Difference between revisions of "Part:BBa K398000"
 
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*Binding, orienting, and activating the substrate for its oxygenation
 
*Binding, orienting, and activating the substrate for its oxygenation
  
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LadA's ability to preferentially capture long-chain alkanes for oxidation sets it apart from other flavoprotein monooxygenases[1].
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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.
  
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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.
  
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[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)
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K398000 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K398000 SequenceAndFeatures</partinfo>
  
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===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K398000 parameters</partinfo>
 
<partinfo>BBa_K398000 parameters</partinfo>
 
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Latest revision as of 00:19, 28 October 2010

Long-Chain Alkane Monooxygenase

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.

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


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI site found at 908