An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction

Journal article

and catalytic Lys258 Nζ amino groups an equally shared deuterium is observed in an apparent low-barrier hydrogen bond (LBHB). Density functional theory calculations were performed to provide further evidence of this LBHB interaction. The structural arrangement and the juxtaposition of PMP and Lys258, facilitated by the LBHB, suggests active site preorganization for the incoming ketoacid substrate that initiates the second half-reaction.

Authors: Drago, VN; Dajnowicz, S; Parks, JM; Blakeley, MP; Keen, DA

• Publication status: Published
• Peer review status: Peer reviewed
• Publisher: Royal Society of Chemistry
• Journal: Chemical Science
• Volume: 13
• Issue: 34
• Pages: 10057-10065
• Publication date: 2022-08-31
• DOI: 10.1039/d2sc02285k
• EISSN: 2041-6539
• ISSN: 2041-6520
• Language: English
• Keywords: Hydrogen bond; Chemistry; Catalysis; Biochemistry; Pyridoxamine; Phosphate; Pyridoxal phosphate; Stereochemistry; Cofactor; Active site; Organic chemistry; Pyridoxal; Molecule; Enzyme