BRENDA - Enzyme Database

2-Keto-3-deoxy-6-phosphogluconic and related aldolases

Wood, W.A.; The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ) 7, 281-302 (1972)
No PubMed abstract available

Data extracted from this reference:

General Stability
EC Number
General Stability
Organism
4.1.2.14
highly stable when frozen in phosphate buffer
Pseudomonas putida
Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
4.1.2.14
2-Keto-3-deoxy-6-phosphogalaconate
-
Pseudomonas putida
4.1.2.14
2-keto-3-deoxygluconate
-
Pseudomonas putida
4.1.2.14
5-Keto-4-deoxyglucarate
-
Pseudomonas putida
4.1.3.17
2-oxoglutarate
-
Arachis hypogaea
4.1.3.17
pyruvate
-
Arachis hypogaea
4.1.3.42
pyruvate
competitive inhibition of glyoxylate binding
Bacteria
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.1.2.14
0.1
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
Pseudomonas putida
4.1.2.23
6
-
3-deoxy-D-manno-octulosonate
-
Enterobacter cloacae
4.1.3.17
0.086
-
4-hydroxy-4-methyl-2-oxoglutarate
-
Arachis hypogaea
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
4.1.2.20
Co2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.2.20
Fe2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.2.20
Mg2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.2.20
Mn2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.2.20
Mo2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.3.42
additional information
no requirement
Bacteria
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.1.2.14
72000
78000
disc gel electrophoresis
Pseudomonas putida
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.1.2.20
additional information
Escherichia coli
inducible enzyme
?
-
-
-
4.1.3.42
4-hydroxy-2-oxoglutarate
Bacteria
catabolism of hydroxyproline, condensation physiologically less important
?
-
-
-
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
4.1.2.14
Pelomonas saccharophila
-
-
-
4.1.2.14
Pseudomonas putida
-
-
-
4.1.2.20
Escherichia coli
-
-
-
4.1.2.20
no activity in Bacillus subtilis
-
hexarate-grown
-
4.1.2.21
Pelomonas saccharophila
-
-
-
4.1.2.23
Enterobacter cloacae
-
-
-
4.1.3.17
Arachis hypogaea
-
-
-
4.1.3.42
Bacteria
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
4.1.2.23
-
Enterobacter cloacae
Reaction
EC Number
Reaction
Commentary
Organism
4.1.2.14
2-dehydro-3-deoxy-6-phospho-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
mechanism; Schiff base formation between a lysine epsilon-amino group and carbonyl compounds 6-phospho-2-dehydro-3-deoxy-D-gluconate
Pseudomonas putida
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
4.1.3.17
cotyledon
-
Arachis hypogaea
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.1.2.23
additional information
-
-
Enterobacter cloacae
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.2.14
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
4971
Pelomonas saccharophila
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
4.1.2.14
2-dehydro-3-deoxy-D-gluconate 6-phosphate
highly specific in direction of cleavage
4971
Pseudomonas putida
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
4.1.2.14
additional information
catalyzes decarboxylation of oxaloacetate at much slower rate than it cleaves
4971
Pseudomonas putida
?
-
-
-
-
4.1.2.14
additional information
catalyzes exchange of the methyl hydrogen of pyruvate with protons of water
4971
Pseudomonas putida
?
-
-
-
-
4.1.2.14
additional information
catalyzes exchange of the methyl hydrogen of pyruvate with protons of water
4971
Pelomonas saccharophila
?
-
-
-
-
4.1.2.20
2-dehydro-3-deoxy-D-glucarate
-
4971
Escherichia coli
pyruvate + tartronate semialdehyde
-
4971
Escherichia coli
-
4.1.2.20
additional information
inducible enzyme
4971
Escherichia coli
?
-
-
-
-
4.1.2.20
Pyruvate + D-glyceraldehyde
-
4971
Escherichia coli
?
-
-
-
-
4.1.2.20
pyruvate + glycolaldehyde
-
4971
Escherichia coli
2-oxo-4,5-dihydroxy-L-pentanoic acid
-
-
-
-
4.1.2.20
Pyruvate + glyoxylate
-
4971
Escherichia coli
?
-
-
-
-
4.1.2.20
Pyruvate + L-glyceraldehyde
-
4971
Escherichia coli
?
-
-
-
-
4.1.2.20
Pyruvate + tartronate semialdehyde
-
4971
Escherichia coli
2-Dehydro-3-deoxy-D-glucarate
-
4971
Escherichia coli
-
4.1.2.20
Pyruvate + tartronate semialdehyde
-
4971
Escherichia coli
5-Dehydro-4-deoxy-D-glucarate
-
4971
Escherichia coli
-
4.1.2.21
2-dehydro-3-deoxy-D-galactonate 6-phosphate
-
4971
Pelomonas saccharophila
pyruvate + D-glyceraldehyde 3-phosphate
-
4971
Pelomonas saccharophila
-
4.1.2.23
3-deoxy-D-manno-octulosonate
-
4971
Enterobacter cloacae
pyruvate + D-arabinose
-
4971
Enterobacter cloacae
-
4.1.2.23
pyruvate + D-arabinose
-
4971
Enterobacter cloacae
3-deoxy-D-manno-octulosonate
-
4971
Enterobacter cloacae
-
4.1.2.23
pyruvate + D-ribose
-
4971
Enterobacter cloacae
?
-
-
-
-
4.1.3.17
4-hydroxy-4-methyl-2-oxoglutarate
-
4971
Arachis hypogaea
pyruvate + pyruvate
-
4971
Arachis hypogaea
-
4.1.3.42
4-hydroxy-2-oxoglutarate
catabolism of hydroxyproline, condensation physiologically less important
4971
Bacteria
?
-
-
-
-
Subunits
EC Number
Subunits
Commentary
Organism
4.1.2.14
trimer
3 * 23000-24000, SDS-PAGE
Pseudomonas putida
4.1.3.42
dimer
-
Bacteria
Temperature Stability [°C]
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
4.1.2.14
9
-
inactivation above
Pseudomonas putida
Turnover Number [1/s]
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.1.2.14
additional information
-
additional information
-
Pseudomonas putida
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.1.2.14
7.5
8.7
-
Pseudomonas putida
4.1.2.23
7
-
-
Enterobacter cloacae
4.1.3.17
9
-
and above
Arachis hypogaea
pH Range
EC Number
pH Minimum
pH Maximum
Commentary
Organism
4.1.3.42
7.4
9.6
-
Bacteria
General Stability (protein specific)
EC Number
General Stability
Organism
4.1.2.14
highly stable when frozen in phosphate buffer
Pseudomonas putida
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
4.1.2.14
2-Keto-3-deoxy-6-phosphogalaconate
-
Pseudomonas putida
4.1.2.14
2-keto-3-deoxygluconate
-
Pseudomonas putida
4.1.2.14
5-Keto-4-deoxyglucarate
-
Pseudomonas putida
4.1.3.17
2-oxoglutarate
-
Arachis hypogaea
4.1.3.17
pyruvate
-
Arachis hypogaea
4.1.3.42
pyruvate
competitive inhibition of glyoxylate binding
Bacteria
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
4.1.2.14
0.1
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
Pseudomonas putida
4.1.2.23
6
-
3-deoxy-D-manno-octulosonate
-
Enterobacter cloacae
4.1.3.17
0.086
-
4-hydroxy-4-methyl-2-oxoglutarate
-
Arachis hypogaea
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
4.1.2.20
Co2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.2.20
Fe2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.2.20
Mg2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.2.20
Mn2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.2.20
Mo2+
absolute cation requirement, activation in the order of increasing effectiveness: Mg2+, Co2+, Fe2+, Mn2+, Mo2+
Escherichia coli
4.1.3.42
additional information
no requirement
Bacteria
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
4.1.2.14
72000
78000
disc gel electrophoresis
Pseudomonas putida
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4.1.2.20
additional information
Escherichia coli
inducible enzyme
?
-
-
-
4.1.3.42
4-hydroxy-2-oxoglutarate
Bacteria
catabolism of hydroxyproline, condensation physiologically less important
?
-
-
-
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
4.1.2.23
-
Enterobacter cloacae
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
4.1.3.17
cotyledon
-
Arachis hypogaea
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
4.1.2.23
additional information
-
-
Enterobacter cloacae
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4.1.2.14
2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
4971
Pelomonas saccharophila
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
4.1.2.14
2-dehydro-3-deoxy-D-gluconate 6-phosphate
highly specific in direction of cleavage
4971
Pseudomonas putida
pyruvate + D-glyceraldehyde 3-phosphate
-
-
-
-
4.1.2.14
additional information
catalyzes decarboxylation of oxaloacetate at much slower rate than it cleaves
4971
Pseudomonas putida
?
-
-
-
-
4.1.2.14
additional information
catalyzes exchange of the methyl hydrogen of pyruvate with protons of water
4971
Pseudomonas putida
?
-
-
-
-
4.1.2.14
additional information
catalyzes exchange of the methyl hydrogen of pyruvate with protons of water
4971
Pelomonas saccharophila
?
-
-
-
-
4.1.2.20
2-dehydro-3-deoxy-D-glucarate
-
4971
Escherichia coli
pyruvate + tartronate semialdehyde
-
4971
Escherichia coli
-
4.1.2.20
additional information
inducible enzyme
4971
Escherichia coli
?
-
-
-
-
4.1.2.20
Pyruvate + D-glyceraldehyde
-
4971
Escherichia coli
?
-
-
-
-
4.1.2.20
pyruvate + glycolaldehyde
-
4971
Escherichia coli
2-oxo-4,5-dihydroxy-L-pentanoic acid
-
-
-
-
4.1.2.20
Pyruvate + glyoxylate
-
4971
Escherichia coli
?
-
-
-
-
4.1.2.20
Pyruvate + L-glyceraldehyde
-
4971
Escherichia coli
?
-
-
-
-
4.1.2.20
Pyruvate + tartronate semialdehyde
-
4971
Escherichia coli
2-Dehydro-3-deoxy-D-glucarate
-
4971
Escherichia coli
-
4.1.2.20
Pyruvate + tartronate semialdehyde
-
4971
Escherichia coli
5-Dehydro-4-deoxy-D-glucarate
-
4971
Escherichia coli
-
4.1.2.21
2-dehydro-3-deoxy-D-galactonate 6-phosphate
-
4971
Pelomonas saccharophila
pyruvate + D-glyceraldehyde 3-phosphate
-
4971
Pelomonas saccharophila
-
4.1.2.23
3-deoxy-D-manno-octulosonate
-
4971
Enterobacter cloacae
pyruvate + D-arabinose
-
4971
Enterobacter cloacae
-
4.1.2.23
pyruvate + D-arabinose
-
4971
Enterobacter cloacae
3-deoxy-D-manno-octulosonate
-
4971
Enterobacter cloacae
-
4.1.2.23
pyruvate + D-ribose
-
4971
Enterobacter cloacae
?
-
-
-
-
4.1.3.17
4-hydroxy-4-methyl-2-oxoglutarate
-
4971
Arachis hypogaea
pyruvate + pyruvate
-
4971
Arachis hypogaea
-
4.1.3.42
4-hydroxy-2-oxoglutarate
catabolism of hydroxyproline, condensation physiologically less important
4971
Bacteria
?
-
-
-
-
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
4.1.2.14
trimer
3 * 23000-24000, SDS-PAGE
Pseudomonas putida
4.1.3.42
dimer
-
Bacteria
Temperature Stability [°C] (protein specific)
EC Number
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
4.1.2.14
9
-
inactivation above
Pseudomonas putida
Turnover Number [1/s] (protein specific)
EC Number
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
4.1.2.14
additional information
-
additional information
-
Pseudomonas putida
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
4.1.2.14
7.5
8.7
-
Pseudomonas putida
4.1.2.23
7
-
-
Enterobacter cloacae
4.1.3.17
9
-
and above
Arachis hypogaea
pH Range (protein specific)
EC Number
pH Minimum
pH Maximum
Commentary
Organism
4.1.3.42
7.4
9.6
-
Bacteria