Difference between revisions of "Part:BBa K855004"

 
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理弘-生物-谢依朋 17:12:02
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==Kinetic Parameters and Enzyme Activity in different conditions: WHU-China==
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<partinfo>BBa_K855004 parameters</partinfo>
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<center><img src = "https://2020.igem.org/wiki/images/5/59/T--WHU-China--parts5-5.png" style = "width:160px;height:120px"></center>
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<figcaption><center><b>Fig1: Steady-State Rate Constants for PvdQ-Catalyzed Hydrolysis of Selected Substrates. a:not determined because limited substrate solubility prevents determination of Vmax. b:Fitting error is ≤8%.  </b></center></figcaption>
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<center><img src = "https://2020.igem.org/wiki/images/f/f3/T--WHU-China--parts6-6.png" style = "width:160px;height:120px"></center>
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<figcaption><center><b>Fig2: Distribution of the various interaction energies of PvdQ-Ligand complexes. </b></center></figcaption>
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<p> The Michaelis constant (Km) and kcat value of an enzyme have always been important as they show the efficiency of the enzyme towards its substrate. So they are frequently used to decide whether the enzyme is “good” or not according to specific situation. And the various energy changes may also provide an insight of the enzyme-ligand interactions. So we submit the data we obtain from literatures[1][2] about pvdQ gene, including kinetic parameters towards different substrates and energy changes in the enzyme-ligand interaction process. Further users can conduct their experiments or models based on these data then.</p>
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<p>Reference:</p>
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<p>1.Clevenger K D, Wu R, Er J A V, et al., Rational Design of a Transition State Analogue with Picomolar Affinity for Pseudomonas aeruginosa PvdQ, a Siderophore Biosynthetic Enzyme[J]. Acs Chemical Biology, 2013, 8(10):2192-2200.</p>
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<p>2. Liu Y, Ebalunode J O, Briggs J M, Insights into the substrate binding specificity of quorum-quenching acylase PvdQ[J]. Journal of Molecular Graphics and Modelling, 2019.</p>

Revision as of 09:45, 27 October 2020


pvdQ gene form pseudomonas aeruginosa PAO1 with his tag added before stop condon

pvdQ gene codes for an acylase that can degrade long-chain Nacylhomoserine lactones (AHLs), e.g. 3-oxo-C12-HSL.

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 1489
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 1489
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 1196
    Illegal XhoI site found at 1594
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 1489
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 1489
    Illegal NgoMIV site found at 31
    Illegal NgoMIV site found at 770
    Illegal NgoMIV site found at 1172
    Illegal NgoMIV site found at 1329
    Illegal NgoMIV site found at 1556
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI.rc site found at 1926


理弘-生物-谢依朋 17:12:02

Kinetic Parameters and Enzyme Activity in different conditions: WHU-China

BBa_K855004 parameters

Fig1: Steady-State Rate Constants for PvdQ-Catalyzed Hydrolysis of Selected Substrates. a:not determined because limited substrate solubility prevents determination of Vmax. b:Fitting error is ≤8%.
Fig2: Distribution of the various interaction energies of PvdQ-Ligand complexes.

The Michaelis constant (Km) and kcat value of an enzyme have always been important as they show the efficiency of the enzyme towards its substrate. So they are frequently used to decide whether the enzyme is “good” or not according to specific situation. And the various energy changes may also provide an insight of the enzyme-ligand interactions. So we submit the data we obtain from literatures[1][2] about pvdQ gene, including kinetic parameters towards different substrates and energy changes in the enzyme-ligand interaction process. Further users can conduct their experiments or models based on these data then.

Reference:

1.Clevenger K D, Wu R, Er J A V, et al., Rational Design of a Transition State Analogue with Picomolar Affinity for Pseudomonas aeruginosa PvdQ, a Siderophore Biosynthetic Enzyme[J]. Acs Chemical Biology, 2013, 8(10):2192-2200.

2. Liu Y, Ebalunode J O, Briggs J M, Insights into the substrate binding specificity of quorum-quenching acylase PvdQ[J]. Journal of Molecular Graphics and Modelling, 2019.