Difference between revisions of "Part:BBa K5043002"

 
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<partinfo>BBa_K5043002 short</partinfo>
 
<partinfo>BBa_K5043002 short</partinfo>
  
nidB forms together with nidA, phtAc and phtAd pyrene dioxygenase enzyme complex. This complex catalyzes the oxydation of pyrene to Cis-4,5-Dihydro-4,5-dihydroxypyrene. This is the first step in biodegradation of pyrene.
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nidB forms together with nidA, phtAc and phtAd a pyrene dioxygenase enzyme complex. This complex catalyzes the oxidation of pyrene to cis-4,5-Dihydro-4,5-dihydroxypyrene. This is the first step in biodegradation of pyrene.
  
This part was derived from Mycobacterium vanbaalenii Pyr-1 which is a known pyrene degrading bacteria. It was also reported, that nidAB is able to oxydize other high molecular weight polycyclic aromatic hydrocarbons. [1]
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This part was derived from <i> Mycobacterium vanbaalenii </i> Pyr-1 which is a known pyrene degrading bacteria. It was also reported that nidAB is able to oxidize other high molecular weight polycyclic aromatic hydrocarbons. [1]
  
 
[1] O. Kweon, S.-J. Kim, J. P. Freeman, J. Song, S. Baek, and C. E. Cerniglia, "Substrate specificity and structural characteristics of the novel Rieske nonheme iron aromatic ring-hydroxylating oxygenases NidAB and NidA3B3 from Mycobacterium vanbaalenii PYR-1," mBio, vol. 1, no. 2, 2010, doi: 10.1128/mBio.00135-10
 
[1] O. Kweon, S.-J. Kim, J. P. Freeman, J. Song, S. Baek, and C. E. Cerniglia, "Substrate specificity and structural characteristics of the novel Rieske nonheme iron aromatic ring-hydroxylating oxygenases NidAB and NidA3B3 from Mycobacterium vanbaalenii PYR-1," mBio, vol. 1, no. 2, 2010, doi: 10.1128/mBio.00135-10

Latest revision as of 09:35, 30 September 2024


nidB from M. vanbaalenii Pyr-1

nidB forms together with nidA, phtAc and phtAd a pyrene dioxygenase enzyme complex. This complex catalyzes the oxidation of pyrene to cis-4,5-Dihydro-4,5-dihydroxypyrene. This is the first step in biodegradation of pyrene.

This part was derived from Mycobacterium vanbaalenii Pyr-1 which is a known pyrene degrading bacteria. It was also reported that nidAB is able to oxidize other high molecular weight polycyclic aromatic hydrocarbons. [1]

[1] O. Kweon, S.-J. Kim, J. P. Freeman, J. Song, S. Baek, and C. E. Cerniglia, "Substrate specificity and structural characteristics of the novel Rieske nonheme iron aromatic ring-hydroxylating oxygenases NidAB and NidA3B3 from Mycobacterium vanbaalenii PYR-1," mBio, vol. 1, no. 2, 2010, doi: 10.1128/mBio.00135-10


Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 395
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 395
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 395
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 395
  • 1000
    COMPATIBLE WITH RFC[1000]