lupanine is a quinolizidine alkaloid and is particularly abundant in species of the genus Lupinus. It can be degraded by bacteria. The first step in its catabolism by a Pseudomonas sp. is hydroxylation to 17-hydroxylupanine
lupanine is a quinolizidine alkaloid produced by plants of the genus Lupinus. It is metabolized by a Pseudomonas sp. with conversion into 17-hydroxylupanine as the first step. The enzyme involved is induced by growth of the organism on lupanine. cofactors. It catalyses the dehydrogenation of lupanine with the PQQ acting as electron acceptor and the electrons are transferred to the haem before being passed to an external acceptor. This acceptor has not yet been identified but the enzyme rapidly reduces horse heart cytochrome c. Addition of water to the dehydrogenated lupanine gives the hydroxylated product
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)
lupanine is a quinolizidine alkaloid and is particularly abundant in species of the genus Lupinus. It can be degraded by bacteria. The first step in its catabolism by a Pseudomonas sp. is hydroxylation to 17-hydroxylupanine
lupanine is a quinolizidine alkaloid produced by plants of the genus Lupinus. It is metabolized by a Pseudomonas sp. with conversion into 17-hydroxylupanine as the first step. The enzyme involved is induced by growth of the organism on lupanine. cofactors. It catalyses the dehydrogenation of lupanine with the PQQ acting as electron acceptor and the electrons are transferred to the haem before being passed to an external acceptor. This acceptor has not yet been identified but the enzyme rapidly reduces horse heart cytochrome c. Addition of water to the dehydrogenated lupanine gives the hydroxylated product
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)
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)
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)
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
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
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
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
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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+
Presence and role of a second disulphide bond in recombinant lupanine hydroxylase using site-directed mutagenesis with 143Cys/Ser and 124,143Cys/Ser mutations in Escherichia coli