Coding
BPO

Part:BBa_K2461002

Designed by: Jessica Harms   Group: iGEM17_UNebraska-Lincoln   (2017-10-16)


Vanadium Dependent Bromoperoxidase

Vanadium dependent bromoperoxidase is a kind of haloperoxidase that is involved in the bromination of organic halo-compounds associated with defense and pigmentation in seaweeds and marine algae. The active site features a vanadium oxide center attached to the protein via one histidine side chain and a collection of hydrogen bonds to the oxide ligands. The enzyme can use many different hydrocarbon substrates to catalyse the oxidation of bromide by hydrogen peroxide. The resulting electrophilic bromonium cation (Br+) attacks hydrocarbons (symbolized as R-H in the following equation): R-H + Br+ + H2O2 → R-Br + H2O + OH−


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal NheI site found at 169
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal AgeI site found at 1234
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 391
    Illegal SapI.rc site found at 115
    Illegal SapI.rc site found at 1312
    Illegal SapI.rc site found at 1720

Our Application

Figure 1:Proposed catalytic cycle of the vanadium dependent bromoperoxidase.

We took this specific bromoperoxidase sequence from the marine algae species Corallina pilulifera to be used in our composite part (BBa_K246100). We picked this specific species because it has been proven that feeding Corallina pilulifera to cattle can reduce methane emissions by up to 50%.[1] Each cow releases 70 kg to 120 kg of methane annually, and coupled with the sheer magnitude of the cattle industry this has become a problem of increasing importance. We will use the vanadium-dependent bromoperoxidase enzyme to create bromoform; the main compound in seaweed that is responsible for decreasing methane emissions in cattle. Bromoform works by inhibiting the efficiency of the methyltransferase enzyme by reacting with the reduced vitamin B12 cofactor required for the second to last step of methanogenesis.

[1]. Kinley, R. D., and Fredeen, A. H. (2014) In vitro evaluation of feeding North Atlantic storm toss seaweeds on ruminal digestion. Journal of Applied Phycology 27, 2387–2393.


[edit]
Categories
Parameters
None