Search results
Results From The WOW.Com Content Network
Similarly, it has been demonstrated that zinc chelators can inhibit the hydrolytic activity of metallo-β-lactamases against β-lactam antibiotics, restoring the activity of the latter. [6] Metallo-beta-lactamases are important enzymes because they are involved in the breakdown of antibiotics by antibiotic-resistant bacteria. [7]
The other type of beta-lactamase is of the metallo type ("type B"). Metallo-beta-lactamases (MBLs) need metal ion(s) (1 or 2 Zn 2+ ions [2]) on their active site for their catalytic activities. [3] The structure of the New Delhi metallo-beta-lactamase 1 is given by 6C89. It resembles a RNase Z, from which it is thought to have evolved.
Two zinc ions present in the active binding site. NDM-1 functions through two zinc ions present in the active site that cause hydrolysis of the beta-lactams, rendering them ineffective. Experimental data has shown that zinc chelators can prevent the hydrolysis of beta-lactams mediated by metallo-beta-lactamases. [14]
212442 Ensembl ENSG00000147592 ENSMUSG00000025937 UniProt Q53H82 Q99KR3 RefSeq (mRNA) NM_016027 NM_145381 RefSeq (protein) NP_057111 NP_663356 Location (UCSC) Chr 8: 70.64 – 70.67 Mb Chr 1: 13.69 – 13.73 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Lactamase, beta 2 is a protein that in humans is encoded by the LACTB2 gene. Structure LACTB2 is located on the 8th chromosome ...
A lactam is a cyclic amide, and beta-lactams are named so because the nitrogen atom is attached to the β-carbon atom relative to the carbonyl. The simplest β-lactam possible is 2-azetidinone. β-lactams are significant structural units of medicines as manifested in many β-lactam antibiotics . [ 2 ]
The β-lactam core structures. (A) A penam.(B) A carbapenam.(C) An oxapenam.(D) A penem.(E) A carbapenem.(F) A monobactam.(G) A cephem.(H) A carbacephem.(I) An oxacephem. This is a list of common β-lactam antibiotics—both administered drugs and those not in clinical use—organized by structural class.
An example of such an enzyme is New Delhi metallo-beta-lactamase 1, discovered in 2009.) The genes encoding these enzymes may be inherently present on the bacterial chromosome or may be acquired via plasmid transfer (plasmid-mediated resistance), and β-lactamase gene expression may be induced by exposure to β-lactams. [citation needed]
A zinc finger is a small protein structural motif that is characterized by the coordination of one or more zinc ions (Zn 2+) which stabilizes the fold. The term zinc finger was originally coined to describe the finger-like appearance of a hypothesized structure from the African clawed frog (Xenopus laevis) transcription factor IIIA.