Sequences of the active-site peptides of three of the high-Mr penicillin-binding proteins of Escherichia coli K-12
File(s)
Published version
Author(s)
KECK, W
GLAUNER, B
SCHWARZ, U
BROOMESMITH, JK
SPRATT, BG
Type
Journal Article
Abstract
The amino acid compositions of the radioactive
peptides obtained from trypsin digestion of ['4C]benzylpenicillin-labeled
penicillin-binding proteins (PBPs) 1A, 1B,
and 3 of Escherichia coli have been obtained. Complete digestion
of these peptides with a combination of aminopeptidase M
and carboxypeptidase Y showed that benzylpenicillin was
bound to a serine residue in each of these proteins. Comparison
of the compositions of the penicillin-labeled peptides with
the complete amino acid sequences of PBPs 1A, 1B, and 3
showed that the acylated serine occurs near the middle of each
of the proteins, within the conserved sequence Gly-Ser-XaaXaa-Lys-Pro.
The sequence around the acylated serine of these
high Mr PBPs shows little similarity to that around the acylated
serine of the low-Mr PBPs (D-alanine carboxypeptidases) or
of the class A or class C 3-lactamases, except that in all of
these enzymes which interact with penicillin the acylated serine
residue occurs within the sequence Ser-Xaa-Xaa-Lys.
peptides obtained from trypsin digestion of ['4C]benzylpenicillin-labeled
penicillin-binding proteins (PBPs) 1A, 1B,
and 3 of Escherichia coli have been obtained. Complete digestion
of these peptides with a combination of aminopeptidase M
and carboxypeptidase Y showed that benzylpenicillin was
bound to a serine residue in each of these proteins. Comparison
of the compositions of the penicillin-labeled peptides with
the complete amino acid sequences of PBPs 1A, 1B, and 3
showed that the acylated serine occurs near the middle of each
of the proteins, within the conserved sequence Gly-Ser-XaaXaa-Lys-Pro.
The sequence around the acylated serine of these
high Mr PBPs shows little similarity to that around the acylated
serine of the low-Mr PBPs (D-alanine carboxypeptidases) or
of the class A or class C 3-lactamases, except that in all of
these enzymes which interact with penicillin the acylated serine
residue occurs within the sequence Ser-Xaa-Xaa-Lys.
Date Issued
1985-04-01
Date Acceptance
1984-12-03
Citation
Proceedings of the National Academy of Sciences of the United States of America, 1985, 82 (7), pp.1999-2003
ISSN
1091-6490
Publisher
National Academy of Sciences
Start Page
1999
End Page
2003
Journal / Book Title
Proceedings of the National Academy of Sciences of the United States of America
Volume
82
Issue
7
Copyright Statement
The author(s) retains copyright to individual articles published prior to 1992, and this article is posted by permission from the author. Proc. Nati. Acad. Sci. USA
Vol. 82, pp. 1999-2003, April 1985
Vol. 82, pp. 1999-2003, April 1985
Subjects
Science & Technology
Multidisciplinary Sciences
Science & Technology - Other Topics
MULTIDISCIPLINARY SCIENCES
Publication Status
Published