Conversion of Serine‐Type Aldehyde Tags by the Radical SAM Protein AtsB from Methanosarcina mazei. (18th July 2019)

• Record Type: Journal Article
• Authors: Krüger, Tobias; Weiland, Stefanie; Boschanski, Mareile; Sinha, Prem Kumar; Falck, Georg; Müller, Kristian M.; Dierks, Thomas; Sewald, Norbert
• Is Part Of: Chembiochem. Volume 20:Number 16(2019)
• Page Start: 2074
• Page End: 2078
• Publication Date: 2019-07-18
• Subjects: aldehydes -- enzymes -- formylglycine -- peptides -- protein engineering; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201900322
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract: Formylglycine‐generating enzymes provide a convenient tool for site‐specific protein derivatization. Their ability to oxidize cysteine or serine residues within a defined consensus sequence to C α ‐formylglycine (FGly) allows for the targeted introduction of a unique chemical handle for various bioconjugation reactions. In recent years, oxygen‐dependent FGly‐generating enzyme saw broad use in protein functionalization and the generation of protein conjugates. Yet, the FGly‐generating system AtsB, along with its capability to convert unusual aldehyde tag sequences, remains mostly unused. Herein, the ability of AtsB from Methanosarcina mazei to convert nonclassical aldehyde tags of the SX(A/P)XR‐type and its potential use in bioconjugation chemistry are demonstrated. Abstract : Change it again SAM ! The radical S ‐adenosyl methionine protein AtsB from M. mazei (MM‐AtsB) is tested for the conversion of serine‐type aldehyde tags for the site‐specific introduction of noncanonical C α ‐formylglycine (FGly) in vitro. Oxidation of serine to FGly enables distinct modification of peptides and the production of a fluorescent protein conjugate.