Sandbox Reserved 992: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 5: Line 5:
<Structure load='1ke4' size='400' frame='true' color='white' align='right' caption='AmpC Class C Beta-lactamase' />
<Structure load='1ke4' size='400' frame='true' color='white' align='right' caption='AmpC Class C Beta-lactamase' />


{| class="wikitable" align="right" cellpadding=5 style="float:right; border:1px solid #BBB"
== Function and Mechanism ==
[[Image:Beta-lactam.jpg|200px|thumb|left|A β-lactam antibiotic (Penicillin)]]Clinically, β-lactam antibiotics, characterized by their central chemical structure, are utilized to combat bacterial infections by targeting penicillin-binding proteins (PBPs), also known as transpeptidases. PBPs are enzymes that are located in the cell membrane and function in cross-linking to form the peptidoglycan layer. PBPs have a deprotonated serine which executes nucleophilic attack on the carbonyl carbon. The PBP is then covalently attached to one unit of peptidoglycan. The amino group of an alanine on a second unit of peptidoglycan then performs a second nucleophilic attack on the carbonyl carbon, resulting in two covalently cross-linked peptidoglycan units and the regeneration of the catalytic PBP.<ref>"Peptidoglycan cell wall." The University of Warwick. n.d. Web. 25 Jan 15</ref>
 
{| class="wikitable" align="right" cellpadding=5 style="float:right; border:1px solid #BBB;margin:.46em 0 0 .2em"
|+ Class C β-lactamase
|+ Class C β-lactamase
|-
|-
Line 14: Line 17:
| CAS number ||  
| CAS number ||  
|-
|-
| Olatunkboh || Chijiaku || 22
! style="background: #efefef;" colspan="2" |Databases
|-
|-
| Adrienne || Anthoula || 22
| Adrienne || Anthoula || 22
Line 22: Line 25:
| Jon-Kabat  || Zinn || 22
| Jon-Kabat  || Zinn || 22
|}
|}
== Function and Mechanism ==
[[Image:Beta-lactam.jpg|200px|thumb|left|A β-lactam antibiotic (Penicillin)]]Clinically, β-lactam antibiotics, characterized by their central chemical structure, are utilized to combat bacterial infections by targeting penicillin-binding proteins (PBPs), also known as transpeptidases. PBPs are enzymes that are located in the cell membrane and function in cross-linking to form the peptidoglycan layer. PBPs have a deprotonated serine which executes nucleophilic attack on the carbonyl carbon. The PBP is then covalently attached to one unit of peptidoglycan. The amino group of an alanine on a second unit of peptidoglycan then performs a second nucleophilic attack on the carbonyl carbon, resulting in two covalently cross-linked peptidoglycan units and the regeneration of the catalytic PBP.<ref>"Peptidoglycan cell wall." The University of Warwick. n.d. Web. 25 Jan 15</ref>


[[Image:Peptidoglycan_cross_linking.png|500px|thumb|right|Peptidoglycan with PDB Cross-linking Mechanism]]
[[Image:Peptidoglycan_cross_linking.png|500px|thumb|right|Peptidoglycan with PDB Cross-linking Mechanism]]