Abstract:
:The conserved KTG triad in the class C beta-lactamase from Citrobacter freundii GN346 was examined as to its function by means of site-directed mutagenesis. The following conversions were performed; Lys-315 to arginine, alanine or glutamic acid, Thr-316 to valine, and Gly-317 to alanine, proline or isoleucine. The resultant mutant enzymes revealed that a basic amino acid at position 315 and a small uncharged residue at position 317 are essential for the enzyme activity, but a hydroxyl group at residue 316 is not required for the enzymatic catalysis. The kinetic properties of the purified Arg-315 and Val-316 enzymes provided information on the function of these residues.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Tsukamoto K,Nishida N,Tsuruoka M,Sawai Tdoi
10.1016/0014-5793(90)80416-gsubject
Has Abstractpub_date
1990-10-01 00:00:00pages
243-6issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(90)80416-Gjournal_volume
271pub_type
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