Beta Lactamase is a highly conserved enzyme in both prokaryotes and eukaryotes. In prokaryotes, it gives bacteria such as E.Coli antibiotic resistance. In eukaryotes, it acts as exo and endonucleases to regulate transcription activity.
""Background Information""
There are several classes of antibiotics, including cephalosporin and penicillin [1]. Some common examples of specific drugs in these classes include cefazolin, cefadroxil, penicillin, ampicillin, and methicillin [2]. These antibiotics function by preventing bacteria from forming their cell wall, regardless if the bacteria are gram positive or gram negative [3]. These antibiotics all contain a beta-lactam ring [4].
Inside of the gram positive or gram negative bacteria, there is a protein called the penicillin binding protein. The penicillin binding proteins (PBPs) are what help the peptidoglycan walls to form by linking NAG and NAM chains together. The beta-lactam ring fits particularly well into the PBP, which is how antibiotics like penicillin prevent bacteria from synthesizing its cell wall.
File:Beta-lactam antibiotics example 1.svg
Beta Lactam Ring present in Antibiotics
https://en.wikipedia.org/wiki/%CE%92-lactam_antibiotic#/media/File:Beta-lactam_antibiotics_example_1.svg
File:Penicillin inhibition.svg
Penicillin inhibition
https://en.wikipedia.org/wiki/%CE%92-lactam_antibiotic#/media/File:Penicillin_inhibition.svg
"" Mechanism of Antibiotic Beta Lactam Ring Resistance ""
Bacteria such as E. Coli make and excrete an enzyme called beta lactamase [5]. Bacteria can become resistant to antibiotics that contain lactam rings when the B-lactamase enzyme attacks the beta lactam ring (classified as a hydrolase). Once the beta lactam ring is sliced open, it is no longer functional [6].
""Beta Lactamase in Humans (PDB: 3ZWF)""
In order to make mature tRNAs, first they have to be processed [7]. The enzyme that does tRNA processing is called TRNase Z. In humans, the form of beta lactamase formed uses a zinc-dependent mechanism, noted as metallo-beta lactamase [8]. These enzymes in humans function to regulate nuclear activity, providing exo and endonuclease activity.
""Structural highlights""
Macromolecules:
Two chains (A,B) of Zinc phosphodiesterase ELAC Protein 1 [9].
Unique Ligands
- Phosphate (PO4) ligand on chains A and B of Zinc phosphodiesterase ELAC Protein 1 [10].
- Zinc (Zn) ligand on chains A and B of Zinc phosphodiesterase ELAC Protein 1 [11].
-1,2 Ethanediol (EDO) ligand on chains A and B of Zinc phosphodiesterase ELAC Protein 1 [12].
- Sodium (Na+) ion on chain B of Zinc phosphodiesterase ELAC Protein 1 [13].
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- ↑ Tooke CL, Hinchliffe P, Bragginton EC, Colenso CK, Hirvonen VHA, Takebayashi Y, Spencer J. beta-Lactamases and beta-Lactamase Inhibitors in the 21st Century. J Mol Biol. 2019 Aug 23;431(18):3472-3500. doi: 10.1016/j.jmb.2019.04.002. Epub, 2019 Apr 5. PMID:30959050 doi:https://dx.doi.org/10.1016/j.jmb.2019.04.002
- ↑ Tooke CL, Hinchliffe P, Bragginton EC, Colenso CK, Hirvonen VHA, Takebayashi Y, Spencer J. beta-Lactamases and beta-Lactamase Inhibitors in the 21st Century. J Mol Biol. 2019 Aug 23;431(18):3472-3500. doi: 10.1016/j.jmb.2019.04.002. Epub, 2019 Apr 5. PMID:30959050 doi:https://dx.doi.org/10.1016/j.jmb.2019.04.002
- ↑ Tooke CL, Hinchliffe P, Bragginton EC, Colenso CK, Hirvonen VHA, Takebayashi Y, Spencer J. beta-Lactamases and beta-Lactamase Inhibitors in the 21st Century. J Mol Biol. 2019 Aug 23;431(18):3472-3500. doi: 10.1016/j.jmb.2019.04.002. Epub, 2019 Apr 5. PMID:30959050 doi:https://dx.doi.org/10.1016/j.jmb.2019.04.002
- ↑ https://doi.org/10.1021/cr030102i
- ↑ Dominski Z. Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism. Crit Rev Biochem Mol Biol. 2007 Mar-Apr;42(2):67-93. doi:, 10.1080/10409230701279118. PMID:17453916 doi:https://dx.doi.org/10.1080/10409230701279118
- ↑ doi: https://dx.doi.org/10.2210/pdb3ZWF/pdb
- ↑ https://doi.org/10.1101/575373
- ↑ Dominski Z. Nucleases of the metallo-beta-lactamase family and their role in DNA and RNA metabolism. Crit Rev Biochem Mol Biol. 2007 Mar-Apr;42(2):67-93. doi:, 10.1080/10409230701279118. PMID:17453916 doi:https://dx.doi.org/10.1080/10409230701279118
- ↑ doi: https://dx.doi.org/10.2210/pdb3ZWF/pdb
- ↑ doi: https://dx.doi.org/10.2210/pdb3ZWF/pdb
- ↑ doi: https://dx.doi.org/10.2210/pdb3ZWF/pdb
- ↑ doi: https://dx.doi.org/10.2210/pdb3ZWF/pdb
- ↑ doi: https://dx.doi.org/10.2210/pdb3ZWF/pdb
