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Information on EC 5.4.99.41 - lupeol synthase and Organism(s) Ricinus communis and UniProt Accession Q2XPU7

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.41 lupeol synthase
IUBMB Comments
Also forms some beta-amyrin. The recombinant enzyme from Arabidopsis thaliana gives a 1:1 mixture of lupeol and lupan-3beta,20-diol with small amounts of beta-amyrin, germanicol, taraxasterol and psi-taraxasterol. See EC 4.2.1.128 (lupan-3beta,20-diol synthase).
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This record set is specific for:
Ricinus communis
UNIPROT: Q2XPU7
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Word Map
The taxonomic range for the selected organisms is: Ricinus communis
The enzyme appears in selected viruses and cellular organisms
Synonyms
lupeol synthase, rclus, mdosc5, atlup1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
lupeol synthase
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SYSTEMATIC NAME
IUBMB Comments
(3S)-2,3-epoxy-2,3-dihydrosqualene mutase (cyclizing, lupeol-forming)
Also forms some beta-amyrin. The recombinant enzyme from Arabidopsis thaliana [3] gives a 1:1 mixture of lupeol and lupan-3beta,20-diol with small amounts of beta-amyrin, germanicol, taraxasterol and psi-taraxasterol. See EC 4.2.1.128 (lupan-3beta,20-diol synthase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,3-oxidosqualene
lupeol
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2,3-oxidosqualene
lupeol
show the reaction diagram
lupeol is the main cuticular wax compound during early stages of hypocotyl development. Enzyme is responsible for formation of the cuticular lupeol and thus for the characteristic surface properties of Rhicinus communis stems
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-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
hypocotyl portion of stem, high activity during early development
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LUPS_RICCO
769
0
88321
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
yes
functional expression in Sacchaormyces cerevisiae results in production of lupeol
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Sacchaormyces cerevisiae
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Guhling, O.; Hobl, B.; Yeats, T.; Jetter, R.
Cloning and characterization of a lupeol synthase involved in the synthesis of epicuticular wax crystals on stem and hypocotyl surfaces of Ricinus communis
Arch. Biochem. Biophys.
448
60-72
2006
Ricinus communis (Q2XPU7), Ricinus communis
Manually annotated by BRENDA team