Information on EC 1.17.8.1 - hydroxysqualene dehydroxylase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.17.8.1
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RECOMMENDED NAME
GeneOntology No.
hydroxysqualene dehydroxylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
squalene + FAD + H2O = hydroxysqualene + FADH2
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
hopanoid biosynthesis (bacteria)
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SYSTEMATIC NAME
IUBMB Comments
squalene:FAD oxidoreductase (hydroxylating)
This enzyme, isolated from the bacteria Rhodopseudomonas palustris and Zymomonas mobilis, participates, along with EC 2.5.1.103, presqualene diphosphate synthase, and EC 4.2.3.156, hydroxysqualene synthase, in the conversion of all-trans-farnesyl diphosphate to squalene. Eukaryotes achieve the same goal in a single step, catalysed by EC 2.5.1.21, squalene synthase.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
hydroxysqualene + FADH2
squalene + FAD + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli