Structural and Spectroscopic Characterization of a Product Schiff Base Intermediate in the Reaction of the Quinoprotein Glycine Oxidase, GoxA

Dante Avalos, Sinan Sabuncu, Kyle J. Mamounis, Victor L. Davidson, Pierre Moenne-Loccoz, Erik T. Yukl

Research output: Contribution to journalArticle

1 Citation (Scopus)

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.

Original languageEnglish (US)
JournalBiochemistry
DOIs
StateAccepted/In press - Jan 1 2019

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Schiff Bases
Enzymes
Glycine
Oxidoreductases
Pseudoalteromonas
Deamination
Raman Spectrum Analysis
X ray crystallography
X Ray Crystallography
Substrate Specificity
Catalysis
Raman spectroscopy
Catalyst activity
Catalytic Domain
Proteins
Stabilization
glycine oxidase
Substrates

ASJC Scopus subject areas

  • Biochemistry

Cite this

Structural and Spectroscopic Characterization of a Product Schiff Base Intermediate in the Reaction of the Quinoprotein Glycine Oxidase, GoxA. / Avalos, Dante; Sabuncu, Sinan; Mamounis, Kyle J.; Davidson, Victor L.; Moenne-Loccoz, Pierre; Yukl, Erik T.

In: Biochemistry, 01.01.2019.

Research output: Contribution to journalArticle

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