Characteristics of beta-lactamase-inhibiting proteins from Streptomyces exfoliatus SMF19.
Streptomyces exfoliatus SMF19 produced two types of extracellular beta-lactamase-inhibiting proteins, 48 (beta LIP-I) and 33 (beta LIP-II) kDa. The inhibition mode of beta LIP-I on Bacto Penase and benzylpenicillin as substrates was uncompetitive (i.e., both Km and Vmax were changed), while that of beta LIP-II was noncompetitive (i.e., only Vmax was changed). The inhibition constants of beta LIP-I and beta LIP-II were 0.62 x 10(-4) and 2.74 x 10(-1) mumol, respectively. The N-terminal amino acid sequence of beta LIP-I was NH3-*-S-T-V-F-D-L-V-*-L-G, and that of beta LIP-II was NH3-D-F-*-V-F-D-L-E-A-T-D-E.
Kim
M K
MK
Department of Microbiology, College of Natural Sciences, Seoul National University, Korea.
Lee
K J
KJ
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D008969:Molecular Sequence Data; D013302:Streptomyces / Q000378:metabolism*; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics
D001426:Bacterial Proteins; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases