Botryococcus braunii is a green, pyramid-shaped planktonic microalga that is of potentially great importance in the field of biotechnology. Colonies held together by a lipid biofilm matrix can be found in temperate or tropical oligotrophic lakes and estuaries, and will bloom when in the presence of elevated levels of dissolved inorganic phosphorus. The species is notable for its ability to produce high amounts of hydrocarbons, especially oils in the form of Triterpenes, that are typically around 30–40% of their dry weight. Compared to other green alge species it has a relatively thick cell wall that is accumulated from previous cellular divisions; making extraction of cytoplasmic components rather difficult. Much of the useful hydrocarbon oil is outside of the cell.
Botryococcus is a genus of green algae. The cells form an irregularly shaped aggregate. Thin filaments connect the cells. The cell body is ovoid, 6 to 10 μm long, and 3 to 6 μm wide. Fossils of the genus are known since Precambrian times, and form the single largest biological contributor to crude oil, and are a major component of oil shales.
In enzymology, a GDP-L-fucose synthase (EC 1.1.1.271) is an enzyme that catalyzes the chemical reaction
In enzymology, a secologanin synthase (EC 1.14.19.62, was wrongly classified as EC 1.3.3.9 in the past) is an enzyme that catalyzes the chemical reaction
[Methionine synthase] reductase, or Methionine synthase reductase, encoded by the gene MTRR, is an enzyme that is responsible for the reduction of methionine synthase inside human body. This enzyme is crucial for maintaining the one carbon metabolism, specifically the folate cycle. The enzyme employs one coenzyme, flavoprotein.
In enzymology, a glutamate synthase (NADPH) (EC 1.4.1.13) is an enzyme that catalyzes the chemical reaction
In enzymology, bornyl diphosphate synthase (BPPS) (EC 5.5.1.8) is an enzyme that catalyzes the chemical reaction
Phytoene synthase is a transferase enzyme involved in the biosynthesis of carotenoids. It catalyzes the conversion of geranylgeranyl pyrophosphate to phytoene. This enzyme catalyses the following chemical reaction
Botryococcus squalene synthase (EC 1.3.1.96, SSL-2 (gene)) is an enzyme with systematic name squalene:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction
Squalene methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:squalene C-methyltransferase. This enzyme catalyses the following chemical reaction
Botryococcene C-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:botryococcene C-methyltransferase.
Geranylfarnesyl diphosphate synthase is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transtransferase . This enzyme catalyses the following chemical reaction
Hexaprenyl diphosphate synthase is an enzyme with systematic name geranylgeranyl-diphosphate:isopentenyl-diphosphate transferase . This enzyme catalyses the following chemical reaction
4,4'-diapophytoene synthase is an enzyme with systematic name farnesyl-diphosphate:farnesyl-diphosphate farnesyltransferase . This enzyme catalyses the following chemical reaction
Presqualene diphosphate synthase is an enzyme with systematic name (2E,6E)-farnesyl-diphosphate:(2E,6E)-farnesyl-diphosphate farnesyltransferase . This enzyme catalyses the following chemical reaction
The squalene/phytoene synthase family represents proteins that catalyze the head-to-head condensation of C15 and C20 prenyl units (i.e. farnesyl diphosphate and genranylgeranyl diphosphate). This enzymatic step constitutes part of steroid and carotenoid biosynthesis pathway. Squalene synthase EC (SQS) and Phytoene synthase EC (PSY) are two well-known examples of this protein family and share a number of functional similarities. These similarities are also reflected in their primary structure. In particular three well conserved regions are shared by SQS and PSY; they could be involved in substrate binding and/or the catalytic mechanism. SQS catalyzes the conversion of two molecules of farnesyl diphosphate (FPP) into squalene. It is the first committed step in the cholesterol biosynthetic pathway. The reaction carried out by SQS is catalyzed in two separate steps: the first is a head-to-head condensation of the two molecules of FPP to form presqualene diphosphate; this intermediate is then rearranged in a NADP-dependent reduction, to form squalene:
Syn-copalyl-diphosphate synthase is an enzyme with systematic name 9alpha-copalyl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction
Halimadienyl-diphosphate synthase is an enzyme with systematic name halima-5,13-dien-15-yl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction
Chlorophyllide a and Chlorophyllide b are the biosynthetic precursors of chlorophyll a and chlorophyll b respectively. Their propionic acid groups are converted to phytyl esters by the enzyme chlorophyll synthase in the final step of the pathway. Thus the main interest in these chemical compounds has been in the study of chlorophyll biosynthesis in plants, algae and cyanobacteria. Chlorophyllide a is also an intermediate in the biosynthesis of bacteriochlorophylls.
