Difference between revisions of "Part:BBa K1175007"
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(5) http://www.tandfonline.com/doi/full/10.1080/15583724.2011.615962#tabModule | (5) http://www.tandfonline.com/doi/full/10.1080/15583724.2011.615962#tabModule | ||
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<h1>yesZ</h1>The Beta-Galactosidase yesZ is globular and has three aspects that are important to its function. It contains a zinc ion binding site at the C residues 153, 155, and 158 in yellow. The putative nucleophile and acid base cleavage sites are at the E residues 155 and 296 in red. The active site where substrate binding occurs is through the amino acid residue sequence ETSPSYAASL from residues 296- 305. | <h1>yesZ</h1>The Beta-Galactosidase yesZ is globular and has three aspects that are important to its function. It contains a zinc ion binding site at the C residues 153, 155, and 158 in yellow. The putative nucleophile and acid base cleavage sites are at the E residues 155 and 296 in red. The active site where substrate binding occurs is through the amino acid residue sequence ETSPSYAASL from residues 296- 305. | ||
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Figure A describes the time dependent inactivation of the YesZ enzyme using DNP2FGal. The time dependent inactivation observed as a single exponential decay to a non-zero value when DNP2FGal was incubated with the enzyme. Studies of inactivation kinetics were performed by pre-incubating 100 microliters of the enzyme at 37 oC with DNP2FGal at a range of concentrations in a total volume of 140 microliters."> | Figure A describes the time dependent inactivation of the YesZ enzyme using DNP2FGal. The time dependent inactivation observed as a single exponential decay to a non-zero value when DNP2FGal was incubated with the enzyme. Studies of inactivation kinetics were performed by pre-incubating 100 microliters of the enzyme at 37 oC with DNP2FGal at a range of concentrations in a total volume of 140 microliters."> | ||
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<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
Latest revision as of 03:36, 28 September 2013
beta-galacturonidase (YesZ) from Bacillus Subtilis 168
yesZ The enzyme acts on the terminal end of side chains of Rhamnogalacturonan I Pectin, releasing the free galactose. This gene has been isolated from the bacterium Bacillus subtilis subtilis 168. The enzyme yesZ has beta-galactosidase (beta-galacturonidase) activity, cleaving (1→4)-β-D-galactans to produce single galactose molecules from RG I Pectin.
Usage and Biology Pectin is a component of the primary cell wall of plants. As galactose can be metabolized by the human body and by animals, it is an alternative to the usual target of nutrition/energy boosts in biotechnology, glucose.
(1) http://www.ncbi.nlm.nih.gov/pubmed/17449691 (2) http://subtiwiki.uni-goettingen.de/wiki/index.php/YesZ (3) http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1694227/ (4) http://aem.asm.org/content/73/12/3803 (5) http://www.tandfonline.com/doi/full/10.1080/15583724.2011.615962#tabModule
yesZThe Beta-Galactosidase yesZ is globular and has three aspects that are important to its function. It contains a zinc ion binding site at the C residues 153, 155, and 158 in yellow. The putative nucleophile and acid base cleavage sites are at the E residues 155 and 296 in red. The active site where substrate binding occurs is through the amino acid residue sequence ETSPSYAASL from residues 296- 305. |
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yesZ Enzyme Activity
| The kinetic parameters fo the hydrolysis of pNPGal by wild type YesZ Kcat = 81.4 ± 4 s-1, and Km= 3.0 ± 0.2 mM, and Kcat/Km= 27 ± 2 mM -1 s-1. Figure A describes the time dependent inactivation of the YesZ enzyme using DNP2FGal. The time dependent inactivation observed as a single exponential decay to a non-zero value when DNP2FGal was incubated with the enzyme. Studies of inactivation kinetics were performed by pre-incubating 100 microliters of the enzyme at 37 oC with DNP2FGal at a range of concentrations in a total volume of 140 microliters."> |
copyright permission submitted
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 260
Illegal NgoMIV site found at 395 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 559