Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Substrates and Products (Substrate)

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

<< < Results 101 - 110 of 129 > >>
EC Number Substrates Commentary Substrates Organism Products Commentary (Products) Reversibility
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21more no substrate: 6,7-dihydrofarnesyl diphosphate, 3-desmethylfarnesyl diphosphate Saccharomyces cerevisiae ? - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21more not metabolized: (E)-6,7,10,11-tetrahydrofarnesyl diphosphate Saccharomyces cerevisiae ? - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21more enzyme is key regulator not only for phytosterol but also for triterpene biosynthesis Panax ginseng ? - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21more the catalytic process involves two reactions: firstly, two FPP molecules are condensed to form presqualene diphosphate (PSPP), an intermediate with a cyclopropane C1'-C2-C3 ring structure, and secondly, PSPP undergoes a NADPH-dependent rearrangement and reduction to generate the end product squalene Homo sapiens ? - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21more catalytic mechanism, overview Homo sapiens ? - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21more squalene and botryococcene are branched-chain, triterpene compounds that arise from the head-to-head condensation of two molecules of farnesyl diphosphate to yield 1'-1 and 1'-3 linkages, respectively. Different enzymes are responsible for botryococcene and squalene biosynthesis in the green alga Botryococcus braunii race B. The specificity for the 1'-1 and 1'-3 linkages is controlled by residues in the active sites that can mediate catalytic specificity. Identification of several amino acid positions contributing to the rearrangement of the cyclopropyl intermediate to squalene, The same positions do not appear to be sufficient to account for the cyclopropyl rearrangement to give botryococcene, oerview Botryococcus braunii ? - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21more analysis of substrate specificity, overview Botryococcus braunii ? - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21presqualene diphosphate + NAD(P)H - Rattus norvegicus squalene + NAD(P)+ + diphosphate - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21presqualene diphosphate + NAD(P)H - Saccharomyces cerevisiae squalene + NAD(P)+ + diphosphate - ?
Show all pathways known for 2.5.1.21Display the word mapDisplay the reaction diagram Show all sequences 2.5.1.21presqualene diphosphate + NAD(P)H in presence of reducing pyridine nucleotide, preferably NADPH, squalene is formed, in absence of reducing cofactor the rate of the condensation reaction is lower and all of the product accumulates as presqualene diphosphate Rattus norvegicus squalene + NAD(P)+ + diphosphate - ?
<< < Results 101 - 110 of 129 > >>