Information on EC 1.17.2.2 - lupanine 17-hydroxylase (cytochrome c)

Word Map on EC 1.17.2.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Pseudomonas sp.

EC NUMBER
COMMENTARY hide
1.17.2.2
-
RECOMMENDED NAME
GeneOntology No.
lupanine 17-hydroxylase (cytochrome c)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
lupanine + 2 ferricytochrome c + H2O = 17-hydroxylupanine + 2 ferrocytochrome c + 2 H+
show the reaction diagram
-
-
-
-
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
CAS REGISTRY NUMBER
COMMENTARY hide
39391-26-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
show the reaction diagram
sparteine + pyrroloquinoline quinone + H2O
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
lupanine + pyrroloquinoline quinone + H2O
17-hydroxylupanine + pyrroloquinoline quinol
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
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)
pyrroloquinoline quinone
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
dithiothreitol-induced reduction of LH followed by Cd2+ treatment results in significant loss of activity in a dose-dependent manner
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0036 - 3.6
lupanine
0.00087
sparteine
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
21.3 - 217
lupanine
11.8
sparteine
Pseudomonas sp.
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
69.7
-
25°C, pH 8.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10
-
enzyme is assayed over a range of pH from 7 to 10 in sodium/potassium phosphate, Tris/HCI and glycine/NaOH buffers
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isoelectric focusing, pH 3-10, reduced enzyme
5.3
-
isoelectric focusing, pH 3-10, oxidized enzyme
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
66000
-
ultracentrifugation studies
72000
-
1 * 72000, SDS-PAGE
72256
-
1 * 72256, calculated from sequence
74000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
protein sequence has a 26 amino acid signal sequence at the N-terminal for translocation of the protein to the periplasm
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
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
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C124S/C143S
-
mutant displays no activity compared to wild-type
C143S
-
mutant displays only 25% activity compared to wild-type
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
-