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Information on EC 2.5.1.103 - presqualene diphosphate synthase and Organism(s) Botryococcus braunii and UniProt Accession G0Y286

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EC Tree
IUBMB Comments
Isolated from the green alga Botryococcus braunii BOT22. Unlike EC 2.5.1.21, squalene synthase, where squalene is formed in one step from farnesyl diphosphate, in this alga the intermediate presqualene diphosphate is generated and released by this enzyme. This compound is then converted into either squalene (by EC 1.3.1.96, Botryococcus squalene synthase) or botryococcene (EC 1.3.1.97, botryococcene synthase).
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Botryococcus braunii
UNIPROT: G0Y286
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Word Map
The taxonomic range for the selected organisms is: Botryococcus braunii
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
ssl-1, squalene synthase-like, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
squalene synthase-like
-
squalene synthase
-
-
squalene synthase-like enzyme
-
-
SSL-1
SSL-2
-
isoform
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
(2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase (presqualene diphosphate forming)
Isolated from the green alga Botryococcus braunii BOT22. Unlike EC 2.5.1.21, squalene synthase, where squalene is formed in one step from farnesyl diphosphate, in this alga the intermediate presqualene diphosphate is generated and released by this enzyme. This compound is then converted into either squalene (by EC 1.3.1.96, Botryococcus squalene synthase) or botryococcene (EC 1.3.1.97, botryococcene 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 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
show the reaction diagram
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
diphosphate + presqualene diphosphate + NADP+
show the reaction diagram
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
show the reaction diagram
-
reaction of enzyme forms squalene synthase and SSL-1
-
-
?
2 geranylgeranyl diphosphate
lycopaoctaene + 2 diphosphate
show the reaction diagram
-
reaction of enzyme form SSL-2
-
-
?
presqualene diphosphate + NADPH + H+
squalene + NADP+ + diphosphate
show the reaction diagram
-
reaction of enzyme form SSL-2
-
-
?
additional information
?
-
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 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
show the reaction diagram
-
-
-
?
2 (2E,6E)-farnesyl diphosphate + NADPH + H+
diphosphate + presqualene diphosphate + NADP+
show the reaction diagram
-
-
-
?
2 (2E,6E)-farnesyl diphosphate
presqualene diphosphate + diphosphate
show the reaction diagram
-
reaction of enzyme forms squalene synthase and SSL-1
-
-
?
2 geranylgeranyl diphosphate
lycopaoctaene + 2 diphosphate
show the reaction diagram
-
reaction of enzyme form SSL-2
-
-
?
presqualene diphosphate + NADPH + H+
squalene + NADP+ + diphosphate
show the reaction diagram
-
reaction of enzyme form SSL-2
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
race B
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
SSL_1 belongs to the family of squalene synthase-like enzymes. Triterpene metabolism in Botryococcus braunii operates differently from that in other organisms. While squalene synthase, an ancient and likely progenitor to the other Botryococcus triterpene synthases, catalyzes a two-step reaction within a single enzyme unit without intermediate release, yet in Botryococcus braunii, these activities appear to have separated and evolved interdependently for specialized greater triterpene oil production into SSL-1 an SSL-2
metabolism
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PSDS_BOTBR
403
0
45953
Swiss-Prot
other Location (Reliability: 2)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y175A
site-sirected mutagenesis, mutant substrate specificity and activity compared to the wild-type
Y175F
site-sirected mutagenesis, mutant substrate specificity and activity compared to the wild-type
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene SSL-1, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
screening for squalene synthase-like genes, identification of gene SSL-1, DNA and amino acid sequence determmination and analysis, co-expression with SSL-2 leads to30fold increased squalene production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Niehaus, T.D.; Okada, S.; Devarenne, T.P.; Watt, D.S.; Sviripa, V.; Chappell, J.
Identification of unique mechanisms for triterpene biosynthesis in Botryococcus braunii
Proc. Natl. Acad. Sci. USA
108
12260-12265
2011
Botryococcus braunii (G0Y286), Botryococcus braunii
Manually annotated by BRENDA team
Bell, S.A.; Niehaus, T.D.; Nybo, S.E.; Chappell, J.
Structure-function mapping of key determinants for hydrocarbon biosynthesis by squalene and squalene synthase-like enzymes from the green alga Botryococcus braunii race B
Biochemistry
53
7570-7581
2014
Botryococcus braunii (G0Y286), Botryococcus braunii
Manually annotated by BRENDA team
Thapa, H.R.; Naik, M.T.; Okada, S.; Takada, K.; Molnar, I.; Xu, Y.; Devarenne, T.P.
A squalene synthase-like enzyme initiates production of tetraterpenoid hydrocarbons in Botryococcus braunii Race L
Nat. Commun.
7
11198
2016
Botryococcus braunii, Botryococcus braunii Race L
Manually annotated by BRENDA team