TY - JOUR
T1 - The inhibition of metallo-β-lactamase by thioxo-cephalosporin derivatives
AU - Tsang, Wing Y.
AU - Dhanda, Anupma
AU - Schofield, Christopher J.
AU - Frère, Jean Marie
AU - Galleni, Moreno
AU - Page, Michael I.
PY - 2004/4
Y1 - 2004/4
N2 - The 8-thioxocephalosporins are poor substrates for the B. cereus metallo β-lactamase (kcat/Km=61.4 M-1 s -1) and act as weak competitive inhibitors (Ki ∼700 μM). The hydrolysis product of thioxocephalosporin, a thioacid, also inhibits the enzyme competitively with a Ki=96 μM, whereas the cyclic thioxo-piperazinedione, formed by intramolecular aminolysis of thioxocephalexin has a Ki of 29 μM.
AB - The 8-thioxocephalosporins are poor substrates for the B. cereus metallo β-lactamase (kcat/Km=61.4 M-1 s -1) and act as weak competitive inhibitors (Ki ∼700 μM). The hydrolysis product of thioxocephalosporin, a thioacid, also inhibits the enzyme competitively with a Ki=96 μM, whereas the cyclic thioxo-piperazinedione, formed by intramolecular aminolysis of thioxocephalexin has a Ki of 29 μM.
UR - http://www.scopus.com/inward/record.url?scp=1542404603&partnerID=8YFLogxK
U2 - 10.1016/j.bmcl.2004.01.047
DO - 10.1016/j.bmcl.2004.01.047
M3 - Article
C2 - 15026061
AN - SCOPUS:1542404603
VL - 14
SP - 1737
EP - 1739
JO - Bioorganic and Medicinal Chemistry Letters
JF - Bioorganic and Medicinal Chemistry Letters
SN - 0960-894X
IS - 7
ER -