Difference between revisions of "Part:BBa K5531012"

 
Line 1: Line 1:
  
−
__NOTOC__
+
 
 
<partinfo>BBa_K5531012 short</partinfo>
 
<partinfo>BBa_K5531012 short</partinfo>
  
−
P4H
 
  
−
 
−
<!-- Add more about the biology of this part here
 
−
===Usage and Biology===
 
  
 
<!-- -->
 
<!-- -->
Line 13: Line 9:
 
<partinfo>BBa_K5531012 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K5531012 SequenceAndFeatures</partinfo>
  
 +
<!DOCTYPE html>
 +
<html lang="en">
 +
<head>
 +
    <meta charset="UTF-8">
 +
    <meta name="viewport" content="width=device-width, initial-scale=1.0">
 +
    <title>BBa_K5531012 (P4H)</title>
 +
    <style>
 +
        img {
 +
            max-width: 80%; /* Adjust this percentage to change size relative to text */
 +
            height: auto; /* Maintain aspect ratio */
 +
        }
 +
        .caption {
 +
            text-align: center;
 +
            font-size: 0.9em;
 +
            margin-top: 5px;
 +
            margin-bottom: 20px; /* Space below the caption */
 +
        }
 +
    </style>
 +
</head>
 +
<body>
 +
    <h2>BBa_K5531012 (P4H)</h2>
  
−
<!-- Uncomment this to enable Functional Parameter display
+
    <h3>Profile</h3>
−
===Functional Parameters===
+
    <p>
−
<partinfo>BBa_K5531012 parameters</partinfo>
+
        <strong>Name:</strong> P4H<br>
−
<!-- -->
+
        <strong>Base Pairs:</strong> 738 bp<br>
 +
        <strong>Origin:</strong> <em>Arabidopsis thaliana</em> (Mouse-ear cress); synthesized<br>
 +
        <strong>Properties:</strong> Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxylates preferentially prolines in the second positions in the -Pro-Pro-Gly-triplets. Hydroxyprolines are essential constituents of many plant cell wall glycoproteins, such as extensions, hydroxyproline-rich glycoproteins, lectins, and arabinogalactan proteins. Can hydroxylate collagen-like peptides and hypoxia-inducible transcription factor peptides [1].
 +
    </p>
 +
 
 +
    <!-- Figure 1 -->
 +
    <div style="text-align:center;">
 +
        <img src="https://static.igem.wiki/teams/5531/bba-k5531012/1.png" alt="Figure 1: Protein structure diagram of P4H">
 +
        <div class="caption">Fig. 1. Protein structure diagram of P4H</div>
 +
    </div>
 +
 
 +
    <h3>References</h3>
 +
    <p>
 +
        [1] Rutschmann C, Baumann S, Cabalzar J, Luther KB, Hennet T. Recombinant expression of hydroxylated human collagen in <em>Escherichia coli</em>. <em>Appl Microbiol Biotechnol</em>. 2014 May;98(10):4445-55.
 +
    </p>
 +
   
 +
</body>
 +
</html>

Revision as of 10:49, 29 September 2024


P4H


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
    COMPATIBLE WITH RFC[1000]

<!DOCTYPE html> BBa_K5531012 (P4H)

BBa_K5531012 (P4H)

Profile

Name: P4H
Base Pairs: 738 bp
Origin: Arabidopsis thaliana (Mouse-ear cress); synthesized
Properties: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxylates preferentially prolines in the second positions in the -Pro-Pro-Gly-triplets. Hydroxyprolines are essential constituents of many plant cell wall glycoproteins, such as extensions, hydroxyproline-rich glycoproteins, lectins, and arabinogalactan proteins. Can hydroxylate collagen-like peptides and hypoxia-inducible transcription factor peptides [1].

Figure 1: Protein structure diagram of P4H
Fig. 1. Protein structure diagram of P4H

References

[1] Rutschmann C, Baumann S, Cabalzar J, Luther KB, Hennet T. Recombinant expression of hydroxylated human collagen in Escherichia coli. Appl Microbiol Biotechnol. 2014 May;98(10):4445-55.