S96A mutant of streptomyces K15 DD-transpeptidase

Catalytic mechanism of the Streptomyces K15 DD-transpeptidase/penicillin-binding protein probed by site-directed mutagenesis and structural analysis.

The Crystal Structure of a Penicilloyl-Serine Transferase of Intermediate Penicillin Sensitivity

Crystallization and X-Ray Diffraction Study of the Streptomyces K15 Penicillin-Binding Dd-Transpeptidase

D-ALANYL-D-ALANINE CARBOXYPEPTIDASE, DD-PEPTIDASE

VTKPTIAAVGGYAMNNGTGTTLYTKAADTRRSTGSTTKIMTAKVVLAQSNLNLDAKVTIQKAYSDYVVANNASQAHLIVG
DKVTVRQLLYGLMLPAGCDAAYALADKYGSGSTRAARVKSFIGKMNTAATNLGLHNTHFDSFDGIGNGANYSTPRDLTKI
ASSAMKNSTFRTVVKTKAYTAKTVTKTGSIRTMDTWKNTNGLLSSYSGAIGVKTGSGPEAKYCLVFAATRGGKTVIGTVL
ASTSIPARESDATKIMNYGFAL

Tris 0.1M, PEG 6K 22%, NaCl 0.4M, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K

K38H MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

C98A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

C98N MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

R248L MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

PENICILLIN-BINDING, DD-TRANSPEPTIDASE, SERINE PEPTIDASE, BETA-LACTAMASE, HYDROLASE CARBOXYPEPTIDASE, HYDROLASE

VTKPTIAAVGGYAMNNGTGTTLYTKAADTRRSTGSTTKIMTAKVVLAQSNLNLDAKVTIQKAYSDYVVANKPSQAHLIVG
DKVTVRQLLYGLMLPSGCDAAYALADKYGSGSQAAARVKSFIGKMNTAATNLGLHNTHFDSFDGIGNGANYSTPRHLTKI
ASSAMKNSTFRTVVKTKAYTAKTVTKTGSIRTMDTWKNTNGLLSSYSGAIGVKTGSGPEAKYCLVFAATRGGKTVIGTVL
ASTSIPARESDATKIMNYGFAL