SHV-1 beta-lactamase (SHV-1)

SHV-1 beta-lactamase is a **class A serine beta-lactamase enzyme** primarily found in *Klebsiella pneumoniae* but also present in other Gram-negative enterobacteria[5]. It hydrolyzes the beta-lactam ring of penicillins and early cephalosporins, conferring resistance to these antibiotics[2][8]. Its structure is very similar to TEM-1 beta-lactamase but features a wider active site, which is crucial for interaction with both substrates and inhibitors[1][2]. SHV-1 is mostly chromosomally encoded in *K. pneumoniae*, but related plasmid-borne variants (Extended-spectrum SHV-beta-lactamases, ESBLs) have spread widely and confer resistance to newer cephalosporins. The enzyme’s hydrolytic mechanism involves key conserved motifs centered around a nucleophilic serine residue. Therapeutically, SHV-1 poses a significant problem for the treatment of bacterial infections because its presence can render many beta-lactam drugs ineffective[2][3][8]. Detection of SHV-1 in clinical isolates is vital for appropriate antibiotic selection, and the emergence of inhibitor-resistant variants further complicates therapies[6].

Other names

SHV beta-lactamaseSulfhydryl variable beta-lactamase

Hydrolysis/inactivation of beta-lactam antibiotics by breaking the beta-lactam ring Drugs/inhibitors form acyl–enzyme intermediates, some inhibitors (e.g., sulbactam) stabilizing inactive forms or intermediates[4]