BRENDA - Enzyme Database show
show all sequences of 1.1.1.346

Optimizing an artificial metabolic pathway: engineering the cofactor specificity of Corynebacterium 2,5-diketo-D-gluconic acid reductase for use in vitamin C biosynthesis

Banta, S.; Swanson, B.A.; Wu, S.; Jarnagin, A.; Anderson, S.; Biochemistry 41, 6226-6236 (2002)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
F22Y/A272G
substrate-binding pocket double mutant with decreased kcat value for NADPH compared to the wild type enzyme
Corynebacterium sp.
F22Y/K232G/R235G/R238H/A272G
mutant with wild type kcat value for NADPH
Corynebacterium sp.
F22Y/K232G/R235T/R238H/A272G 420
mutant with decreased kcat value for NADPH compared to the wild type enzyme
Corynebacterium sp.
F22Y/K232G/R238H/A272G
mutant with decreased kcat value for NADPH compared to the wild type enzyme; the mutant exhibits activity with NADH that is more than 2 orders of magnitude higher than that of the wild type enzyme and retains a high level of activity with NADPH
Corynebacterium sp.
K232G/R238H
mutant with decreased kcat value for NADPH compared to the wild type enzyme
Corynebacterium sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
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+
-
440311
Corynebacterium sp.
2-dehydro-L-gulonate + NADP+
-
-
-
?
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.2
-
NADPH
mutant enzyme F22Y/S233T/R235S/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
3.3
-
NADPH
mutant enzyme F22Y/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
7
-
NADPH
mutant enzyme F22Y/K232G/R235G/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
7.3
-
NADPH
mutant enzyme K232G/R238H, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
18.3
-
NADPH
mutant enzyme F22Y/K232G/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C; wild type enzyme, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NADPH
the enzyme has a preference for NADPH over NADH
Corynebacterium sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADPH
the enzyme has a preference for NADPH over NADH
Corynebacterium sp.
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
F22Y/A272G
substrate-binding pocket double mutant with decreased kcat value for NADPH compared to the wild type enzyme
Corynebacterium sp.
F22Y/K232G/R235G/R238H/A272G
mutant with wild type kcat value for NADPH
Corynebacterium sp.
F22Y/K232G/R235T/R238H/A272G 420
mutant with decreased kcat value for NADPH compared to the wild type enzyme
Corynebacterium sp.
F22Y/K232G/R238H/A272G
mutant with decreased kcat value for NADPH compared to the wild type enzyme; the mutant exhibits activity with NADH that is more than 2 orders of magnitude higher than that of the wild type enzyme and retains a high level of activity with NADPH
Corynebacterium sp.
K232G/R238H
mutant with decreased kcat value for NADPH compared to the wild type enzyme
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+
-
440311
Corynebacterium sp.
2-dehydro-L-gulonate + NADP+
-
-
-
?
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.2
-
NADPH
mutant enzyme F22Y/S233T/R235S/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
3.3
-
NADPH
mutant enzyme F22Y/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
7
-
NADPH
mutant enzyme F22Y/K232G/R235G/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
7.3
-
NADPH
mutant enzyme K232G/R238H, in 100 mM Bis-Tris, pH 7.0, at 25°C
Corynebacterium sp.
18.3
-
NADPH
mutant enzyme F22Y/K232G/R238H/A272G, in 100 mM Bis-Tris, pH 7.0, at 25°C; wild type enzyme, in 100 mM Bis-Tris, pH 7.0, at 25°C
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
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1
-
1
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4
-
2
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1
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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
-
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2
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2
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6
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2
1
1
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1
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2
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1
1
2
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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
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-
-
1
1
-
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-
-
-
-
-
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1
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1
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1
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1
1
1
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1
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-
-
-
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-
-
-
-
-
-
440310
Banta
Alteration of the specificity ...
Corynebacterium sp.
Protein Eng.
15
131-140
2002
-
-
1
-
40
-
-
-
-
-
1
-
-
2
-
-
1
-
-
-
-
-
2
1
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1
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1
1
-
40
-
-
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1
-
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1
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-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
440311
Banta
Optimizing an artificial metab ...
Corynebacterium sp.
Biochemistry
41
6226-6236
2002
-
-
-
-
5
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
5
-
-
-
1
-
-
-
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-
-
1
-
5
-
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-
-
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-
-
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-
-
1
-
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5
-
-
-
-
-
-
-
-
-
-
440312
Habrych
Purification and identificatio ...
Escherichia coli, Escherichia coli BL21-(DE3)
Biotechnol. Prog.
18
257-261
2002
-
-
-
-
-
-
-
1
-
-
1
-
-
2
-
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1
-
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-
1
1
5
1
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1
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1
-
1
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-
1
-
-
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1
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1
-
-
-
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1
-
-
1
1
5
1
-
-
-
1
-
-
-
1
-
1
1
-
-
-
440307
Khurana
Molecular modeling of substrat ...
Corynebacterium sp.
Proteins
39
68-75
2000
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
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-
-
1
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-
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1
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1
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2
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1
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440306
Yum
Identification of the yqhE and ...
Escherichia coli
Appl. Environ. Microbiol.
65
3341-3346
1999
-
-
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-
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3
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8
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1
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2
1
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1
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3
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1
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2
1
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1
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-
-
-
-
-
-
-
286278
Yum
Purification and characterizat ...
Brevibacterium ketosoreductum, Brevibacterium ketosoreductum ATCC 21914
Biosci. Biotechnol. Biochem.
62
154-156
1998
-
-
-
-
-
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-
2
-
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2
-
-
2
-
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1
-
-
-
2
-
5
1
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-
1
-
1
1
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1
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1
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2
-
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2
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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
-
-
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-
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3
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1
-
-
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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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-
-
-
-
-
-
-
-
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-
-
721898
Maremonti
-
Characterisation of 2,5-diketo ...
Corynebacterium sp.
Biotechnol. Lett.
18
845-850
1996
-
-
-
-
-
-
-
1
-
-
2
-
-
1
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1
-
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2
-
1
1
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1
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1
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1
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2
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1
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2
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1
1
-
-
1
-
-
-
-
1
-
-
-
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-
-
440303
Sonoyama
-
Purification and properties of ...
Corynebacterium sp., Corynebacterium sp. SHS 0007
J. Ferment. Technol.
65
311-317
1987
-
-
-
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4
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2
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2
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1
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5
1
1
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1
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2
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1
1
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2
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1
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4
-
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2
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1
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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
-
-
-
-
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6
6
1
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2
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2
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1
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2
2
5
1
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1
2
1
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1
1
1
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1
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6
1
6
1
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2
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1
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2
2
5
1
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1
2
1
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1
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