Difference between revisions of "Part:BBa K3739009"
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<partinfo>BBa_K3739009 short</partinfo>
 
<partinfo>BBa_K3739009 short</partinfo>
  
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Histidine ammonia-lyase with a his-tag is involved in catalyzing the reaction of changing L-histidine into trans-urocanate. LMT is a signal peptile.
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LMT here represents a signal peptide used to secrect the fusion protein outside the cell. The enzyme catalyzes the reaction of converting histidine to form toxic urocanic acid and his-tag is added to purify the protein.
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===Biology===
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LMT
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Lytic murein transglycosylase (LMT) is an enzyme which is able to degrade murein, a component of cell wall of bacteria. There are two kind of LMTs existing in ''E.coli'': the membrane-binding one and the soluble one. The gene coding LMT homolog is also incorporated in the genome of ''Vibrio natriegens''. The LMT signal peptide (named LMT in our parts) is from the LMT homolog, which can lead the fused protein secreted out of ''Vibrio natriegens''.
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hutH
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The HutH comes from ''Pseudomonas putida''. Under natural conditions, many microorganisms can use the histidine ammonia-lyase (HutH) to change L-histidine into urocanic acid. HutH catalyzes the first step in the degradation of histidine, and the product urocanic acid is further metabolized to glutamate. This enzyme could be found in the liver of vertebrates and in bacteria such as ''Escherichia coli'', ''Salmonella'' and ''Pseudomonas''. It is specific for L-histidine and can be inhibited by D-histidine or imidazole. The active center of the enzyme is thought to be dehydroalanine.
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===Usage===
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Used to construct the composite part <partinfo>BBa_K3739040</partinfo> and <partinfo>BBa_K3739107</partinfo>.
  
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===Usage and Biology===
 
  
 
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Revision as of 22:57, 21 October 2021


LMT-his-hutH

LMT here represents a signal peptide used to secrect the fusion protein outside the cell. The enzyme catalyzes the reaction of converting histidine to form toxic urocanic acid and his-tag is added to purify the protein.

Biology

LMT

Lytic murein transglycosylase (LMT) is an enzyme which is able to degrade murein, a component of cell wall of bacteria. There are two kind of LMTs existing in E.coli: the membrane-binding one and the soluble one. The gene coding LMT homolog is also incorporated in the genome of Vibrio natriegens. The LMT signal peptide (named LMT in our parts) is from the LMT homolog, which can lead the fused protein secreted out of Vibrio natriegens.

hutH

The HutH comes from Pseudomonas putida. Under natural conditions, many microorganisms can use the histidine ammonia-lyase (HutH) to change L-histidine into urocanic acid. HutH catalyzes the first step in the degradation of histidine, and the product urocanic acid is further metabolized to glutamate. This enzyme could be found in the liver of vertebrates and in bacteria such as Escherichia coli, Salmonella and Pseudomonas. It is specific for L-histidine and can be inhibited by D-histidine or imidazole. The active center of the enzyme is thought to be dehydroalanine.

Usage

Used to construct the composite part BBa_K3739040 and BBa_K3739107.


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 219
    Illegal NgoMIV site found at 655
    Illegal NgoMIV site found at 1390
    Illegal NgoMIV site found at 1626
    Illegal AgeI site found at 292
    Illegal AgeI site found at 1119
    Illegal AgeI site found at 1615
  • 1000
    COMPATIBLE WITH RFC[1000]