Difference between revisions of "Penicillin-binding proteins"

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* [[DacA]]
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==Carboxypeptidases==
* [[DacB]]
+
 
* [[DacC]]
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* [[DacA]] PBP 5
* [[DacF]]
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* [[DacB]] PBP 5*
* [[PbpA]]
+
* [[DacC]] PBP4A
* [[PbpB]]
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* [[DacF]] PBP I
* [[PbpC]]
+
 
* [[PbpD]]
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==Transpeptidases==
* [[PbpE]]
+
 
 +
* [[PbpA]] PBP2A
 +
* [[PbpB]] PBP2B
 +
* [[PbpC]] PBP3
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* [[PbpH]] PBP H
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* [[PbpI]] PBP4B
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* [[SpoVD]] spore cortex-specific PBP
 +
 
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==Endopeptidases==
 +
 
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* [[PbpE]] PBP 4* (spore coat)
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* [[PbpX]] PBP X
 +
 
 +
==Bifunctional glucosyltransferases/ transpeptidases==
 +
* [[PbpD]]: PBP 4
 
* [[PbpF]]
 
* [[PbpF]]
 
* [[PbpG]]
 
* [[PbpG]]
* [[PbpH]]
+
* [[PonA]]: PBP 1
* [[PbpI]]
+
 
* [[PbpX]]
+
==Related pages==
* [[PonA]]
+
* [[Cell wall synthesis]]
* [[SpoVD]]
+
* [[Cell shape]]
* [[YkuA]]
+
* [[elongasome]]
* [[YrrR]]
+
* [http://subtiwiki.uni-goettingen.de/pathways/cellwall.html Cell wall synthesis in SubtiPathways]
* [[YwhE]]
+
 
 +
==Important original publications==
 +
<pubmed>22909777 29456081 26499795</pubmed>
 +
 
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==Reviews==
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<pubmed> 18266856 18248419 16911039 16339737 14662355 31974163</pubmed>

Latest revision as of 12:42, 20 July 2020

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