Lupanine 17-hydroxylase (cytochrome c)

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Lupanine 17-hydroxylase (cytochrome c)
Lupanine 17-hydroxylase (cytochrome c)
Identifiers
EC no.	1.17.2.2
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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NCBI	proteins

Last updated July 31, 2025

Lupanine 17-hydroxylase (cytochrome c) (EC 1.17.2.2, lupanine dehydrogenase (cytochrome c)) is an enzyme with systematic name lupanine:cytochrome c-oxidoreductase (17-hydroxylating).^[1]^[2] This enzyme catalyses the following chemical reaction

lupanine + 2 ferricytochrome c + H₂O

\rightleftharpoons

17-hydroxylupanine + 2 ferrocytochrome c + 2 H⁺

The enzyme isolated from Pseudomonas putida contains heme c and requires pyrroloquinoline quinone (PQQ) for activity

References

↑ Hopper DJ, Rogozinski J, Toczko M (October 1991). "Lupanine hydroxylase, a quinocytochrome c from an alkaloid-degrading Pseudomonas sp". The Biochemical Journal. 279 ( Pt 1) (Pt 1): 105–9. doi:10.1042/bj2790105. PMC 1151552 . PMID 1656935.
↑ Hopper DJ, Kaderbhai MA (April 2003). "The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647 (1–2): 110–5. doi:10.1016/s1570-9639(03)00070-0. PMID 12686118.

External links

Lupanine+17-hydroxylase+(cytochrome+c) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

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[1] Hopper DJ, Rogozinski J, Toczko M (October 1991). "Lupanine hydroxylase, a quinocytochrome c from an alkaloid-degrading Pseudomonas sp". The Biochemical Journal. 279 ( Pt 1) (Pt 1): 105–9. doi:10.1042/bj2790105. PMC 1151552 . PMID 1656935.

[2] Hopper DJ, Kaderbhai MA (April 2003). "The quinohaemoprotein lupanine hydroxylase from Pseudomonas putida". Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1647 (1–2): 110–5. doi:10.1016/s1570-9639(03)00070-0. PMID 12686118.

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[2]

v t e Other oxidoreductases (EC 1.15–1.21)
1.15: Acting on superoxide as acceptor	Superoxide dismutase SOD1 SOD2 SOD3
1.16: Oxidizing metal ions	Ceruloplasmin (Methionine synthase) reductase
1.17: Acting on CH or CH2 groups	Xanthine oxidase Ribonucleotide reductase 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase 7-Hydroxymethyl chlorophyll a reductase
1.18: Acting on iron–sulfur proteins as donors	Nitrogenase
1.19: Acting on reduced flavodoxin as donor	Nitrogenase (flavodoxin)
1.20: Acting on phosphorus or arsenic in donors	Glutaredoxin GLRX GLRX2 GLRX3 GLRX5
1.21: Acting on X-H and Y-H to form an X-Y bond	Isopenicillin N synthase Columbamine oxidase Reticuline oxidase Sulochrin oxidase (+)-bisdechlorogeodin-forming (-)-bisdechlorogeodin-forming Aureusidin synthase Tetrahydrocannabinolic acid synthase Cannabidiolic acid synthase Dichlorochromopyrrolate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)