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Literature summary extracted from

  • Seddon, A.P.; Li, L.; Meister, A.
    Resolution of 5-oxo-L-prolinase into a 5-oxo-L-proline-dependent ATPase and a coupling protein (1984), J. Biol. Chem., 259, 8091-8094.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.5.2.9 0.043
-
 5-oxo-L-proline
-
 Pseudomonas putida
3.5.2.9 0.15
-
 MgATP2-
-
 Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.9 K+
-
 Rattus norvegicus
3.5.2.9 K+ maximal activity of component A as an ATPase requires 80-300 mM Pseudomonas putida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.2.9 51000
-
 2 protein compounds, component A exhibits 5-oxo-L-proline depedent ATPase activity, component A composed of 6 heterodimers, 6 * 51000 + 6 * 64000, SDS-PAGE, component B is a coupling protein without ATPase activity, 8 * 82000, octamer, SDS-PAGE Pseudomonas putida
3.5.2.9 64000
-
 2 protein compounds, component A exhibits 5-oxo-L-proline depedent ATPase activity, component A composed of 6 heterodimers, 6 * 51000 + 6 * 64000, SDS-PAGE, component B is a coupling protein without ATPase activity, 8 * 82000, octamer, SDS-PAGE Pseudomonas putida
3.5.2.9 82000
-
 2 protein compounds, component A exhibits 5-oxo-L-proline depedent ATPase activity, component A composed of 6 heterodimers, 6 * 51000 + 6 * 64000, SDS-PAGE, component B is a coupling protein without ATPase activity, 8 * 82000, octamer, SDS-PAGE Pseudomonas putida
3.5.2.9 115000
-
 native molecular weight, component A, gel filtration Pseudomonas putida
3.5.2.9 650000
-
 component B, gel filtration, native conditions Pseudomonas putida
3.5.2.9 750000
-
 component A, gel filtration, native conditions Pseudomonas putida

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.5.2.9 5-oxo-L-proline + H2O + ATP Rattus norvegicus
-
 L-glutamate + ADP + phosphate
-
 ?
3.5.2.9 5-oxo-L-proline + H2O + ATP Pseudomonas putida
-
 L-glutamate + ADP + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.9 Pseudomonas putida
-
-
-
3.5.2.9 Rattus norvegicus
-
 rat
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.2.9
-
 Rattus norvegicus
3.5.2.9 separate purification of components A and B Pseudomonas putida

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.5.2.9 kidney
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.5.2.9 75
-
 purified component B Pseudomonas putida
3.5.2.9 243
-
 purified component A Pseudomonas putida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.9 5-oxo-L-proline + H2O + ATP
-
 Rattus norvegicus L-glutamate + ADP + phosphate
-
 ?
3.5.2.9 5-oxo-L-proline + H2O + ATP
-
 Pseudomonas putida L-glutamate + ADP + phosphate
-
 ?
3.5.2.9 L-2-oxothiazolidine-4-carboxylate + H2O + ATP
-
 Rattus norvegicus L-cysteine + ADP + phosphate
-
 ?
3.5.2.9 L-2-oxothiazolidine-4-carboxylate + H2O + ATP
-
 Pseudomonas putida L-cysteine + ADP + phosphate
-
 ?
3.5.2.9 MgATP2- + H2O
-
 Pseudomonas putida ?
-
 ?
3.5.2.9 additional information no activity observed with 5-oxo-D-proline Pseudomonas putida ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.2.9 polymer 2 protein compounds, component A exhibits 5-oxo-L-proline depedent ATPase activity, component A composed of 6 heterodimers, 6 * 51000 + 6 * 64000, SDS-PAGE, component B is a coupling protein without ATPase activity, 8 * 82000, octamer, SDS-PAGE Pseudomonas putida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.5.2.9 8.2
-
 component A-catalyzed 5-oxoproline-dependent cleavage of ATP Pseudomonas putida
3.5.2.9 9.5
-
 component B Pseudomonas putida