scholarly journals Protonation states of active-site lysines of penicillin-binding protein 6 from Escherichia coli and the mechanistic implications

2014 ◽  
Vol 82 (7) ◽  
pp. 1348-1358 ◽  
Author(s):  
Malika Kumarasiri ◽  
Weilie Zhang ◽  
Qicun Shi ◽  
Jed F. Fisher ◽  
Shahriar Mobashery
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Binding Protein ◽  
Penicillin Binding Protein

scholarly journals Identification of the active site in penicillin-binding protein 3 of Escherichia coli.

1985 ◽  
Vol 164 (1) ◽  
pp. 456-460 ◽  
Author(s):  
R A Nicholas ◽  
J L Strominger ◽  
H Suzuki ◽  
Y Hirota
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Binding Protein ◽  
Penicillin Binding Protein

scholarly journals Primary and predicted secondary structures of the Actinomadura R39 extracellular dd-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4

1992 ◽  
Vol 282 (3) ◽  
pp. 781-788 ◽  
Author(s):  
B Granier ◽  
C Duez ◽  
S Lepage ◽  
S Englebert ◽  
J Dusart ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Active Site ◽  
Binding Capacity ◽  
Binding Protein ◽  
Secondary Structures ◽  
Streptomyces Lividans ◽  
Dimensional Structure ◽  
Peptidase Activity ◽  
Penicillin Binding Protein

As derived from gene cloning and sequencing, the 489-amino-acid DD-peptidase/penicillin-binding protein (PBP) produced by Actinomadura R39 has a primary structure very similar to that of the Escherichia coli PBP4 [Mottl, Terpstra & Keck (1991) FEMS Microbiol. Lett. 78, 213-220]. Hydrophobic-cluster analysis of the two proteins shows that, providing that a large 174-amino-acid stretch is excluded from the analysis, the bulk of the two polypeptide chains possesses homologues of the active-site motifs and secondary structures found in the class A beta-lactamase of Streptomyces albus G of known three-dimensional structure. The 174-amino-acid insert occurs at equivalent places in the two PBPs, between helices alpha 2 and alpha 3, away from the active site. Such an insert is unique among the penicilloyl serine transferases. It is proposed that the Actinomadura R39 PBP and E. coli PBP4 form a special class, class C, of low-Mr PBPs/DD-peptidases. A vector has been constructed and introduced by electrotransformation in the original Actinomadura R39 strain, allowing high-level expression and secretion of the DD-peptidase/PBP (250 mg.l-1). The gene encoding the desired protein is processed differently in Actinomadura R39 and Streptomyces lividans. Incorrect processing in Streptomyces lividans leads to a secreted protein which is inert in terms of DD-peptidase activity and penicillin-binding capacity.

Purification and sequencing of the active site tryptic peptide from penicillin-binding protein 1b of Escherichia coli

Biochemistry ◽  
1985 ◽  
Vol 24 (14) ◽  
pp. 3448-3453 ◽  
Author(s):  
Robert A. Nicholas ◽  
Hideho Suzuki ◽  
Yukinori Hirota ◽  
Jack L. Strominger
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Tryptic Peptide ◽  
Binding Protein ◽  
Penicillin Binding Protein

Identification of the Penicillin-Binding Active Site of Penicillin-Binding Protein 2 of Escherichia coli

1988 ◽  
Vol 104 (5) ◽  
pp. 822-826 ◽  
Author(s):  
Akiko Takasuga ◽  
Hiroyuki Adachi ◽  
Fumitoshi Ishino ◽  
Michio Matsuhashi ◽  
Takahisa Ohta ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Binding Protein ◽  
Penicillin Binding Protein

Binding of penicillin to thiol-penicillin-binding protein 3 of Escherichia coli: identification of its active site

1985 ◽  
Vol 201 (3) ◽  
pp. 499-504 ◽  
Author(s):  
Nicole Houba-Hérin ◽  
Hiroshi Hara ◽  
Masayori Inouye ◽  
Yukinori Hirota
Keyword(s):  
Escherichia Coli ◽  
Active Site ◽  
Binding Protein ◽  
Penicillin Binding Protein
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