH and temperature not specified in the publication
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0.00044
all-trans retinyl ester
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pH and temperature not specified in the publication
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brenda
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brenda
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low expression
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brenda
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high expression
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brenda
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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
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the enzyme plays a key role in the generation of 13-cis retinoic acid, as well as in the modulation of neuronal functions in the brain
additional information
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key residues determining the isomerization product specificity of the enzyme are Tyr58, Phe103, and Leu133
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RP65B_DANRE
532
0
60613
Swiss-Prot
other Location (Reliability: 2 )
RP65C_DANRE
532
0
60879
Swiss-Prot
other Location (Reliability: 2 )
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61000
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x * 61000, recombinant enzyme, SDS-PAGE
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?
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x * 61000, recombinant enzyme, SDS-PAGE
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F103L
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in terms of isomerization specificity mutant shows a substantially increases level of production of 13-cis retinol
K222M
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in terms of isomerization specificity mutant only slightly increases level of production of 13-cis retinol
L133S
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in terms of isomerization specificity mutant shows a substantially increases level of production of 13-cis retinol
Y58N
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in terms of isomerization specificity mutant generates exclusively 13-cis retinol
Y58N/F103L
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double mutant generates predominantly 11-cis retinol
F103I
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mutant produces reduced amounts of 13-cis-retinol and reduced production of 11-cis-retinol compared to wild-type
F103L
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mutant produces increased amounts of 13-cis-retinol but reduced production of 11-cis-retinol compared to wild-type
F103W
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mutant produces reduced amounts of 13-cis-retinol and reduced production of 11-cis-retinol compared to wild-type
F103Y
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mutant produces reduced amounts of 13-cis-retinol and reduced production of 11-cis-retinol compared to wild-type
F312L
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mutant shows severly impaired enzymatic activity
F312W
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mutant shows severly impaired enzymatic activity
F312Y
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mutant shows severly impaired enzymatic activity
F418A
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mutant shows severly impaired enzymatic activity
F418L
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mutant shows severly impaired enzymatic activity
F418W
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mutant shows severly impaired enzymatic activity
F418Y
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mutant shows severly impaired enzymatic activity
F526A
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mutant shows a increased production level of 13-cis-retinol compared to wild-type
F526L
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mutant shows a decreased production level of 11-cis-retinol compared to wild-type
F526W
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mutant shows a decreased production level of 11-cis-retinol compared to wild-type
F526Y
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mutant shows a decreased production level of 11-cis-retinol compared to wild-type
F61A
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mutant shows severly impaired enzymatic activity
F61L
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mutant shows severly impaired enzymatic activity
F61W
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mutant shows severly impaired enzymatic activity
F61Y
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mutant shows severly impaired enzymatic activity
Y338A
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mutant produces increased amounts of 13-cis-retinol but reduced production of 11-cis-retinol compared to wild-type
Y338F
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mutant produces similar amounts of 13-cis-retinol but reduced production of 11-cis-retinol compared to wild-type
Y338L
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mutant produces similar amounts of 13-cis-retinol but reduced production of 11-cis-retinol compared to wild-type
Y338W
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mutant produces similar amounts of 13-cis-retinol but reduced production of 11-cis-retinol compared to wild-type
L103F
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site-directed mutagenesis, site-directed mutagenesis, the mutation reverses the enzyme isomerization product specificity from formation of 13-cis-retinol to 11-cis-retinol, product of EC 3.1.1.64. Formation of 62.5% 13-cis-retinol and 37.5% 11-cis-retinol
L103F
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in terms of isomerization specificity mutant shows a highly reduced level of 13-cis retinol while increasing the level of 11-cis-retinol (compared to wild-tpye)
M222K
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site-directed mutagenesis, the mutation does not affect the enzyme isomerization product specificity of the enzyme
M222K
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in terms of isomerization specificity mutant shows no effect and generates exclusively 13-cis-retinol similar to wild-type
N58Y
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site-directed mutagenesis, the mutation completely reverses the enzyme isomerization product specificity from formation of 13-cis-retinol to 11-cis-retinol, product of EC 3.1.1.64. Formation of 28.7% 13-cis-retinol and 71.3% 11-cis-retinol
N58Y
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in terms of isomerization specificity mutant shows a highly reduced level of 13-cis retinol while increasing the level of 11-cis-retinol (compared to wild-tpye)
N58Y/L103F
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site-directed mutagenesis, the mutation does not affect the enzyme isomerization product specificity of the enzyme
N58Y/L103F
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N58Y/L103F double mutant shows a product specificity identical to that of wild-type 13cIMH
S133L
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site-directed mutagenesis, site-directed mutagenesis, the mutation reverses the enzyme isomerization product specificity from formation of 13-cis-retinol to 11-cis-retinol, product of EC 3.1.1.64. Formation of 94.4% 13-cis-retinol and 5.6% 11-cis-retinol
S133L
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in terms of isomerization specificity mutant shows only a slightly reduced level of 13-cis retinol while increasing the level of 11-cis-retinol (compared to wild-tpye)
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Ni-NTA column chromatography
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expressed in 293A-LRAT and 293T
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expressed in HEK-293A cells
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expression of wild-type enzyme and mutants in HEK-293A cells
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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
brenda
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
brenda
Chander, P.; Gentleman, S.; Poliakov, E.; Redmond, T.
Aromatic residues in the substrate cleft of RPE65 protein govern retinol isomerization and modulate its progression
J. Biol. Chem.
287
30552-30559
2012
Mus musculus
brenda
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