Information on EC 3.1.1.90 - all-trans-retinyl ester 13-cis isomerohydrolase

for references in articles please use BRENDA:EC3.1.1.90
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.1.90
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RECOMMENDED NAME
GeneOntology No.
all-trans-retinyl ester 13-cis isomerohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an all-trans-retinyl ester + H2O = 13-cis-retinol + a fatty acid
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
all-trans retinyl ester + H2O
11-cis retinol + ?
show the reaction diagram
all-trans retinyl ester + H2O
13-cis retinol + ?
show the reaction diagram
an all-trans-retinyl ester + H2O
13-cis-retinol + a fatty acid
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
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
13-cis-retinol + a fatty acid
show the reaction diagram
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the enzyme generates exclusively 13-cis-retinol
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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dependent on
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bipyridine
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complete inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0026
all-trans retinyl ester
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pH and temperature not specified in the publication
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00044
all-trans retinyl ester
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pH and temperature not specified in the publication
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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low expression
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
61000
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x * 61000, recombinant enzyme, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 61000, recombinant enzyme, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in 293A-LRAT and 293T
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expressed in HEK-293A cells; expression of wild-type enzyme and mutants in HEK-293A cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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); 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
L133S
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in terms of isomerization specificity mutant shows a substantially increases level of production of 13-cis retinol
M222K
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in terms of isomerization specificity mutant shows no effect and generates exclusively 13-cis-retinol similar to wild-type; site-directed mutagenesis, the mutation does not affect the enzyme isomerization product specificity of the enzyme
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); 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/L103F
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N58Y/L103F double mutant shows a product specificity identical to that of wild-type 13cIMH; site-directed mutagenesis, the mutation does not affect the enzyme isomerization product specificity of the enzyme
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); 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
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