Difference between revisions of "Penicillin-binding proteins"
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==Carboxypeptidases== | ==Carboxypeptidases== | ||
| − | * [[DacA]] | + | * [[DacA]] PBP 5 |
| − | * [[DacB]] | + | * [[DacB]] PBP 5* |
| − | * [[DacC]] | + | * [[DacC]] PBP4A |
| − | * [[DacF]] | + | * [[DacF]] PBP I |
==Transpeptidases== | ==Transpeptidases== | ||
| Line 11: | Line 11: | ||
* [[PbpB]] PBP2B | * [[PbpB]] PBP2B | ||
* [[PbpC]] PBP3 | * [[PbpC]] PBP3 | ||
| − | |||
* [[PbpH]] PBP H | * [[PbpH]] PBP H | ||
* [[PbpI]] PBP4B | * [[PbpI]] PBP4B | ||
| − | |||
* [[SpoVD]] spore cortex-specific PBP | * [[SpoVD]] spore cortex-specific PBP | ||
| Line 23: | Line 21: | ||
==Bifunctional glucosyltransferases/ transpeptidases== | ==Bifunctional glucosyltransferases/ transpeptidases== | ||
| − | * [[PbpD]] | + | * [[PbpD]]: PBP 4 |
* [[PbpF]] | * [[PbpF]] | ||
* [[PbpG]] | * [[PbpG]] | ||
* [[PonA]]: PBP 1 | * [[PonA]]: PBP 1 | ||
| + | |||
| + | ==Related pages== | ||
| + | * [[Cell wall synthesis]] | ||
| + | * [[Cell shape]] | ||
| + | * [[elongasome]] | ||
| + | * [http://subtiwiki.uni-goettingen.de/pathways/cellwall.html Cell wall synthesis in SubtiPathways] | ||
| + | |||
| + | ==Important original publications== | ||
| + | <pubmed>22909777 29456081 26499795</pubmed> | ||
==Reviews== | ==Reviews== | ||
| − | <pubmed> 18266856 18248419 16911039 16339737 14662355 </pubmed> | + | <pubmed> 18266856 18248419 16911039 16339737 14662355 31974163</pubmed> |
Latest revision as of 12:42, 20 July 2020
Contents
Carboxypeptidases
Transpeptidases
Endopeptidases
Bifunctional glucosyltransferases/ transpeptidases
Related pages
Important original publications
Yoshikazu Kawai, Katarzyna Mickiewicz, Jeff Errington
Lysozyme Counteracts β-Lactam Antibiotics by Promoting the Emergence of L-Form Bacteria.
Cell: 2018, 172(5);1038-1049.e10
[PubMed:29456081]
[WorldCat.org]
[DOI]
(I p)
Jonathan M Fura, Daniel Kearns, Marcos M Pires
D-Amino Acid Probes for Penicillin Binding Protein-based Bacterial Surface Labeling.
J Biol Chem: 2015, 290(51);30540-50
[PubMed:26499795]
[WorldCat.org]
[DOI]
(I p)
Ozden Kocaoglu, Rebecca A Calvo, Lok-To Sham, Loralyn M Cozy, Bryan R Lanning, Samson Francis, Malcolm E Winkler, Daniel B Kearns, Erin E Carlson
Selective penicillin-binding protein imaging probes reveal substructure in bacterial cell division.
ACS Chem Biol: 2012, 7(10);1746-53
[PubMed:22909777]
[WorldCat.org]
[DOI]
(I p)
Reviews
Truc Do, Julia E Page, Suzanne Walker
Uncovering the activities, biological roles, and regulation of bacterial cell wall hydrolases and tailoring enzymes.
J Biol Chem: 2020, 295(10);3347-3361
[PubMed:31974163]
[WorldCat.org]
[DOI]
(I p)
Eric Sauvage, Frédéric Kerff, Mohammed Terrak, Juan A Ayala, Paulette Charlier
The penicillin-binding proteins: structure and role in peptidoglycan biosynthesis.
FEMS Microbiol Rev: 2008, 32(2);234-58
[PubMed:18266856]
[WorldCat.org]
[DOI]
(P p)
André Zapun, Carlos Contreras-Martel, Thierry Vernet
Penicillin-binding proteins and beta-lactam resistance.
FEMS Microbiol Rev: 2008, 32(2);361-85
[PubMed:18248419]
[WorldCat.org]
[DOI]
(P p)
Pauline Macheboeuf, Carlos Contreras-Martel, Viviana Job, Otto Dideberg, Andréa Dessen
Penicillin binding proteins: key players in bacterial cell cycle and drug resistance processes.
FEMS Microbiol Rev: 2006, 30(5);673-91
[PubMed:16911039]
[WorldCat.org]
[DOI]
(P p)
Dirk-Jan Scheffers, Mariana G Pinho
Bacterial cell wall synthesis: new insights from localization studies.
Microbiol Mol Biol Rev: 2005, 69(4);585-607
[PubMed:16339737]
[WorldCat.org]
[DOI]
(P p)
David L Popham, Kevin D Young
Role of penicillin-binding proteins in bacterial cell morphogenesis.
Curr Opin Microbiol: 2003, 6(6);594-9
[PubMed:14662355]
[WorldCat.org]
[DOI]
(P p)
