In vitro peptidoglycan polymerization catalysed by penicillin binding protein 1b of Escherichia coli K-12

FEBS Letters ◽  
1980 ◽  
Vol 110 (2) ◽  
pp. 245-249 ◽  
Author(s):  
Hideho Suzuki ◽  
Yveline Van Heijenoort ◽  
Toshihide Tamura ◽  
Junzo Mizoguchi ◽  
Yukinori Hirota ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
K 12

scholarly journals Further studies on rod A mutant: A round morphological mutant of Escherichia coli K-12 with wild-type penicillin-binding protein 2.

1980 ◽  
Vol 44 (12) ◽  
pp. 2937-2941 ◽  
Author(s):  
Hiroshi MATSUZAWA ◽  
Sadamitsu ASOH ◽  
Takahisa OHTA ◽  
Shigeo TAMAKI ◽  
Michio MATSUHASHI
Keyword(s):  
Escherichia Coli ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Wild Type ◽  
Morphological Mutant ◽  
K 12

scholarly journals Purification and Characterization of PBP4a, a New Low-Molecular-Weight Penicillin-Binding Protein fromBacillus subtilis

2001 ◽  
Vol 183 (5) ◽  
pp. 1595-1599 ◽  
Author(s):  
Colette Duez ◽  
Marc Vanhove ◽  
Xavier Gallet ◽  
Fabrice Bouillenne ◽  
Jean-Denis Docquier ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Molecular Weight ◽  
Binding Protein ◽  
Order Rate Constant ◽  
Low Molecular Weight ◽  
Penicillin Binding Protein ◽  
Purification And Characterization ◽  
The Third

ABSTRACT Penicillin-binding protein 4a (PBP4a) from Bacillus subtilis was overproduced and purified to homogeneity. It clearly exhibits dd-carboxypeptidase and thiolesterase activities in vitro. Although highly isologous to the Actinomadura sp. strain R39 DD-peptidase (B. Granier, C. Duez, S. Lepage, S. Englebert, J. Dusart, O. Dideberg, J. van Beeumen, J. M. Frère, and J. M. Ghuysen, Biochem. J. 282:781–788, 1992), which is rapidly inactivated by many β-lactams, PBP4a is only moderately sensitive to these compounds. The second-order rate constant (k 2/K) for the acylation of the essential serine by benzylpenicillin is 300,000 M−1s−1 for the Actinomadura sp. strain R39 peptidase, 1,400 M−1 s−1 for B. subtilis PBP4a, and 7,000 M−1 s−1 forEscherichia coli PBP4, the third member of this class of PBPs. Cephaloridine, however, efficiently inactivates PBP4a (k 2/K = 46,000 M−1 s−1). PBP4a is also much more thermostable than the R39 enzyme.

scholarly journals PenA, a penicillin-binding protein-type thioesterase specialized for small peptide cyclization

2021 ◽  
Author(s):  
Kenichi Matsuda ◽  
Kei Fujita ◽  
Toshiyuki Wakimoto
Keyword(s):  
Enzymatic Activity ◽  
Computational Model ◽  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Small Peptide ◽  
Peptide Cyclization ◽  
Chain Lengths ◽  
Non Ribosomal Peptides

Abstract Penicillin binding protein-type thioesterases (PBP-type TEs) are a recently identified group of peptide cyclases that catalyze head-to-tail macrolactamization of non-ribosomal peptides. PenA, a new member of this group, is involved in the biosyntheses of cyclic pentapeptides. In this study, we demonstrated the enzymatic activity of PenA in vitro, and analyzed its substrate scope with a series of synthetic substrates. A comparison of the reaction profiles between PenA and SurE, a representative PBP-type TE, showed that PenA is more specialized for small peptide cyclization. A computational model provided a possible structural rationale for the altered specificity for substrate chain lengths.

scholarly journals Differential Suppression of priA2::kan Phenotypes in Escherichia coli K-12 by Mutations in priA, lexA, and dnaC

Genetics ◽  
1996 ◽  
Vol 143 (1) ◽  
pp. 5-13 ◽  
Author(s):  
Steven J Sandler ◽  
Hardeep S Samra ◽  
Alvin J Clark
Keyword(s):  
Escherichia Coli ◽  
Dna Replication ◽  
Mutant Allele ◽  
Wild Type ◽  
Suppressor Mutations ◽  
Dnab Helicase ◽  
K 12 ◽  
Extragenic Suppressors ◽  
Assembly Activity

Abstract First identified as an essential component of the ϕX174 in vitro DNA replication system, PriA has ATPase, helicase, translocase, and primosome-assembly activities. priA1::kan strains of Escherichia coli are sensitive to UV irradiation, deficient in homologous recombination following transduction, and filamentous. priA2::kan strains have eightfold higher levels of uninduced SOS expression than wild type. We show that (1) priA1::kan strains have eightfold higher levels of uninduced SOS expression, (2) priA2::kan strains are UVS and Rec−, (3) lexA3 suppresses the high basal levels of SOS expression of a priA2::kan strain, and (4) plasmid-encoded priA300 (K230R), a mutant allele retaining only the primosome-assembly activity of priA+, restores both UVR and Rec+ phenotypes to a priA2::kan strain. Finally, we have isolated 17 independent UVR Rec+ revertants of priA2::kan strains that carry extragenic suppressors. All 17 map in the C-terminal half of the dnaC gene. DnaC loads the DnaB helicase onto DNA as a prelude for primosome assembly and DNA replication. We conclude that priA's primosome-assembly activity is essential for DNA repair and recombination and that the dnaC suppressor mutations allow these processes to occur in the absence of priA.

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