BRENDA - Enzyme Database show
show all sequences of 1.14.14.80

Marmoset cytochrome P450 4A11, a novel arachidonic acid and lauric acid omega-hydroxylase expressed in liver and kidney tissues

Uehara, S.; Uno, Y.; Ishii, S.; Inoue, T.; Sasaki, E.; Yamazaki, H.; Xenobiotica 47, 553-561 (2017)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene CYPP4504A11, located on chromosome 7, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time RT PCR enzyme expression analysis, recombinant expression in Escherichia coli
Callithrix jacchus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Callithrix jacchus
-
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
in heme
Callithrix jacchus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
Callithrix jacchus
-
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
Callithrix jacchus
-
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
additional information
Callithrix jacchus
Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Callithrix jacchus
A0A1P8NQJ7
white-tufted-ear marmoset
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
highest expression level
Callithrix jacchus
-
liver
-
Callithrix jacchus
-
additional information
expression pattern by real-time RT PCR and immunoblottig. No expression in brains, lungs, and small intestines
Callithrix jacchus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
-
746560
Callithrix jacchus
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
-
746560
Callithrix jacchus
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes
746560
Callithrix jacchus
?
-
-
-
-
additional information
the enzyme sequence contains consensus sequences of six substrate recognition sites. Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes. CYP4A11 hydroxylates fatty acids at their omega and omega-1 positions
746560
Callithrix jacchus
?
-
-
-
-
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Callithrix jacchus
heme
the enzyme contains one heme-binding domain
Callithrix jacchus
NADPH
-
Callithrix jacchus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene CYPP4504A11, located on chromosome 7, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, real-time RT PCR enzyme expression analysis, recombinant expression in Escherichia coli
Callithrix jacchus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome P450
-
Callithrix jacchus
heme
the enzyme contains one heme-binding domain
Callithrix jacchus
NADPH
-
Callithrix jacchus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
microsome
-
Callithrix jacchus
-
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
in heme
Callithrix jacchus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
Callithrix jacchus
-
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
Callithrix jacchus
-
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
?
additional information
Callithrix jacchus
Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
highest expression level
Callithrix jacchus
-
liver
-
Callithrix jacchus
-
additional information
expression pattern by real-time RT PCR and immunoblottig. No expression in brains, lungs, and small intestines
Callithrix jacchus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
arachidonic acid + [reduced NADPH-hemoprotein reductase] + O2
-
746560
Callithrix jacchus
20-hydroxyarachidonic acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
lauric acid + [reduced NADPH-hemoprotein reductase] + O2
-
746560
Callithrix jacchus
12-hydroxylauric acid + [oxidized NADPH-hemoprotein reductase] + H2O
-
-
-
?
additional information
Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes
746560
Callithrix jacchus
?
-
-
-
-
additional information
the enzyme sequence contains consensus sequences of six substrate recognition sites. Marmoset CYP4A11 enzyme heterologously expressed in Escherichia coli preferentially catalyzes the omega-hydroxylation of arachidonic acid and lauric acid, similar to enzymes from Macaca fascicularis and Homo sapiens. The lauric acid omega-hydroxylation activity of marmoset CYP4A11 is low compared with those of marmoset liver microsomes. CYP4A11 hydroxylates fatty acids at their omega and omega-1 positions
746560
Callithrix jacchus
?
-
-
-
-
Other publictions for EC 1.14.14.80
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)
746320
Zhang
Ablation of cytochrome P450 o ...
Mus musculus
Proc. Natl. Acad. Sci. USA
114
3181-3185
2017
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1
1
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746560
Uehara
Marmoset cytochrome P450 4A11 ...
Callithrix jacchus
Xenobiotica
47
553-561
2017
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1
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1
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4
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3
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4
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3
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1
3
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1
1
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3
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3
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4
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744773
Han
Biochemical analysis of recom ...
Homo sapiens
Drug Metab. Pharmacokinet.
31
445-450
2016
1
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1
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3
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17
-
1
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3
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1
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1
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2
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3
1
1
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17
1
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3
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1
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1
3
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3
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17
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1
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3
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1
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2
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3
1
1
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17
1
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18
18
746057
Bjelica
Fatty acid omega-hydroxylases ...
Solanum tuberosum
Plant Cell Rep.
35
2435-2448
2016
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4
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1
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1
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1
1
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744772
Saito
Functional characterization o ...
Homo sapiens
Drug Metab. Pharmacokinet.
30
119-122
2015
-
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1
-
9
-
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7
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1
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1
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1
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1
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9
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7
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1
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1
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733174
Huang
Expression and characterizatio ...
Starmerella bombicola
Appl. Environ. Microbiol.
80
766-776
2014
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3
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6
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14
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1
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14
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1
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1
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1
1
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744097
Huang
Expression and characterizati ...
Starmerella bombicola, Starmerella bombicola ATCC 22214
Appl. Environ. Microbiol.
80
766-776
2014
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1
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3
1
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28
-
9
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1
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36
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2
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1
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2
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3
6
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3
3
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28
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3
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36
-
3
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3
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2
6
-
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744323
Kim
Kinetic analysis of lauric ac ...
Homo sapiens
Biochemistry
53
6161-6172
2014
1
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2
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2
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2
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703412
Nakano
Expression and characterizatio ...
Homo sapiens
Drug Metab. Dispos.
37
2119-2122
2009
-
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1
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1
3
1
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1
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1
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1
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1
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1
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1
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1
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1
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4
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1
1
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-
706321
Dobritsa
CYP704B1 is a long-chain fatty ...
Arabidopsis thaliana
Plant Physiol.
151
574-589
2009
-
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1
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3
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2
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7
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1
1
1
1
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733891
Van Bogaert
Importance of the cytochrome P ...
Starmerella bombicola
FEMS Yeast Res.
9
87-94
2009
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3
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1
1
1
1
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734431
Gatica
P450 CYP2C epoxygenase and CYP ...
Rattus norvegicus
J. Lipid Res.
48
924-934
2007
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1
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1
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676666
Benveniste
Evolutionary relationship and ...
Arabidopsis thaliana
Plant Sci.
170
326-338
2006
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1
1
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734950
Duan
Differential expression and ev ...
Arabidopsis thaliana
Plant Physiol.
137
1067-1081
2005
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15
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5
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2
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8
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285382
Hoch
Structural determination of th ...
Homo sapiens, Rattus norvegicus
Arch. Biochem. Biophys.
373
63-71
2000
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2
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1
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13
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8
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2
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25
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21
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5
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2
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14
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5
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25
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24
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733243
Benveniste
CYP86A1 from Arabidopsis thali ...
Arabidopsis thaliana
Biochem. Biophys. Res. Commun.
243
688-693
1998
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6
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734106
Hiratsuka
Sex and strain differences in ...
Mus musculus
J. Biochem.
119
340-345
1996
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3
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1
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734105
Kawashima
Purification and cDNA cloning ...
Homo sapiens
J. Biochem.
116
74-80
1994
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1
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