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	<updated>2026-09-16T12:32:29Z</updated>
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		<id>https://proteopedia.org/index.php?title=Molecular_Playground/Beta-galactosidase&amp;diff=2585284</id>
		<title>Molecular Playground/Beta-galactosidase</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/Beta-galactosidase&amp;diff=2585284"/>
		<updated>2016-04-01T07:11:33Z</updated>

		<summary type="html">&lt;p&gt;Doug Juers: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
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&#039;&#039;&#039;β-Galactosidase&#039;&#039;&#039; is a hydrolase enzyme that catalyzes the hydrolysis of beta- galactosidase into monosaccharides (carbon/energy source).  Is encoded by the &#039;&#039;lacZ&#039;&#039; gene of the &#039;&#039;lac&#039;&#039; operon in E.coli.  It is a large 120 kDa, &amp;gt;1000 amino acids) protein that forms a tetramer.  &lt;br /&gt;
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It is commonly used as a reporter molecule in genetics and molecular biology.  Usually, experiments are designed so that the β-Galactosidase concentration in the cell is a readout for some aspect of a system being studied. When the β-Galactosidase cleaves the substrate o-nitrophenyl-b-D-galactopyraniside (ONPG), o-nitrophenol is released. This compound has a yellow color, and absorbs 420 nm light. To measure β-Galactosidase activity the accumulation of yellow color (increase 420 nm absorbance)/minute is monitored.&lt;br /&gt;
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==3D structures of beta-galactosidase==&lt;br /&gt;
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[[Beta-galactosidase]]&lt;/div&gt;</summary>
		<author><name>Doug Juers</name></author>
	</entry>
	<entry>
		<id>https://proteopedia.org/index.php?title=Molecular_Playground/Beta-galactosidase&amp;diff=2585283</id>
		<title>Molecular Playground/Beta-galactosidase</title>
		<link rel="alternate" type="text/html" href="https://proteopedia.org/index.php?title=Molecular_Playground/Beta-galactosidase&amp;diff=2585283"/>
		<updated>2016-04-01T07:11:00Z</updated>

		<summary type="html">&lt;p&gt;Doug Juers: &lt;/p&gt;
&lt;hr /&gt;
&lt;div&gt;One of the [[CBI Molecules]] being studied in the  [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground].&lt;br /&gt;
&lt;br /&gt;
&#039;&#039;&#039;β-Galactosidase&#039;&#039;&#039; is a hydrolase enzyme that catalyzes the hydrolysis of beta- galactosidase into monosaccharides (carbon/energy source).  Is encoded by the &#039;&#039;lacZ&#039;&#039; gene of the &#039;&#039;lac&#039;&#039; operon in E.coli.  It is a large 120 kDa, &amp;gt;1000 amino acids) protein that forms a tetramer.  &lt;br /&gt;
&lt;br /&gt;
It is commonly used as a reporter molecule in genetics and molecular biology.  Usually, experiments are designed so that the β-Galactosidase concentration in the cell is a readout for some aspect of a system being studied. When the β-Galactosidase cleaves the substrate o-nitrophenyl-b-D-galactopyraniside (ONPG), o-nitrophenol is released. This compound has a yellow color, and absorbs 420 nm light. To measure β-Galactosidase activity the accumulation of yellow color (increase 420 nm absorbance)/minute is monitored.&lt;br /&gt;
&lt;br /&gt;
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{{STRUCTURE_3iap |  PDB=3iap  |  SCENE=  }}&lt;br /&gt;
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==3D structures of beta-galactosidase==&lt;br /&gt;
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[[Beta-galactosidase]]&lt;/div&gt;</summary>
		<author><name>Doug Juers</name></author>
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