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Information on EC 1.17.2.2 - lupanine 17-hydroxylase (cytochrome c)
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1.17.2.2 lupanine 17-hydroxylase (cytochrome c)IUBMB Comments
The enzyme isolated from Pseudomonas putida contains heme c and requires pyrroloquinoline quinone (PQQ) for activity
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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2
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+
2
+
2
Synonyms
lupanine hydroxylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
lupanine dehydrogenase (cytochrome c)
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lupanine hydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
lupanine + 2 ferricytochrome c + H2O = 17-hydroxylupanine + 2 ferrocytochrome c + 2 H+
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SYSTEMATIC NAME
IUBMB Comments
lupanine:cytochrome c-oxidoreductase (17-hydroxylating)
The enzyme isolated from Pseudomonas putida contains heme c and requires pyrroloquinoline quinone (PQQ) for activity
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CAS REGISTRY NUMBER
COMMENTARY
39391-26-9
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
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-
?
lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
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-
?
lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
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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
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-
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lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
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
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-
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lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
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)
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
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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 + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
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
-
-
?
lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
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)
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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)
heme
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the midpoint redox potential of the heme in the purified enzyme is + 193 mV
pyrroloquinoline quinone
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contains one molecule of pyrroloquinoline quinone per molecule of enzyme
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)
pyrroloquinoline quinone
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removed from the enzyme by isoelectric focusing to give inactive apoenzyme
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
Ca2+
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
Ca2+
heme-containing inactive protein in inclusion bodies is renatured and reactivated with pyrroloquinoline quinone and Ca2+ to give active enzyme
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
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dithiothreitol
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dithiothreitol-induced reduction of LH followed by Cd2+ treatment results in significant loss of activity in a dose-dependent manner
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10
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enzyme is assayed over a range of pH from 7 to 10 in sodium/potassium phosphate, Tris/HCI and glycine/NaOH buffers
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A7D9D3N8_9GAMM
382
0
42252
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
66000
72000
74000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
protein sequence has a 26 amino acid signal sequence at the N-terminal for translocation of the protein to the periplasm
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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+
heme-containing inactive protein in inclusion bodies is renatured and reactivated with pyrroloquinoline quinone and Ca2+ to give active enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hopper, D.J.; Rogozinski, J.; Toczko, M.
Lupanine hydroxylase, a quinocytochrome c from an alkaloid-degrading Pseudomonas sp.
Biochem. J.
279
105-109
1991
Pseudomonas sp.
brenda
Hopper, D.J.; Kaderbhai, M.A.; Marriott, S.A.; Young, M.; Rogozinski, J.
Cloning, sequencing and heterologous expression of the gene for lupanine hydroxylase, a quinocytochrome c from a Pseudomonas sp.
Biochem. J.
367
483-489
2002
Pseudomonas sp. (Q934G0), Pseudomonas sp.
brenda
Hopper, D.J.; Rogozinski, J.
Redox potential of the haem c group in the quinocytochrome, lupanine hydroxylase, an enzyme located in the periplasm of a Pseudomonas sp.
Biochim. Biophys. Acta
1383
160-164
1998
Pseudomonas sp.
brenda
Hopper, D.J.; Kaderbhai, M.A.
The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida
Biochim. Biophys. Acta
1647
110-115
2003
Pseudomonas sp. (Q934G0)
brenda
Stampolidis, P.; Kaderbhai, N.N.; Kaderbhai, M.A.
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
FEMS Microbiol. Lett.
334
35-43
2012
Pseudomonas sp.
brenda
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Release 2023.1 (January 2023)
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