Isoserine-based biotinylated photoaffinity probes that interact with penicillin-binding protein 1bElectronic supplementary information (ESI) available: spectroscopic characterization for all new compounds. Fig. S1: decrease in absorbance at 366 nm as a function of irradiation time for 1b. See http://www.rsc.org/suppdata/cc/b2/b204007g/

2002 ◽  
pp. 1630-1631 ◽  
Author(s):  
Thomas Rühl ◽  
Daniela Volke ◽  
Katherina Stembera ◽  
Yasumaru Hatanaka ◽  
Horst Hennig ◽  
...  
Keyword(s):  
Irradiation Time ◽  
Binding Protein ◽  
Spectroscopic Characterization ◽  
Supplementary Information ◽  
Penicillin Binding Protein ◽  
Photoaffinity Probes ◽  
New Compounds

ChemInform Abstract: Isoserine-Based Biotinylated Photoaffinity Probes that Interact with Penicillin-Binding Protein 1b.

ChemInform ◽  
2010 ◽  
Vol 33 (46) ◽  
pp. no-no
Author(s):  
Thomas Ruehl ◽  
Daniela Volke ◽  
Katherina Stembera ◽  
Yasumaru Hatanaka ◽  
Horst Hennig ◽  
...  
Keyword(s):  
Binding Protein ◽  
Penicillin Binding Protein ◽  
Photoaffinity Probes

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.

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