BRENDA - Enzyme Database show
show all sequences of 1.1.1.35

Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization

Qin, Y.M.; Poutanen, M.H.; Helander, H.M.; Kvist, A.P.; Siivari, K.M.; Schmitz, W.; Conzelmann, E.; Hellman, U.; Hiltunen, J.K.; Biochem. J. 321, 21-28 (1997)

Data extracted from this reference:

Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Rattus norvegicus
-
Wistar rat
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.17
-
(S)-3-hydroxydecanoyl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I
Rattus norvegicus
4.22
-
(S)-3-hydroxybutyryl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I
Rattus norvegicus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-3-hydroxybutyryl-CoA + NAD+
-
33732
Rattus norvegicus
3-oxobutyryl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxydecanoyl-CoA + ?
-
33732
Rattus norvegicus
3-oxodecanoyl-CoA + NADH + H+
-
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.17
-
(S)-3-hydroxydecanoyl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I
Rattus norvegicus
4.22
-
(S)-3-hydroxybutyryl-CoA as substrate, activity of L-specific 3-hydroxyacyl-CoA dehydrogenase in perMFE-I
Rattus norvegicus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-3-hydroxybutyryl-CoA + NAD+
-
33732
Rattus norvegicus
3-oxobutyryl-CoA + NADH + H+
-
-
-
?
(S)-3-hydroxydecanoyl-CoA + ?
-
33732
Rattus norvegicus
3-oxodecanoyl-CoA + NADH + H+
-
-
-
?
Other publictions for EC 1.1.1.35
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)
729651
Schmid
Enzymes of the benzoyl-coenzym ...
Ferroglobus placidus, Ferroglobus placidus DSM 10642
Environ. Microbiol.
17
3289-3300
2015
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-
1
-
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2
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1
1
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1
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4
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1
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1
1
-
-
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726748
Hawkins
Conversion of 4-hydroxybutyrat ...
Metallosphaera sedula, Metallosphaera sedula DSM 5348
Appl. Environ. Microbiol.
80
2536-2545
2014
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1
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1
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1
1
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1
1
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1
1
723558
Narayan
Short-chain 3-hydroxyacyl-coen ...
Mus musculus
PLoS ONE
7
e35048
2012
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2
2
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722124
Schulz
Role of medium- and short-chai ...
Mus musculus
Endocrinology
152
4641-4651
2011
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-
1
-
1
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1
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4
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1
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3
3
-
-
-
727751
Ramos-Vera
Identification of missing gene ...
Metallosphaera sedula, Metallosphaera sedula DSM 5348
J. Bacteriol.
193
1201-1211
2011
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1
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2
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1
2
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3
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1
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2
1
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1
1
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1
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1
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1
1
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1
2
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1
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2
1
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4
1
1
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1
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1
1
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-
-
712966
Taylor
Characterization of a beta-hyd ...
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
Microbiology
156
1975-1982
2010
-
-
1
-
-
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5
4
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2
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2
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5
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1
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8
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1
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4
2
1
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3
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2
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1
3
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5
-
4
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2
-
2
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1
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-
8
-
1
-
-
4
2
1
-
2
-
2
2
-
-
-
716755
Teufel
Bacterial phenylalanine and ph ...
Escherichia coli, Pseudomonas sp., Pseudomonas sp. Y2
Proc. Natl. Acad. Sci. USA
107
14390-14395
2010
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5
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3
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3
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2
2
-
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-
695832
Chung
Microbial production of 3-hydr ...
Pseudomonas putida
Appl. Microbiol. Biotechnol.
83
513-519
2009
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-
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-
1
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3
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699171
Kapoor
3-Hydroxyacyl-coenzyme A dehyd ...
Homo sapiens
J. Clin. Endocrinol. Metab.
94
2221-2225
2009
-
1
-
-
-
-
-
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2
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1
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4
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1
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1
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4
-
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700827
Beaudoin
Functional characterization of ...
Arabidopsis thaliana
Plant Physiol.
150
1174-1191
2009
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-
1
-
1
-
1
-
1
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1
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6
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1
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1
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1
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6
-
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1
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-
684902
Filling
Role of short-chain hydroxyacy ...
Homo sapiens
Biochem. Biophys. Res. Commun.
368
6-11
2008
-
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1
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-
-
-
11
1
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3
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1
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1
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12
3
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1
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11
1
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2
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1
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12
3
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-
695470
Yang
Re: Hadh2 and 3-hydroxyacyl-Co ...
Mus musculus
Am. J. Physiol. Endocrinol. Metab.
295
E987-E987
2008
1
1
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1
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1
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684609
Liu
Production and characterizatio ...
Pseudomonas putida, Pseudomonas putida KT2442
Appl. Microbiol. Biotechnol.
76
1153-1159
2007
-
-
-
-
1
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2
-
13
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4
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1
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1
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1
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4
-
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685573
Liu
Formation of an enolate interm ...
Rattus norvegicus
Bioorg. Med. Chem. Lett.
17
3187-3190
2007
-
-
1
-
2
-
-
1
1
-
-
1
-
2
-
-
1
1
-
1
-
-
7
-
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-
1
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1
1
-
2
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1
1
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1
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1
-
1
-
-
7
-
-
-
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687573
Martens
Specificity in beta cell expre ...
Homo sapiens, Rattus norvegicus
J. Biol. Chem.
282
21134-21144
2007
-
-
-
-
2
-
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3
-
1
2
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4
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3
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4
1
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2
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1
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673264
van Hove
The HADHSC gene encoding short ...
Homo sapiens
Diabetes
55
3193-3196
2006
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-
1
-
3
-
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1
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2
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673340
He
Roles of type 10 17beta-hydrox ...
Homo sapiens
Endocr. Metab. Immune Disord. Drug Targets
6
95-102
2006
-
-
-
-
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-
2
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4
-
2
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7
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7
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7
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672317
Puyaubert
Temporal gene expression of 3- ...
Brassica napus
Biochim. Biophys. Acta
1687
152-163
2005
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1
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2
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1
2
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4
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4
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1
1
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1
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7
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2
2
2
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2
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673530
Yang
3-Hydroxyacyl-CoA dehydrogenas ...
Homo sapiens, Sus scrofa
FEBS J.
272
4874-4883
2005
-
1
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2
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1
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2
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2
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674100
Yi
Direct evidence for the functi ...
Fusarium verticillioides, Fusarium verticillioides A0149
J. Agric. Food Chem.
53
5456-5460
2005
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1
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2
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6
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1
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1
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1
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657276
Liu
Expression and purification of ...
Rattus norvegicus
Protein Expr. Purif.
37
344-351
2004
-
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1
-
3
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4
2
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1
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4
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1
1
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-
2
2
2
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4
1
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2
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1
2
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3
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4
2
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1
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1
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2
2
2
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4
1
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657049
Winkler
A new type of a multifunctiona ...
Euglena gracilis 1224-5/25, Euglena gracilis
Plant Physiol.
131
753-762
2003
-
-
-
-
-
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1
1
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5
2
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3
-
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1
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1
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4
2
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1
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1
1
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5
2
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1
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1
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4
2
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-
1
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286588
Barycki
Biochemical characterization a ...
Homo sapiens
Biochemistry
38
5786-5789
1999
-
-
1
1
-
-
-
4
1
-
1
1
-
3
-
-
-
-
-
2
1
-
1
1
-
-
-
4
-
-
-
1
-
-
-
-
-
1
1
1
-
-
-
-
-
4
1
-
1
1
-
-
-
-
-
2
1
-
1
1
-
-
-
4
-
-
-
-
-
-
-
-
-
-
286589
He
Human brain short chain L-3-hy ...
Homo sapiens
J. Biol. Chem.
274
15014-15019
1999
-
-
-
-
-
-
-
6
2
-
-
2
-
2
-
-
-
-
-
2
5
-
7
-
-
-
-
3
2
-
-
1
-
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-
1
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6
2
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2
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2
5
-
7
-
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-
3
2
-
-
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-
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-
-
-
286590
He
Molecular cloning, expression ...
Sus scrofa
Biochim. Biophys. Acta
1392
119-126
1998
-
-
1
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Noyes
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