Difference between revisions of "Part:BBa K398000"
| (10 intermediate revisions by the same user not shown) | |||
| Line 2: | Line 2: | ||
<partinfo>BBa_K398000 short</partinfo> | <partinfo>BBa_K398000 short</partinfo> | ||
| + | [[Image:LadA-Dimer.jpg|400px|thumb|right|Ribbon diagram of the LadA dimer.]] | ||
A flavoprotein alkane monooxygenase native to Geobacillus thermodinitrificans NG-80-2. It has been found to specifically oxidize the terminal regions of alkanes ranging from C15 up to at least C36. The product is the corresponding primary alkanol. LadA forms a catalytic complex with flavin mononucleotide (FMN) which utilizes dioxygen to insert an oxygen atom into the substrate. | A flavoprotein alkane monooxygenase native to Geobacillus thermodinitrificans NG-80-2. It has been found to specifically oxidize the terminal regions of alkanes ranging from C15 up to at least C36. The product is the corresponding primary alkanol. LadA forms a catalytic complex with flavin mononucleotide (FMN) which utilizes dioxygen to insert an oxygen atom into the substrate. | ||
| Line 10: | Line 11: | ||
*Binding, orienting, and activating the substrate for its oxygenation | *Binding, orienting, and activating the substrate for its oxygenation | ||
| − | LadA's ability to preferentially capture long-chain alkanes for oxidation sets it apart from other flavoprotein monooxygenases | + | LadA's ability to preferentially capture long-chain alkanes for oxidation sets it apart from other flavoprotein monooxygenases. For more information see the references below. |
| − | [[ | + | See [https://parts.igem.org/Part:BBa_K398017 BBa_K398017] and [https://parts.igem.org/Part:BBa_K398027 BBa_K398027] for the characterized protein generators. |
| − | + | ||
| + | [1] Li, L. et al, Crystal Structure of Long-Chain Alkane Monooxygenase (LadA) in Complex with Coenzyme FMN: Unveiling the Long-Chain Alkane Hydroxylase. <i>J. Mol. Biol</i>, <b>376</b>, 453-465 (2008) | ||
<!-- --> | <!-- --> | ||
| Line 19: | Line 21: | ||
<partinfo>BBa_K398000 SequenceAndFeatures</partinfo> | <partinfo>BBa_K398000 SequenceAndFeatures</partinfo> | ||
| − | + | <!-- | |
| − | <!-- | + | |
===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K398000 parameters</partinfo> | <partinfo>BBa_K398000 parameters</partinfo> | ||
<!-- --> | <!-- --> | ||
Latest revision as of 00:19, 28 October 2010
Long-Chain Alkane Monooxygenase
A flavoprotein alkane monooxygenase native to Geobacillus thermodinitrificans NG-80-2. It has been found to specifically oxidize the terminal regions of alkanes ranging from C15 up to at least C36. The product is the corresponding primary alkanol. LadA forms a catalytic complex with flavin mononucleotide (FMN) which utilizes dioxygen to insert an oxygen atom into the substrate.
The general catalytic function involves three chemical processes:
- Reduction of the cofactor flavin mononucleotide (FMN to FMNH2) by NAD(P)H
- Reaction of FMNH2 with O2
- Binding, orienting, and activating the substrate for its oxygenation
LadA's ability to preferentially capture long-chain alkanes for oxidation sets it apart from other flavoprotein monooxygenases. For more information see the references below.
See BBa_K398017 and BBa_K398027 for the characterized protein generators.
[1] Li, L. et al, Crystal Structure of Long-Chain Alkane Monooxygenase (LadA) in Complex with Coenzyme FMN: Unveiling the Long-Chain Alkane Hydroxylase. J. Mol. Biol, 376, 453-465 (2008)
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI site found at 908