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	<title>beta-lactamase Archives - Online Biology Notes</title>
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		<title>Beta-lactamase: functional classification</title>
		<link>https://www.onlinebiologynotes.com/beta-lactamase-functional-classification/</link>
		
		<dc:creator><![CDATA[Gaurab Karki]]></dc:creator>
		<pubDate>Wed, 10 Oct 2018 14:29:10 +0000</pubDate>
				<category><![CDATA[Pharmaceutical Microbiology]]></category>
		<category><![CDATA[beta-lactamase]]></category>
		<category><![CDATA[functional classification of beta lactamase]]></category>
		<category><![CDATA[types of beta-lactamase]]></category>
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					<description><![CDATA[<p>Beta-lactamase: functional classification Beta-lactamase is an enzyme capable of hydrolyzing β-lactam antibiotics. β-lactamase degrade β-lactam antibiotics by opening the β-lactam ring. The microorganisms producing beta-lactamase <a class="mh-excerpt-more" href="https://www.onlinebiologynotes.com/beta-lactamase-functional-classification/" title="Beta-lactamase: functional classification">[...]</a></p>
<p>The post <a href="https://www.onlinebiologynotes.com/beta-lactamase-functional-classification/">Beta-lactamase: functional classification</a> appeared first on <a href="https://www.onlinebiologynotes.com">Online Biology Notes</a>.</p>
]]></description>
										<content:encoded><![CDATA[<h1>Beta-lactamase: functional classification</h1>
<ul>
<li>Beta-lactamase is an enzyme capable of hydrolyzing β-lactam antibiotics. β-lactamase degrade β-lactam antibiotics by opening the β-lactam ring. The microorganisms producing beta-lactamase enzyme become resistant β-lactam antibiotics.</li>
</ul>
<h2>Classification of β-lactamase enzyme on the basis of function:</h2>
<h3><strong>Group 1 β-lactamase :</strong></h3>
<ul>
<li>These are class-C enzyme and are cephalosporinase which are not inhibited by clavulanic acid.</li>
<li>They are also resistant to cefamycin</li>
</ul>
<h3><strong>Group 2 β-lactamase:</strong></h3>
<ul>
<li>These includes class-A enzyme and are penicillinase and cephalosporinase.</li>
<li>Inhibited by clavulanic acid.</li>
</ul>
<p><strong>Sub class:</strong></p>
<p><strong>i. Group 2b e (extended spectrum) β-lactamase:</strong></p>
<ul>
<li>These are ESBL capable of hydrolyzing penicillin even 3<sup>rd</sup> and 4<sup>th</sup> generation cephalosporin but are hydrolyzed by clavulanic acid.</li>
</ul>
<p><strong>ii. Group 2b r β-lactamase:</strong></p>
<ul>
<li>These includes inhibitor resistant β-lactamase. These may be resistant to sulbactum and clavulanic acid but are susceptible to inhibition by tazobactum.</li>
</ul>
<p><strong>iii. Group 2c β-lactamase:</strong></p>
<ul>
<li>These includes carbenicillinase. These enzymes hydrolyses carbenicillin more than Benzylpenicillin. These are class-A enzyme. They also show activity towards Oxacillin.</li>
</ul>
<p><strong>iv. Group 2d (extended spectrum) β-lactamase:</strong></p>
<ul>
<li>These are class-A or D enzyme and includes Cloxacillinase (oxacillinase). These enzymes hydrolyses cloxacillin more than Benzylpenicillin and also has activity against carbenicillin.</li>
</ul>
<p><strong>v. Group 2e β-lactamase:</strong></p>
<ul>
<li>These are class-A enzyme. These includes cephalosporinase. These are inhibited by clavulanic acid.</li>
</ul>
<p><strong>vi. Group 2f β-lactamase:</strong></p>
<ul>
<li>These are class-A enzyme. These includes carbapenimase. These are serine based enzyme which are also inhibited by clavulanic acid.</li>
</ul>
<h3>Group 3 β-lactamase:</h3>
<ul>
<li>These includes class-B enzyme and are zinc based metalloenzyme. Eg. Carbapenimase</li>
<li>These are not inhibited by clavulanic acid.</li>
<li>They are chromosomal mediated enzymes</li>
</ul>
<h3>Group 4 β-lactamase:</h3>
<ul>
<li>These includes penicillinase</li>
<li>These are not inhibited by clavulanic acid.</li>
</ul>
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<h2>Beta-lactamase: functional classification</h2>
<p>The post <a href="https://www.onlinebiologynotes.com/beta-lactamase-functional-classification/">Beta-lactamase: functional classification</a> appeared first on <a href="https://www.onlinebiologynotes.com">Online Biology Notes</a>.</p>
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