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Literature summary extracted from

  • Hopper, D.J.; Kaderbhai, M.A.
    The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida (2003), Biochim. Biophys. Acta, 1647, 110-115.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.17.2.2 expressed in Escherichia coli, the haemoprotein is present in amorphous inclusion bodies that are isolatable with the cell membranes, followed by centrifugation of the lysed cells Pseudomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.17.2.2 0.00087
-
 sparteine
-
 Pseudomonas sp.
1.17.2.2 0.0036
-
 lupanine
-
 Pseudomonas sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.17.2.2 periplasm
-
 Pseudomonas sp.
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.17.2.2 Ba2+ reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+. Sr2+ and Ba2+ are equally competent at reactivating the enzyme in conjunction with pyrroloquinoline quinone. Mg2 + is much less effective Pseudomonas sp.
1.17.2.2 Ca2+ reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+. Sr2+ and Ba2+ are equally competent at reactivating the enzyme in conjunction with pyrroloquinoline quinone. Mg2 + is much less effective Pseudomonas sp.
1.17.2.2 Sr2+ reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+. Sr2+ and Ba2+ are equally competent at reactivating the enzyme in conjunction with pyrroloquinoline quinone. Mg2 + is much less effective Pseudomonas sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.17.2.2 66000
-
 ultracentrifugation studies Pseudomonas sp.
1.17.2.2 72000
-
 1 * 72000, SDS-PAGE Pseudomonas sp.
1.17.2.2 72256
-
 1 * 72256, calculated from sequence Pseudomonas sp.
1.17.2.2 74000
-
 gel filtration Pseudomonas sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.17.2.2 lupanine + pyrroloquinoline quinone + H2O Pseudomonas sp. the quinohaemoprotein, contains one covalently bound haem per molecule, the C-terminal domain contains characteristics of a cytochrome c. The haem accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone) 17-hydroxylupanine + pyrroloquinoline quinol
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.17.2.2 Pseudomonas sp. Q934G0
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.17.2.2 proteolytic modification protein sequence has a 26 amino acid signal sequence at the N-terminal for translocation of the protein to the periplasm Pseudomonas sp.

Purification (Commentary)

EC Number Purification (Comment) Organism
1.17.2.2
-
 Pseudomonas sp.

Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.17.2.2 expressed in Escherichia coli, procedure is developed to renature and reactivate the enzyme, which is associated with the inclusion bodies. Reactivation requires addition of pyrroloquinoline quinone and is dependent on Ca2+ Pseudomonas sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.17.2.2 lupanine + pyrroloquinoline quinone + H2O the quinohaemoprotein, contains one covalently bound haem per molecule, the C-terminal domain contains characteristics of a cytochrome c. The haem accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone) Pseudomonas sp. 17-hydroxylupanine + pyrroloquinoline quinol
-
 ?
1.17.2.2 sparteine + pyrroloquinoline quinone + H2O
-
 Pseudomonas sp. ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.17.2.2 monomer 1 * 72000, SDS-PAGE Pseudomonas sp.
1.17.2.2 monomer 1 * 72256, calculated from sequence Pseudomonas sp.

Synonyms

EC Number Synonyms Comment Organism
1.17.2.2 lupanine hydroxylase
-
 Pseudomonas sp.

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.17.2.2 11.8
-
 sparteine
-
 Pseudomonas sp.
1.17.2.2 217
-
 lupanine
-
 Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.17.2.2 cytochrome c a quinohaemoprotein, contains one covalently bound haem per molecule, the C-terminal domain contains characteristics of a cytochrome c. The heme accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone) Pseudomonas sp.
1.17.2.2 pyrroloquinoline quinone quinohaemoprotein, contains a molecule of pyrroloquinoline quinone. The heme accepts only one electron, for the two-electron dehydrogenase reaction, a second electron acceptor must be present (pyrroloquinoline quinone) Pseudomonas sp.