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show all sequences of 1.1.1.384

Combined structural and functional investigation of a C-3''-ketoreductase involved in the biosynthesis of dTDP-L-digitoxose

Kubiak, R.L.; Holden, H.M.; Biochemistry 50, 5905-5917 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Actinomadura kijaniata
Crystallization (Commentary)
Crystallization
Organism
hanging drop method of vapor diffusion, binary and ternary complexes of KijD10 with NADP+ and dTDP-benzene, 2.0 A resolution or better
Actinomadura kijaniata
Engineering
Amino acid exchange
Commentary
Organism
K102A
mutant protein is completely inactive
Actinomadura kijaniata
K102E
mutant enzyme retains some activity, but its catalytic efficiency is reduced by more than 4 orders of magnitude from that for the wild-type enzyme
Actinomadura kijaniata
K102M
mutant protein is completely inactive
Actinomadura kijaniata
K102Q
mutant protein is completely inactive
Actinomadura kijaniata
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic data are determined for mutant enzymes and wild-type enzyme
Actinomadura kijaniata
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
Actinomadura kijaniata
the enzyme is involved in the biosynthesis of dTDP-L-digitoxose
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Actinomadura kijaniata
B3TMR8
-
-
Purification (Commentary)
Commentary
Organism
-
Actinomadura kijaniata
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
the enzyme is involved in the biosynthesis of dTDP-L-digitoxose
729208
Actinomadura kijaniata
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
-
-
-
?
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose =(2R,6S)-6-hydroxy-2-methyldihydro-2H-pyran-3,4-dione
729208
Actinomadura kijaniata
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose = dTDP-2,6-dideoxy-alpha-D-threo-hexopyranos-4-ulose
-
-
?
dTDP-3-dehydro-6-deoxy-alpha D-galactose + NADPH + H+
-
729208
Actinomadura kijaniata
dTDP-fucose + NADP+
-
-
-
?
dTDP-3-dehydro-6-deoxy-alpha-D-glucose + NADPH + H+
-
729208
Actinomadura kijaniata
dTDP-quinovose + NADP+
-
-
-
?
additional information
to functioning on its natural substrate, KijD10 can also turn over sugars that contain hydroxyl groups at the C-2 and C-4 positions. It does not discriminate with respect to the orientation of the hydroxyl group at C-4
729208
Actinomadura kijaniata
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Actinomadura kijaniata
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic data are determined for mutant enzymes and wild-type enzyme
Actinomadura kijaniata
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Actinomadura kijaniata
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Actinomadura kijaniata
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging drop method of vapor diffusion, binary and ternary complexes of KijD10 with NADP+ and dTDP-benzene, 2.0 A resolution or better
Actinomadura kijaniata
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K102A
mutant protein is completely inactive
Actinomadura kijaniata
K102E
mutant enzyme retains some activity, but its catalytic efficiency is reduced by more than 4 orders of magnitude from that for the wild-type enzyme
Actinomadura kijaniata
K102M
mutant protein is completely inactive
Actinomadura kijaniata
K102Q
mutant protein is completely inactive
Actinomadura kijaniata
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic data are determined for mutant enzymes and wild-type enzyme
Actinomadura kijaniata
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
Actinomadura kijaniata
the enzyme is involved in the biosynthesis of dTDP-L-digitoxose
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Actinomadura kijaniata
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
the enzyme is involved in the biosynthesis of dTDP-L-digitoxose
729208
Actinomadura kijaniata
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
-
-
-
?
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + NADPH + H+
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose =(2R,6S)-6-hydroxy-2-methyldihydro-2H-pyran-3,4-dione
729208
Actinomadura kijaniata
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose + NADP+
dTDP-4-dehydro-2,6-dideoxy-alpha-D-glucose = dTDP-2,6-dideoxy-alpha-D-threo-hexopyranos-4-ulose
-
-
?
dTDP-3-dehydro-6-deoxy-alpha D-galactose + NADPH + H+
-
729208
Actinomadura kijaniata
dTDP-fucose + NADP+
-
-
-
?
dTDP-3-dehydro-6-deoxy-alpha-D-glucose + NADPH + H+
-
729208
Actinomadura kijaniata
dTDP-quinovose + NADP+
-
-
-
?
additional information
to functioning on its natural substrate, KijD10 can also turn over sugars that contain hydroxyl groups at the C-2 and C-4 positions. It does not discriminate with respect to the orientation of the hydroxyl group at C-4
729208
Actinomadura kijaniata
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Actinomadura kijaniata
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic data are determined for mutant enzymes and wild-type enzyme
Actinomadura kijaniata
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Actinomadura kijaniata
General Information
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of dTDP-L-digitoxose
Actinomadura kijaniata
General Information (protein specific)
General Information
Commentary
Organism
physiological function
the enzyme is involved in the biosynthesis of dTDP-L-digitoxose
Actinomadura kijaniata
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic data are determined for mutant enzymes and wild-type enzyme
Actinomadura kijaniata
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic data are determined for mutant enzymes and wild-type enzyme
Actinomadura kijaniata
Other publictions for EC 1.1.1.384
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)
729208
Kubiak
Combined structural and functi ...
Actinomadura kijaniata
Biochemistry
50
5905-5917
2011
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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
4
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1
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1
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5
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1
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1
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1
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1
731977
Hong
In vitro characterization of t ...
Saccharopolyspora spinosa
J. Am. Chem. Soc.
130
4954-4967
2008
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1
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2
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2
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1
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1
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732465
Wang
Biosynthesis of the dideoxysug ...
Streptomyces venezuelae
Microbiology
148
1091-1103
2002
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731140
Aguirrezabalaga
Identification and expression ...
Streptomyces antibioticus
Antimicrob. Agents Chemother.
44
1266-1275
2000
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1
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