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2.5.1.86: trans,polycis-decaprenyl diphosphate synthase

This is an abbreviated version!
For detailed information about trans,polycis-decaprenyl diphosphate synthase, go to the full flat file.

Word Map on EC 2.5.1.86

Reaction

(2Z,6E)-farnesyl diphosphate
+ 7 isopentenyl diphosphate = 7 diphosphate +
trans,octacis-decaprenyl diphosphate

Synonyms

cis-decaprenyl diphosphate synthase, decaprenyl diphosphate synthase, decaprenyl diphosphate synthase 1, decaprenyl diphosphate synthase 2, DPP synthase, DPPS, DPS1, long-chain prenyl diphosphate synthase, MtDPPS, polyprenyl diphosphate synthase, Rv2361c, SlDPS, Z-decaprenyl-diphosphate synthase

ECTree

     2 Transferases
         2.5 Transferring alkyl or aryl groups, other than methyl groups
             2.5.1 Transferring alkyl or aryl groups, other than methyl groups (only sub-subclass identified to date)
                2.5.1.86 trans,polycis-decaprenyl diphosphate synthase

Inhibitors

Inhibitors on EC 2.5.1.86 - trans,polycis-decaprenyl diphosphate synthase

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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(2-methyl-1,3-dioxa-8-azaspiro[4.5]dec-8-yl)-8-nitro-6-(trifluoromethyl)-4H-1,3-benzothiazin-4-one
i.e. BTZ043. Benzothiazinones mediate killing of Corynebacterineae by blocking decaprenyl phosphate recycling involved in cell wall biosynthesis. In the presence of benzothiazinones (BTZ), the bacilli accumulate decaprenyl-phosphoribose and fail to recycle decaprenyl phosphate, which results in the depletion of decaprenyl phosphate and ultimately leads to cell death. Overexpression of Z-decaprenyl-diphosphate synthase gene NCgl2203 in wild-type Corynebacterium glutamicum increases resistance to benzothiazinone BTZ043. BTZ043 targets DprE1, which is a FAD-containing oxidoreductase involved in the epimerization of decaprenyl-phosphoribose to decaprenyl-phosphoarabinose
BPH-640
a bisphosphonate inhibitor, three-dimensional structure from crystal structure, dimeric DPPS structure with one bound BPH-640 molecule in each monomer, overview. BPH-640 occupies a dimer interface binding site, sandwiched between residues G77, N78, G79, R80, T83, R89, and R127 of monomer A and residues R292 and F293 of monomer B