Low pKa lysine residues at the active site of sarcosine oxidase from Corynebacterium sp. U-96

Biochemical and Biophysical Research Communications
Etsuko B MukouyamaHaruo Suzuki

Abstract

Sarcosine oxidase from Corynebacterium sp. U-96 is inactivated by iodoacetamide with the modification of two specific residues. Comparing the amino acid sequence and mass spectra of the peptide fragments containing the modified residues with those from the native enzyme, the modified residues were identified to be lysine. The pKa of these residues were estimated to be 8.5 and 6.7 from the pH dependence of inactivation in the presence and absence of the competitive inhibitor, acetate. These estimated pKa values are much lower than that of the epsilon-amino group of lysine residue. There may be unique microenvironments around these residues that activate their -amino groups to be susceptible to iodoacetamide. A possible role of the lysine residue with pKa 6.7 is discussed.

References

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Mar 21, 2002·Journal of Protein Chemistry·Etsuko B MukouyamaHaruo Suzuki

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Citations

Jun 11, 2005·Biochemical and Biophysical Research Communications·Koh IdaHaruo Suzuki
Aug 17, 2011·The Journal of General Physiology·Darren LockeAndrew L Harris
Jun 18, 2010·Toxicological Sciences : an Official Journal of the Society of Toxicology·Lihai ZhangRichard M LoPachin
Jul 19, 2013·Journal of Virology·Onyinyechukwu UchimeMargaret Kielian
Sep 15, 2014·Neuroscience Letters·Richard M LoPachin, Terrence Gavin
May 31, 2019·Molecular & Cellular Proteomics : MCP·Bright D DanquahMichael O Glocker
Aug 28, 2020·The Journal of Biological Chemistry·Kwabena F M OpuniMichael O Glocker
Aug 1, 2019·Molecular & Cellular Proteomics : MCP·Bright D DanquahMichael O Glocker

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