Difference between revisions of "Part:BBa K5043002"
m |
Beyzademirel (Talk | contribs) |
||
| Line 3: | Line 3: | ||
<partinfo>BBa_K5043002 short</partinfo> | <partinfo>BBa_K5043002 short</partinfo> | ||
| − | nidB forms together with nidA, phtAc and phtAd pyrene dioxygenase enzyme complex. This complex | + | 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] | + | 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
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 395
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 395
- 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 395
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 395
- 1000COMPATIBLE WITH RFC[1000]