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show all sequences of 1.1.1.162

Cloning and sequence analysis of D-erythrulose reductase from chicken: its close structural relation to tetrameric carbonyl reductases

Maeda, M.; Kaku, H.; Shimada, M.; Nishioka, T.; Protein Eng. 15, 611-617 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
-
Gallus gallus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Gallus gallus
-
; NCBI Nucleotide:AB049356
-
Posttranslational Modification
Posttranslational Modification
Commentary
Organism
additional information
probably acetylated methionine at N-terminal
Gallus gallus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
; most abundant
Gallus gallus
-
liver
-
Gallus gallus
-
additional information
enzyme is detected in all organs tested
Gallus gallus
-
testis
-
Gallus gallus
-
Subunits
Subunits
Commentary
Organism
More
comparative modeling of enzyme based on structure of tetrameric carbonyl reductase
Gallus gallus
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Gallus gallus
Posttranslational Modification (protein specific)
Posttranslational Modification
Commentary
Organism
additional information
probably acetylated methionine at N-terminal
Gallus gallus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
; most abundant
Gallus gallus
-
liver
-
Gallus gallus
-
additional information
enzyme is detected in all organs tested
Gallus gallus
-
testis
-
Gallus gallus
-
Subunits (protein specific)
Subunits
Commentary
Organism
More
comparative modeling of enzyme based on structure of tetrameric carbonyl reductase
Gallus gallus
Other publictions for EC 1.1.1.162
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)
286093
Maeda
Cloning and sequence analysis ...
Gallus gallus
Protein Eng.
15
611-617
2002
-
-
1
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
5
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
5
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286091
Maeda
D-erythrulose reductase can al ...
Gallus gallus
J. Biochem.
123
602-606
1998
-
-
-
-
-
-
-
12
-
-
-
2
-
3
-
-
1
-
-
10
10
-
18
-
-
-
-
-
2
1
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
12
-
-
-
2
-
-
-
1
-
10
10
-
18
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
286092
Morii
Methods for enzymatic and colo ...
Bos taurus, Gallus gallus
Anal. Biochem.
151
188-191
1985
-
2
-
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
2
-
-
4
-
2
-
-
-
-
2
-
4
-
-
-
-
2
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
4
-
2
-
-
-
-
2
-
-
-
-
-
-
-
-
286086
Uehara
D-Erythrulose reductase from b ...
Bos taurus
Methods Enzymol.
89
232-237
1982
-
-
-
1
-
1
3
3
-
-
2
-
-
2
1
-
1
1
-
5
1
1
2
1
-
-
1
-
2
-
-
3
-
-
-
-
-
-
3
1
-
1
-
3
-
3
-
-
2
-
-
1
-
1
-
5
1
1
2
1
-
-
1
-
2
-
-
-
-
-
-
-
-
-
286088
Uehara
Studies on D-tetrose metabolis ...
Gallus gallus
J. Biochem.
87
47-55
1980
-
-
-
1
-
-
-
3
-
-
2
1
-
3
-
-
1
-
-
2
1
-
3
1
1
-
1
-
3
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
3
-
-
2
1
-
-
-
1
-
2
1
-
3
1
1
-
1
-
3
-
-
-
-
-
-
-
-
-
286090
Uehara
Effect of NADP+ and its analog ...
Bos taurus
J. Biochem.
85
1003-1008
1979
-
-
-
-
-
2
3
-
-
-
-
-
-
2
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
3
-
-
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286089
Uehara
Studies on D-tetrose metabolis ...
Bos taurus
J. Biochem.
78
519-526
1975
-
-
-
1
-
1
-
-
-
-
-
-
-
2
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
286087
Uehara
Studies on D-tetrose metabolis ...
Bos taurus
J. Biochem.
75
333-345
1974
-
-
-
-
-
1
-
2
-
-
2
-
-
2
-
-
1
-
-
2
1
-
2
1
-
-
3
-
2
-
-
2
-
-
-
-
-
-
2
-
-
1
-
-
-
2
-
-
2
-
-
-
-
1
-
2
1
-
2
1
-
-
3
-
2
-
-
-
-
-
-
-
-
-