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Literature summary extracted from

  • Wood, W.A.
    2-Keto-3-deoxy-6-phosphogluconic and related aldolases (1972), The Enzymes, 3rd Ed. (Boyer, P. D. , ed. ), 7, 281-302.
No PubMed abstract available

General Stability

EC Number General Stability Organism
4.1.2.14 highly stable when frozen in phosphate buffer Pseudomonas putida

Inhibitors

EC Number Inhibitors Comment 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 Comment Organism Structure
4.1.2.14 0.1
-
6-phospho-2-dehydro-3-deoxy-D-gluconate
-
Pseudomonas putida
4.1.3.17 0.086
-
4-hydroxy-4-methyl-2-oxoglutarate
-
Arachis hypogaea
4.1.2.23 6
-
3-deoxy-D-manno-octulosonate
-
Enterobacter cloacae

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
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 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 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] Comment Organism
4.1.2.14 72000 78000 disc gel electrophoresis Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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 UniProt Comment Textmining
4.1.2.23 Enterobacter cloacae
-
-
-
4.1.3.17 Arachis hypogaea
-
-
-
4.1.3.42 Bacteria
-
-
-
4.1.2.20 Escherichia coli
-
-
-
4.1.2.20 no activity in Bacillus subtilis
-
hexarate-grown
-
4.1.2.14 Pseudomonas putida
-
-
-
4.1.2.14 Pelomonas saccharophila
-
-
-
4.1.2.21 Pelomonas saccharophila
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.2.23
-
Enterobacter cloacae

Source Tissue

EC Number Source Tissue Comment 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] Comment Organism
4.1.2.23 additional information
-
-
Enterobacter cloacae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.2.14 additional information catalyzes decarboxylation of oxaloacetate at much slower rate than it cleaves Pseudomonas putida ?
-
?
4.1.2.14 additional information catalyzes exchange of the methyl hydrogen of pyruvate with protons of water Pseudomonas putida ?
-
?
4.1.2.14 additional information catalyzes exchange of the methyl hydrogen of pyruvate with protons of water Pelomonas saccharophila ?
-
?
4.1.2.20 additional information inducible enzyme Escherichia coli ?
-
?
4.1.2.14 2-dehydro-3-deoxy-D-gluconate 6-phosphate
-
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 Pseudomonas putida pyruvate + D-glyceraldehyde 3-phosphate
-
?
4.1.2.20 Pyruvate + D-glyceraldehyde
-
Escherichia coli ?
-
?
4.1.2.20 2-dehydro-3-deoxy-D-glucarate
-
Escherichia coli pyruvate + tartronate semialdehyde
-
?
4.1.2.20 pyruvate + tartronate semialdehyde
-
Escherichia coli 2-dehydro-3-deoxy-D-glucarate
-
?
4.1.2.20 pyruvate + tartronate semialdehyde
-
Escherichia coli 5-dehydro-4-deoxy-D-glucarate
-
?
4.1.2.20 pyruvate + glycolaldehyde
-
Escherichia coli 2-oxo-4,5-dihydroxy-L-pentanoic acid
-
?
4.1.2.20 Pyruvate + glyoxylate
-
Escherichia coli ?
-
?
4.1.2.20 Pyruvate + L-glyceraldehyde
-
Escherichia coli ?
-
?
4.1.2.21 2-dehydro-3-deoxy-D-galactonate 6-phosphate
-
Pelomonas saccharophila pyruvate + D-glyceraldehyde 3-phosphate
-
?
4.1.2.23 3-deoxy-D-manno-octulosonate
-
Enterobacter cloacae pyruvate + D-arabinose
-
?
4.1.2.23 pyruvate + D-arabinose
-
Enterobacter cloacae 3-deoxy-D-manno-octulosonate
-
?
4.1.2.23 pyruvate + D-ribose
-
Enterobacter cloacae ?
-
?
4.1.3.17 4-hydroxy-4-methyl-2-oxoglutarate
-
Arachis hypogaea pyruvate + pyruvate
-
?
4.1.3.42 4-hydroxy-2-oxoglutarate catabolism of hydroxyproline, condensation physiologically less important Bacteria ?
-
?

Subunits

EC Number Subunits Comment 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] Comment 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 Comment Organism Structure
4.1.2.14 additional information
-
additional information
-
Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment 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 Comment Organism
4.1.3.42 7.4 9.6
-
Bacteria