Difference between revisions of "Part:BBa K1371004"

 
 
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<partinfo>BBa_K1371004 short</partinfo>
 
<partinfo>BBa_K1371004 short</partinfo>
  
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One of parts of the DEBS1
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The leading role of the loading part is Acyltransfer-ase, AT domain. In this part, we will introduce the function of AT domain by analyzing the chemical reactions between AT domain, ACP domain and polyketide chains.
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The function of AT domain is activating the extended units, propionyl groups which will be combined with the polyketide chains.
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In Loading, Proplonyl-CoA reacts with the oxhydryl on the pecific binding sites of AT domains and binds to AT domain, and then CoA-SHs are displaced. At this time, proplonyl groups have been activated. They are transferred onto the ACP domains in Loading and anchored there.
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In Module 1 or Module 2, AT domains anchor the proplonyl groups of (2S)Methylmalonyl-CoA to the ACP domains in Module 1 or Module 2 by the same mechanism. The proplonyl groups anchored wait for the catalysis of KS domain in the next step.
  
 
<!-- Add more about the biology of this part here
 
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Latest revision as of 08:28, 16 October 2014

AT-ACP-L1(loading module)

The leading role of the loading part is Acyltransfer-ase, AT domain. In this part, we will introduce the function of AT domain by analyzing the chemical reactions between AT domain, ACP domain and polyketide chains.

The function of AT domain is activating the extended units, propionyl groups which will be combined with the polyketide chains.

In Loading, Proplonyl-CoA reacts with the oxhydryl on the pecific binding sites of AT domains and binds to AT domain, and then CoA-SHs are displaced. At this time, proplonyl groups have been activated. They are transferred onto the ACP domains in Loading and anchored there.

In Module 1 or Module 2, AT domains anchor the proplonyl groups of (2S)Methylmalonyl-CoA to the ACP domains in Module 1 or Module 2 by the same mechanism. The proplonyl groups anchored wait for the catalysis of KS domain in the next step.

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
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 507
    Illegal AgeI site found at 318
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 1432