BRENDA - Enzyme Database
show all sequences of 1.1.1.264

Sequence analysis of the GntII (subsidiary) system for gluconate metabolism reveals a novel pathway for L-idonate acid catabolism in Escherichia coli

Bausch, C.; Peekhaus, N.; Utz, C.; Blais, T.; Murray, E.; Lowary, T.; Conway, T.; J. Bacteriol. 180, 3704-3710 (1998)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
overexpression in Escherichia coli
Escherichia coli
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1
-
L-Idonate
-
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-idonate + NAD(P)+
Escherichia coli
specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate
5-dehydrogluconate + NAD(P)H
-
Escherichia coli
r
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
P39346
K-12 strains, idnD gene
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition:L-idonate-grown cell
induction of enzyme synthesis by L-idonate containing culture medium
Escherichia coli
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.04
-
with NADPH as cofactor
Escherichia coli
0.05
-
with NADH as cofactor
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
L-idonate + NAD(P)+
specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate
246372
Escherichia coli
5-dehydrogluconate + NAD(P)H
-
246372
Escherichia coli
r
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
preferred cofactor
Escherichia coli
NADPH
less effective than NAD+
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression in Escherichia coli
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
preferred cofactor
Escherichia coli
NADPH
less effective than NAD+
Escherichia coli
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1
-
L-Idonate
-
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
L-idonate + NAD(P)+
Escherichia coli
specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate
5-dehydrogluconate + NAD(P)H
-
Escherichia coli
r
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition:L-idonate-grown cell
induction of enzyme synthesis by L-idonate containing culture medium
Escherichia coli
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
0.04
-
with NADPH as cofactor
Escherichia coli
0.05
-
with NADH as cofactor
Escherichia coli
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
L-idonate + NAD(P)+
specific oxidation of L-idonate with NAD+ as cofactor, involved in the degradation of L-idonate to form D-gluconate
246372
Escherichia coli
5-dehydrogluconate + NAD(P)H
-
246372
Escherichia coli
r
Other publictions for EC 1.1.1.264
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
Synonyms
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)
670701
DeBolt
L-tartaric acid synthesis from ...
Ampelopsis glandulosa var. brevipedunculata, no activity in Ampelopsis aconitifolia, Vitis californica, Vitis vinifera
Proc. Natl. Acad. Sci. USA
103
5608-5613
2006
-
-
3
-
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2
-
-
-
3
-
4
-
-
3
-
-
6
1
-
6
-
6
3
-
-
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6
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6
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-
-
-
-
3
6
-
-
-
-
-
-
2
-
-
-
3
-
-
-
3
-
6
1
-
6
-
3
-
-
-
6
-
-
-
-
-
-
-
-
-
246372
Bausch
Sequence analysis of the GntII ...
Escherichia coli
J. Bacteriol.
180
3704-3710
1998
-
-
1
-
-
-
-
1
-
-
-
1
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
1
-
-
-
1
-
-
-
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-
1
2
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285823
Adachi
-
Crystallization and properties ...
Gluconobacter oxydans
Agric. Biol. Chem.
43
75-83
1979
-
-
-
1
-
1
7
4
-
1
2
1
-
1
-
-
1
-
-
1
1
-
3
1
-
1
-
-
-
2
-
1
1
-
-
-
-
-
-
1
1
-
1
-
7
-
4
-
1
2
1
-
-
-
1
-
1
1
-
3
1
1
-
-
-
2
-
1
-
-
-
-
-
-
-
285822
Chiyonobu
-
Distribution of 2-ketogluconat ...
Acetobacter aceti, Frateuria aurantia, Gluconacetobacter liquefaciens, Gluconobacter albidus, Gluconobacter cerinus, Gluconobacter gluconicus, Gluconobacter oxydans, Gluconobacter roseus, Gluconobacter sphaericus
Agric. Biol. Chem.
39
2425-2427
1975
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-
-
-
-
-
-
-
-
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9
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9
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9
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9
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9
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9
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9
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9
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9
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-
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-
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-
-
-
-
-
-
-
-
285824
Takagi
-
A new enzyme, 5-ketoglucono-id ...
Fusarium sp.
Agric. Biol. Chem.
26
719-720
1962
-
-
-
-
-
-
2
1
-
-
-
1
-
1
-
-
1
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1
-
1
1
-
-
-
-
1
-
1
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1
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-
-
-
-
-
1
-
-
-
-
2
-
1
-
-
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1
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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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