Sulfhydryl variable beta-lactamase (SHV beta-lactamase) (SHV)

Sulfhydryl variable (SHV) beta-lactamase is a prominent member of the Ambler Class A serine beta-lactamases, originally identified as a chromosomally encoded enzyme in Klebsiella pneumoniae [1]. This enzyme plays a critical role in bacterial resistance by catalyzing the hydrolysis of the beta-lactam ring in various antibiotics, including penicillins and early-generation cephalosporins [2]. While the parent SHV-1 enzyme primarily targets penicillins, numerous mutations have led to the emergence of extended-spectrum beta-lactamases (ESBLs), such as SHV-2 and SHV-5, which can degrade third-generation cephalosporins and monobactams [3]. As a therapeutic target, SHV is addressed by co-administering beta-lactam antibiotics with beta-lactamase inhibitors like tazobactam or avibactam to restore antibiotic efficacy [1]. These inhibitors neutralize the enzyme's activity by forming a stable complex at the active site, thereby protecting the partner antibiotic from degradation [2]. Understanding the structural evolution and mutational landscape of SHV is essential for developing next-generation antimicrobial therapies to combat rising global resistance [3].

Other names

SHV-type beta-lactamaseClass A beta-lactamase SHVblaSHVSulfhydryl variable enzyme

Beta-lactamase inhibitors function by binding to the active-site serine residue of the SHV enzyme, forming a stable, often covalent, acyl-enzyme intermediate that prevents the enzyme from hydrolyzing the beta-lactam ring of co-administered antibiotics [1][2].