Difference between revisions of "Part:BBa K3349000"

Revision as of 16:52, 29 September 2020

Pectin Lyase Pnl

This Pectin Lyase is from the organism Paenibacillus amylolyticus . Pnl cleaves at methylated sites of pectin or homogalacturonan substrates at high affinity [1]. Used in conjuction with Pectin lyases PelB and PelC, pectin can be effectively cleaved [1]. A hexa-histidine tag was added to the C-terminus of the coding sequence for nickel affinity purification.

For building thermostable variants of this Pnl enzyme we first did homology modelling as the crystal structure has not been determined.

pnl modelling

Figure 1: Homology modelling of Pnl from P. amylolyticus . The protein structure was done using iTASSER [2] and SWISS-Model [3]. The two structures were then alighned and compared.

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]

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 This Pectin Lyase is from the organism <i> Paenibacillus amylolyticus </i>. Pnl cleaves at methylated sites of pectin or homogalacturonan substrates at high affinity [1]. Used in conjuction with Pectin lyases PelB and PelC, pectin can be effectively cleaved [1]. A hexa-histidine tag was added to the C-terminus of the coding sequence for nickel affinity purification.
-For building thermostable variants of this Pnl enzyme we first did some homology modelling as the crystal structure has not been determined.
+For building thermostable variants of this Pnl enzyme we first did homology modelling as the crystal structure has not been determined.
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+Figure 1: Homology modelling of Pnl from <i>P. amylolyticus </i>. The protein structure was done using iTASSER [2] and SWISS-Model [3]. The two structures were then alighned and compared.