Correction to Selective Targeting by a Mechanism-Based Inactivator

Addition/Correction Cite This: Biochemistry 2017, 56, 5844-5845

pubs.acs.org/biochemistry

Correction to Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5′-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover Romila Mascarenhas, Hoang V. Le, Kenneth D. Clevenger, Helaina J. Lehrer, Dagmar Ringe, Neil L. Kelleher, Richard B. Silverman,* and Dali Liu* Biochemistry 2017, 56 (37), 4951−4961. DOI: 10.1021/acs.biochem.7b00499

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he ChemDraw structure in the graphical abstract [and table of contents (TOC) figure] and Figure 4C did not match the species that was captured in the crystal structure. The figures should have shown the ketimine of glutamate, and not aspartate. The corrected TOC figure and Figure 4 now display the chemical structure of the ketimine of glutamate.

TOC graphic

Received: September 26, 2017 Published: October 18, 2017 © 2017 American Chemical Society

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DOI: 10.1021/acs.biochem.7b00961 Biochemistry 2017, 56, 5844−5845

Biochemistry

Addition/Correction

Figure 4. Structure of Asp-AT with a ketimine intermediate. Protein atoms are shown as green sticks, with oxygen atoms colored red, nitrogen atoms blue, and phosphorus atoms orange. (A) Active site of Asp-AT and a ketimine intermediate formed between PMP and α-ketoglutarate, which is colored yellow (from PDB entry 5VWR). The dashed green lines represent the electrostatic interactions or hydrogen bonds between the ketimine and the active site residues of Asp-AT. (B) Simulated annealing omit map (F0 − Fc) of the adduct. The omit map is shown as a gray mesh at 2.5σ. The omit map was generated after the ketimine had been omitted from the coordinates. (C) Chemical structure of the ketimine intermediate.

5845

DOI: 10.1021/acs.biochem.7b00961 Biochemistry 2017, 56, 5844−5845