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show all sequences of 3.1.1.90

Identification of the key residues determining the product specificity of isomerohydrolase

Takahashi, Y.; Moiseyev, G.; Nikolaeva, O.; Ma, J.X.; Biochemistry 51, 4217-4225 (2012)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expressed in HEK-293A cells; expression of wild-type enzyme and mutants in HEK-293A cells
Danio rerio
Engineering
Amino acid exchange
Commentary
Organism
F103L
in terms of isomerization specificity mutant shows a substantially increases level of production of 13-cis retinol
Danio rerio
K222M
in terms of isomerization specificity mutant only slightly increases level of production of 13-cis retinol
Danio rerio
L103F
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
Danio rerio
L133S
in terms of isomerization specificity mutant shows a substantially increases level of production of 13-cis retinol
Danio rerio
M222K
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
Danio rerio
N58Y
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
Danio rerio
N58Y/L103F
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
Danio rerio
S133L
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
Danio rerio
Y58N
in terms of isomerization specificity mutant generates exclusively 13-cis retinol
Danio rerio
Y58N/F103L
double mutant generates predominantly 11-cis retinol
Danio rerio
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
an all-trans-retinyl ester + H2O
Danio rerio
the enzyme generates exclusively 13-cis-retinol
13-cis-retinol + a fatty acid
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Danio rerio
-
-
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
brain
-
Danio rerio
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
all-trans retinyl ester + H2O
13cIMH generates exclusively 13-cis retinol
729213
Danio rerio
13-cis retinol + ?
-
-
-
-
all-trans retinyl ester + H2O
RPE65c generates predominatly 11-cis retinol and only little 13-cis retinol
729213
Danio rerio
11-cis retinol + ?
-
-
-
-
an all-trans-retinyl ester + H2O
the enzyme generates exclusively 13-cis-retinol
729213
Danio rerio
13-cis-retinol + a fatty acid
-
-
-
?
an all-trans-retinyl ester + H2O
the enzyme generates exclusively 13-cis-retinol, no formation of 11-cis-retinol
729213
Danio rerio
13-cis-retinol + a fatty acid
-
-
-
?
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in HEK-293A cells; expression of wild-type enzyme and mutants in HEK-293A cells
Danio rerio
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F103L
in terms of isomerization specificity mutant shows a substantially increases level of production of 13-cis retinol
Danio rerio
K222M
in terms of isomerization specificity mutant only slightly increases level of production of 13-cis retinol
Danio rerio
L103F
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
Danio rerio
L133S
in terms of isomerization specificity mutant shows a substantially increases level of production of 13-cis retinol
Danio rerio
M222K
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
Danio rerio
N58Y
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
Danio rerio
N58Y/L103F
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
Danio rerio
S133L
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
Danio rerio
Y58N
in terms of isomerization specificity mutant generates exclusively 13-cis retinol
Danio rerio
Y58N/F103L
double mutant generates predominantly 11-cis retinol
Danio rerio
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
an all-trans-retinyl ester + H2O
Danio rerio
the enzyme generates exclusively 13-cis-retinol
13-cis-retinol + a fatty acid
-
-
?
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
brain
-
Danio rerio
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
all-trans retinyl ester + H2O
13cIMH generates exclusively 13-cis retinol
729213
Danio rerio
13-cis retinol + ?
-
-
-
-
all-trans retinyl ester + H2O
RPE65c generates predominatly 11-cis retinol and only little 13-cis retinol
729213
Danio rerio
11-cis retinol + ?
-
-
-
-
an all-trans-retinyl ester + H2O
the enzyme generates exclusively 13-cis-retinol
729213
Danio rerio
13-cis-retinol + a fatty acid
-
-
-
?
an all-trans-retinyl ester + H2O
the enzyme generates exclusively 13-cis-retinol, no formation of 11-cis-retinol
729213
Danio rerio
13-cis-retinol + a fatty acid
-
-
-
?
General Information
General Information
Commentary
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
General Information (protein specific)
General Information
Commentary
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
Other publictions for EC 3.1.1.90
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
729213
Takahashi
Identification of the key resi ...
Danio rerio
Biochemistry
51
4217-4225
2012
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10
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1
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4
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2
2
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732066
Chander
Aromatic residues in the subst ...
Mus musculus
J. Biol. Chem.
287
30552-30559
2012
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23
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1
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23
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714991
Takahashi
An enzymatic mechanism for gen ...
Danio rerio
FEBS J.
278
973-987
2011
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