@article{8c02059e3b3942388e104affba4bea79,
title = "Structural and Spectroscopic Characterization of a Product Schiff Base Intermediate in the Reaction of the Quinoprotein Glycine Oxidase, GoxA",
abstract = "The LodA-like proteins make up a recently identified family of enzymes that rely on a cysteine tryptophylquinone cofactor for catalysis. They differ from other tryptophylquinone enzymes in that they are oxidases rather than dehydrogenases. GoxA is a member of this family that catalyzes the oxidative deamination of glycine. Our previous work with GoxA from Pseudoalteromonas luteoviolacea demonstrated that this protein forms a stable intermediate upon anaerobic incubation with glycine. The spectroscopic properties of this species were unique among those identified for tryptophylquinone enzymes characterized to date. Here we use X-ray crystallography and resonance Raman spectroscopy to identify the GoxA catalytic intermediate as a product Schiff base. Structural work additionally highlights features of the active site pocket that confer substrate specificity, intermediate stabilization, and catalytic activity. The unusual properties of GoxA are discussed within the context of the other tryptophylquinone enzymes.",
author = "Dante Avalos and Sinan Sabuncu and Mamounis, {Kyle J.} and Davidson, {Victor L.} and Pierre Mo{\"e}nne-Loccoz and Yukl, {Erik T.}",
note = "Funding Information: The authors acknowledge the staff at the Berkeley Center for Structural Biology at Lawrence Berkeley National Laboratory. The Berkeley Center for Structural Biology is supported in part by the National Institutes of Health, National Institute of General Medical Sciences, and the Howard Hughes Medical Institute. The Advanced Light Source is supported by the Director, Office of Science, Office of Basic Energy Sciences, of the U.S. Department of Energy under Contract DE-AC02-05CH11231. Funding Information: D.A. and S.S. contributed equally to this work. S.S. and P.M.-L. performed vibrational spectroscopy. D.A. and E.T.Y. crystallized the protein and determined structures. K.J.M. expressed and purified the protein. All authors contributed conceptually to the study and to writing the paper. Funding This research was supported by the National Institute of General Medical Sciences of the National Institutes of Health under Grant R37GM41574 (V.L.D.). Notes The authors declare no competing financial interest. Publisher Copyright: Copyright {\textcopyright} 2019 American Chemical Society.",
year = "2019",
month = feb,
day = "12",
doi = "10.1021/acs.biochem.8b01145",
language = "English (US)",
volume = "58",
pages = "706--713",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "6",
}