Physiological functions of D-alanine carboxypeptidases in Escherichia coli

Ghosh, Anindya S.; Chowdhury, Chiranjit; Nelson, David E.

doi:10.1016/j.tim.2008.04.006

Cited by 138 publications

(210 citation statements)

References 78 publications

Supporting

Mentioning

206

Contrasting

Order By: Relevance

“…E. coli PBPs are visualized by polyacrylamide gel electrophoresis after the treatment of cells with radiolabeled or fluorescence-labeled ␤-lac- tams and are designated according to their electrophoretic migrations (6,49,72,95,103,186,243,291,315). Most PBPs are anchored to the cytoplasmic membrane with their active site in the periplasm (73).…”

Section: Penicillin-binding Peptidasesmentioning

confidence: 99%

“…DD-Carboxypeptidase PBP5. As the major PBP of E. coli (60,243), PBP5 has been extensively studied (72,205,280,301). It was identified with D-alanine carboxypeptidase IA activity encoded by the dacA gene (30,166,191,242).…”

Section: Penicillin-binding Peptidasesmentioning

confidence: 99%

“…Work up to 1995 has been reviewed (99,100,102). More recent reviews have concerned specific hydrolase families (72,73,92,103,185,196,230,295). The aim of the present work is to bring together the past and present abundant information on the PG hydrolases of E. coli and to attempt a critical assessment of their functions in PG maturation, turnover, elongation, septation, and recycling as well as in cell autolysis.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Peptidoglycan Hydrolases of Escherichia coli

Heijenoort

2011

Microbiol Mol Biol Rev

190

233

View full text Add to dashboard Cite

SUMMARY The review summarizes the abundant information on the 35 identified peptidoglycan (PG) hydrolases of Escherichia coli classified into 12 distinct families, including mainly glycosidases, peptidases, and amidases. An attempt is also made to critically assess their functions in PG maturation, turnover, elongation, septation, and recycling as well as in cell autolysis. There is at least one hydrolytic activity for each bond linking PG components, and most hydrolase genes were identified. Few hydrolases appear to be individually essential. The crystal structures and reaction mechanisms of certain hydrolases having defined functions were investigated. However, our knowledge of the biochemical properties of most hydrolases still remains fragmentary, and that of their cellular functions remains elusive. Owing to redundancy, PG hydrolases far outnumber the enzymes of PG biosynthesis. The presence of the two sets of enzymes acting on the PG bonds raises the question of their functional correlations. It is difficult to understand why E. coli keeps such a large set of PG hydrolases. The subtle differences in substrate specificities between the isoenzymes of each family certainly reflect a variety of as-yet-unidentified physiological functions. Their study will be a far more difficult challenge than that of the steps of the PG biosynthesis pathway.

show abstract

Section: Penicillin-binding Peptidasesmentioning

confidence: 99%

Section: Penicillin-binding Peptidasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Peptidoglycan Hydrolases of Escherichia coli

Heijenoort

2011

Microbiol Mol Biol Rev

190

233

View full text Add to dashboard Cite

show abstract

“…11,12,[18][19][20][21][22] Amino acid alignment of the esterase of A. globiformis with the penicillin-binding proteins and family VIII esterases shows that the consensus active site motif of Ser-X-X-Lys, found exclusively among the homologous enzymes, 11) is also considered to be the active site of the esterase in this study (Ser59-Cys-Ser-Lys62), while the other two elements consist of slightly different amino acids, such as Tyr-His-Ala and Lys-Ser-His respectively. In this study, we focused on identifying the catalytic residue and elucidating the role of the lysine residue one helix turn downstream of the serine, and considered the similarities and differences in catalytic mechanism between the esterase in this study and the homologous enzymes through DFP-labeling and site-directed mutagenesis experiments.…”

Section: Resultsmentioning

confidence: 99%

“…Previous reports have discussed the mechanism of catalytic events, i.e., acylation and deacylation steps, of these penicillin-binding proteins, and have reported that several residues in the conserved elements are responsible for catalytic activity. [18][19][20][21][22] In this study, in order to identify the catalytic residues of esterase from A. globiformis and the differences and similarities in the hydrolytic mechanism between this esterase and the other homologous enzymes, both DFPlabeling and site-directed mutagenesis experiments were conducted. Covalent labeling of the esterase with the inhibitor followed by mass spectrometric analysis was performed to identify the active-site nucleophile.…”

Section: Identification Of the Catalytic Residues Of Carboxylesterasementioning

confidence: 99%

Identification of the Catalytic Residues of Carboxylesterase fromArthrobacter globiformisby Diisopropyl Fluorophosphate-Labeling and Site-Directed Mutagenesis

Nishizawa¹,

Yabusaki

Kanaoka³

2011

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

β‐Lactam Antibiotics

Testero

Fisher

Mobashery

2010

Burger's Medicinal Chemistry and Drug Discovery

View full text Add to dashboard Cite

The β‐lactam classes of antibacterials are preeminent in the treatment of bacterial infection due to their unparalleled clinical efficacy and clinical safety. Following the discovery of the penicillins, successive β‐lactam drug discovery has added the cephalosporin, penem cephamycin, clavulanate, monobactam, nocardicin, and carbapenem subclasses. The driving force behind much of this era of discovery is the staggering ability of pathogenic bacteria to adapt previous generations of the β‐lactam by the acquisition and expression of resistance mechanisms. Although many factors contribute to β‐lactam resistance, alterations to the molecular targets of the β‐lactams (the penicillin binding proteins) and the use of enzymes (the β‐lactamases) capable of the hydrolytic deactivation of the β‐lactams are paramount. This review traces the historical development of β‐lactam drug discovery, with emphasis on the most recent progress in the medicinal chemistry, biochemistry, and microbiology of the β‐lactams leading to the discovery of new generation β‐lactam antibacterials effective against the Gram‐negative and ‐positive bacterial pathogens of current medical concern.

show abstract

Physiological functions of D-alanine carboxypeptidases in Escherichia coli

Cited by 138 publications

References 78 publications

Peptidoglycan Hydrolases of Escherichia coli

Peptidoglycan Hydrolases of Escherichia coli

Identification of the Catalytic Residues of Carboxylesterase fromArthrobacter globiformisby Diisopropyl Fluorophosphate-Labeling and Site-Directed Mutagenesis

β‐Lactam Antibiotics

Contact Info

Product

Resources

About