Information on EC 2.5.1.103 - presqualene diphosphate synthase

for references in articles please use BRENDA:EC2.5.1.103
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The expected taxonomic range for this enzyme is: Botryococcus braunii

EC NUMBER
COMMENTARY hide
2.5.1.103
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RECOMMENDED NAME
GeneOntology No.
presqualene diphosphate synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2 (2E,6E)-farnesyl diphosphate = presqualene diphosphate + diphosphate
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4,4'-diapolycopenedioate biosynthesis
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botryococcenes and methylated squalene biosynthesis
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hopanoid biosynthesis (bacteria)
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staphyloxanthin biosynthesis
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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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
race B
Uniprot
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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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
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
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additional information
?
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no synthesis of squalene from presqualene diphosphate, analysis of substrate specificity, overview
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
G0Y286
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2 (2E,6E)-farnesyl diphosphate + NADPH + H+
diphosphate + presqualene diphosphate + NADP+
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene SSL-1, sequence comparisons, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
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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
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y175A
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site-sirected mutagenesis, mutant substrate specificity and activity compared to the wild-type
Y175F
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site-sirected mutagenesis, mutant substrate specificity and activity compared to the wild-type