Information on EC 1.17.8.1 - hydroxysqualene dehydroxylase

for references in articles please use BRENDA:EC1.17.8.1

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EC Tree 1 Oxidoreductases 1.17 Acting on CH or CH₂ groups 1.17.8 With a flavin as acceptor 1.17.8.1 hydroxysqualene dehydroxylase

IUBMB Comments

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.

The enzyme appears in viruses and cellular organisms

Reaction Schemes

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Synonyms
hpnE, more

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

hpnE

3 entries

hpnE

Rhodopseudomonas palustris

hpnE

Q56996

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

squalene + FAD + H2O = hydroxysqualene + FADH2

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PATHWAY SOURCE

PATHWAYS

MetaCyc

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.

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

Reversibility
r=reversible
ir=irreversible
?=not specified

hydroxysqualene + FADH2

squalene + FAD + H2O

2 entries

hydroxysqualene + FADH2

squalene + FAD + H2O

Rhodopseudomonas palustris

737313

Substrates: -
Products: -

hydroxysqualene + FADH2

squalene + FAD + H2O

Zymomonas mobilis

Q56996

737313

Substrates: -
Products: -

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

FAD

2 entries

FAD

Rhodopseudomonas palustris

FAD

Q56996

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only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Rhodopseudomonas palustris

737313

brenda

Zymomonas mobilis

737313

Q56996

UniProt

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

2 entries

physiological function

Rhodopseudomonas palustris

the reactions catalyzed by HpnC-HpnE constitute a three-step route for biosynthesis of squalene from farnesyl diphosphate. HpnD catalyzes formation of presqualene diphosphate from two molecules of farnesyl diphosphate, HpnC converts presqualene diphosphate to hydroxysqualene, and HpnE, a member of the amine oxidoreductase family, reduces hydroxysqualene to squalene

737313

physiological function

Zymomonas mobilis

Q56996

737313

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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).

Q6N3F3 pBLAST

HPNE_RHOPA

Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)

418

43828

Swiss-Prot