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The Escherichia coli Periplasmic Aldehyde Oxidoreductase Is an Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes.

Correia MA, Otrelo-Cardoso AR, Schwuchow V, Sigfridsson Clauss KG, Haumann M, Romão MJ, Leimkühler S, Santos-Silva T
ACS Chem Biol 11 2923-2935 (2016)
Cited: 11 times
EuropePMC logo PMID: 27622978

Abstract

The xanthine oxidase (XO) family comprises molybdenum-dependent enzymes that usually form homodimers (or dimers of heterodimers/trimers) organized in three domains that harbor two [2Fe-2S] clusters, one FAD, and a Mo cofactor. In this work, we crystallized an unusual member of the family, the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli. This is the first example of an E. coli protein containing a molybdopterin-cytosine-dinucleotide cofactor and is the only heterotrimer of the XO family so far structurally characterized. The crystal structure revealed the presence of an unexpected [4Fe-4S] cluster, anchored to an additional 40 residues subdomain. According to phylogenetic analysis, proteins containing this cluster are widely spread in many bacteria phyla, putatively through repeated gene transfer events. The active site of PaoABC is highly exposed to the surface with no aromatic residues and an arginine (PaoC-R440) making a direct interaction with PaoC-E692, which acts as a base catalyst. In order to understand the importance of R440, kinetic assays were carried out, and the crystal structure of the PaoC-R440H variant was also determined.

Reviews citing this publication (5)

  1. Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria. Zhong Q, Kobe B, Kappler U. Front Microbiol 11 615860 (2020)
  2. Evolution, expression, and substrate specificities of aldehyde oxidase enzymes in eukaryotes. Terao M, Garattini E, Romão MJ, Leimkühler S. J Biol Chem 295 5377-5389 (2020)
  3. Coping with inevitable accidents in metabolism. Danchin A. Microb Biotechnol 10 57-72 (2017)
  4. Gut Microbiota Metabolism of Azathioprine: A New Hallmark for Personalized Drug-Targeted Therapy of Chronic Inflammatory Bowel Disease. Lazarević S, Đanic M, Al-Salami H, Mooranian A, Mikov M. Front Pharmacol 13 879170 (2022)
  5. Structure and electrochemistry of proteins harboring iron-sulfur clusters of different nuclearities. Part I. [4Fe-4S]+[2Fe-2S] iron-sulfur proteins. Zanello P. J Struct Biol 200 1-19 (2017)

Articles citing this publication (6)

  1. Enzymatic Preparation of 2,5-Furandicarboxylic Acid (FDCA)-A Substitute of Terephthalic Acid-By the Joined Action of Three Fungal Enzymes. Karich A, Kleeberg SB, Ullrich R, Hofrichter M. Microorganisms 6 E5 (2018)
  2. Impact of the Dimethyl Sulfoxide Reductase Superfamily on the Evolution of Biogeochemical Cycles. Wells M, Kim M, Akob DM, Basu P, Stolz JF. Microbiol Spectr e0414522 (2023)
  3. Discriminating Susceptibility of Xanthine Oxidoreductase Family to Metals. Steunou AS, Babot M, Durand A, Bourbon ML, Liotenberg S, Miotello G, Armengaud J, Ouchane S. Microbiol Spectr 11 e0481422 (2023)
  4. Structural preferences of cysteine sulfinic acid: The sulfinate engages in multiple local interactions with the peptide backbone. Urmey AR, Zondlo NJ. Free Radic Biol Med 148 96-107 (2020)
  5. Crystal structure of an aldehyde oxidase from Methylobacillus sp. KY4400. Uchida H, Mikami B, Yamane-Tanabe A, Ito A, Hirano K, Oki M. J Biochem 163 321-328 (2018)
  6. Integrated pathway mining and selection of an artificial CYP79-mediated bypass to improve benzylisoquinoline alkaloid biosynthesis. Takenaka M, Kamasaka K, Daryong K, Tsuchikane K, Miyazawa S, Fujihana S, Hori Y, Vavricka CJ, Hosoyama A, Kawasaki H, Shirai T, Araki M, Nakagawa A, Minami H, Kondo A, Hasunuma T. Microb Cell Fact 23 178 (2024)


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