BRENDA - Enzyme Database show
show all sequences of 1.1.1.346

Alteration of the specificity of the cofactor-binding pocket of Corynebacterium 2,5-diketo-D-gluconic acid reductase A

Banta, S.; Swanson, B.A.; Wu, S.; Jarnagin, A.; Anderson, S.; Protein Eng. 15, 131-140 (2002)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
mutant enzymes are expressed in Escherichia coli JM109 cells
Corynebacterium sp.
Engineering
Amino acid exchange
Commentary
Organism
K233G
the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
K233H
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
K233M
the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
K233Q
the mutant shows wild type NADPH activity and increased NADH activity
Corynebacterium sp.
K233R
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
K233S
the mutant shows wild type NADPH activity and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
K233T
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235C
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235D
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R235E
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R235G
the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
R235H
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235M
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235N
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235Q
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235S
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235T
the mutant shows wild type NADPH activity and increased NADH activity
Corynebacterium sp.
R235Y
the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R238D
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
R238E
the mutant shows no activity with NADPH and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
R238F
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R238G
the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R238H
the mutant shows wild type NADPH activity and increased NADH activity
Corynebacterium sp.
R238N
the mutant shows reduced NADPH activity and no NADH activity
Corynebacterium sp.
R238Q
the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R238Y
the mutant shows reduced NADPH activity and increased NADH activity ompared to the wild type enzyme
Corynebacterium sp.
S233E
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
S233K
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
S233M
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
S233N
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
S233T
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
S233V
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
V234D
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234E
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234I
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234M
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234M/R235C
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234N
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234Q
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234S
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
1 * 34000, SDS-PAGE
Corynebacterium sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Corynebacterium sp.
-
-
-
Purification (Commentary)
Commentary
Organism
DEAE cellulose resin column chromatography, gel filtration
Corynebacterium sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,5-didehydro-D-gluconate + NADPH + H+
-
440310
Corynebacterium sp.
2-dehydro-L-gulonate + NADP+
-
-
-
?
additional information
the wild type enzyme shows no activity with NADH
440310
Corynebacterium sp.
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
monomer
1 * 34000, SDS-PAGE
Corynebacterium sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
dependent on
Corynebacterium sp.
Cloned(Commentary) (protein specific)
Commentary
Organism
mutant enzymes are expressed in Escherichia coli JM109 cells
Corynebacterium sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
dependent on
Corynebacterium sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
K233G
the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
K233H
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
K233M
the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
K233Q
the mutant shows wild type NADPH activity and increased NADH activity
Corynebacterium sp.
K233R
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
K233S
the mutant shows wild type NADPH activity and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
K233T
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235C
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235D
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R235E
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R235G
the mutant shows decreased NADPH activity and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
R235H
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235M
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235N
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235Q
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235S
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R235T
the mutant shows wild type NADPH activity and increased NADH activity
Corynebacterium sp.
R235Y
the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R238D
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
R238E
the mutant shows no activity with NADPH and increased NADH activity compared to the wild type enzyme
Corynebacterium sp.
R238F
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
R238G
the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R238H
the mutant shows wild type NADPH activity and increased NADH activity
Corynebacterium sp.
R238N
the mutant shows reduced NADPH activity and no NADH activity
Corynebacterium sp.
R238Q
the mutant shows reduced NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
R238Y
the mutant shows reduced NADPH activity and increased NADH activity ompared to the wild type enzyme
Corynebacterium sp.
S233E
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
S233K
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
S233M
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
S233N
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
S233T
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
S233V
the mutant shows no activity with NADPH and NADH
Corynebacterium sp.
V234D
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234E
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234I
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234M
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234M/R235C
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234N
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234Q
the mutant shows wild type NADPH activity and no NADH activity
Corynebacterium sp.
V234S
the mutant shows decreased NADPH activity compared to the wild type enzyme and no NADH activity
Corynebacterium sp.
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
1 * 34000, SDS-PAGE
Corynebacterium sp.
Purification (Commentary) (protein specific)
Commentary
Organism
DEAE cellulose resin column chromatography, gel filtration
Corynebacterium sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2,5-didehydro-D-gluconate + NADPH + H+
-
440310
Corynebacterium sp.
2-dehydro-L-gulonate + NADP+
-
-
-
?
additional information
the wild type enzyme shows no activity with NADH
440310
Corynebacterium sp.
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 34000, SDS-PAGE
Corynebacterium sp.
Other publictions for EC 1.1.1.346
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)
742259
Chen
Cloning, expression and chara ...
Comamonas testosteroni, Comamonas testosteroni ATCC 11996
Chem. Biol. Interact.
234
229-235
2015
-
-
1
-
1
-
-
-
-
-
-
4
-
2
-
-
1
-
-
-
-
-
4
1
-
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-
1
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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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4
1
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-
-
-
-
-
-
-
1
3
3
1
-
-
741575
Kaswurm
Evaluation of the food grade ...
Corynebacterium glutamicum, Corynebacterium glutamicum DSM 20301
AMB Express
3
7-17
2013
-
1
1
-
1
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
6
-
2
1
1
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1
-
-
2
-
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-
1
1
2
-
1
-
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-
2
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-
-
6
-
2
1
1
-
-
-
1
-
-
-
-
2
2
-
-
-
657308
Sanli
Structural alteration of cofac ...
Corynebacterium sp.
Protein Sci.
13
504-512
2004
-
-
-
1
1
-
-
-
-
-
-
-
-
1
-
-
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-
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-
1
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1
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1
1
1
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
440310
Banta
Alteration of the specificity ...
Corynebacterium sp.
Protein Eng.
15
131-140
2002
-
-
1
-
40
-
-
-
-
-
1
-
-
2
-
-
1
-
-
-
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
40
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
440311
Banta
Optimizing an artificial metab ...
Corynebacterium sp.
Biochemistry
41
6226-6236
2002
-
-
-
-
5
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
5
-
-
-
1
-
-
-
-
-
-
1
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
440312
Habrych
Purification and identificatio ...
Escherichia coli, Escherichia coli BL21-(DE3)
Biotechnol. Prog.
18
257-261
2002
-
-
-
-
-
-
-
1
-
-
1
-
-
2
-
-
1
-
-
-
1
1
5
1
-
-
-
1
-
-
-
1
-
1
-
-
-
-
1
-
-
-
-
-
-
1
-
-
1
-
-
-
-
1
-
-
1
1
5
1
-
-
-
1
-
-
-
1
-
1
1
-
-
-
440307
Khurana
Molecular modeling of substrat ...
Corynebacterium sp.
Proteins
39
68-75
2000
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
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-
-
1
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-
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-
1
-
2
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-
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-
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-
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-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
440306
Yum
Identification of the yqhE and ...
Escherichia coli
Appl. Environ. Microbiol.
65
3341-3346
1999
-
-
-
-
-
-
-
-
-
-
3
-
-
8
-
-
1
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-
-
-
-
2
1
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-
1
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-
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3
-
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1
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-
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-
2
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
286278
Yum
Purification and characterizat ...
Brevibacterium ketosoreductum, Brevibacterium ketosoreductum ATCC 21914
Biosci. Biotechnol. Biochem.
62
154-156
1998
-
-
-
-
-
-
-
2
-
-
2
-
-
2
-
-
1
-
-
-
2
-
5
1
-
-
-
-
1
-
1
1
-
1
-
-
-
-
1
-
-
-
-
-
-
2
-
-
2
-
-
-
-
1
-
-
2
-
5
1
-
-
-
-
1
-
1
1
-
-
-
-
-
-
440305
Khurana
Crystal structure of 2,5-diket ...
Corynebacterium sp.
Proc. Natl. Acad. Sci. USA
95
6768-6773
1998
-
-
1
1
-
-
-
-
-
-
-
-
-
3
-
-
1
-
-
-
-
-
1
-
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-
1
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1
1
1
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1
-
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1
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
721898
Maremonti
-
Characterisation of 2,5-diketo ...
Corynebacterium sp.
Biotechnol. Lett.
18
845-850
1996
-
-
-
-
-
-
-
1
-
-
2
-
-
1
-
-
1
-
-
-
2
-
1
1
-
-
1
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-
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1
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-
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-
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1
-
-
2
-
-
-
-
1
-
-
2
-
1
1
-
-
1
-
-
-
-
1
-
-
-
-
-
-
440303
Sonoyama
-
Purification and properties of ...
Corynebacterium sp., Corynebacterium sp. SHS 0007
J. Ferment. Technol.
65
311-317
1987
-
-
-
-
-
-
-
4
-
-
2
-
-
2
-
-
1
-
-
-
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5
1
1
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1
-
2
-
1
1
-
2
-
-
-
-
1
-
-
-
-
-
-
4
-
-
2
-
-
-
-
1
-
-
-
-
5
1
1
-
1
-
2
-
1
2
-
-
-
-
-
-
440304
Miller
Purification and characterizat ...
Corynebacterium sp., Corynebacterium sp. ATCC 31090
J. Biol. Chem.
262
9016-9020
1987
-
-
-
-
-
-
6
6
1
-
2
-
-
2
-
-
1
-
-
-
2
2
5
1
-
-
-
1
2
1
-
1
1
1
-
-
-
-
1
-
-
-
-
6
1
6
1
-
2
-
-
-
-
1
-
-
2
2
5
1
-
-
-
1
2
1
-
1
-
-
-
-
-
-