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Structural characterization of a putative recombinant L-amino acid oxidase from Leptospira interrogans.

Vaigundan, D and Yuvaraj, I and Sunita, P and Sekar, K and Murthy, MRN and Krishnaswamy, PR (2022) Structural characterization of a putative recombinant L-amino acid oxidase from Leptospira interrogans. In: Current Science, 123 (7). pp. 895-906.

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Official URL: https://doi.org/10.18520/cs/v123/i7/895-906


Amino acid oxidases (AOs) are flavin adenine dinucle-otide (FAD)-dependent dimeric enzymes that stereo specifically catalyse the deamination of an α-amino acid leading to an α-keto acid. Putative Leptospira interro-gans recombinant L-amino acid oxidase (Li-rLAO; lacking 20 residues corresponding to the N-terminal signal sequence) was cloned, expressed, purified, and its three-dimensional structure was determined by X-ray crystallography at a resolution of 1.8 à . The active site could be easily identified by the presence of electron density corresponding to a non-covalently bound FAD in both protomers of the dimeric enzyme. Structural analysis of Li-rLAO revealed that its polypeptide fold is similar to those of the previously determined homol-ogous structures as available in the Protein Data Bank. However, a substrate-binding residue found at the active site of other previously determined homologous struc-tures was not conserved in Li-rLAO, suggesting that its specificity may differ from those of earlier reported structures. Not surprisingly, Li-rLAO showed no activ-ity for most amino acids and amines; it exhibited a low activity only with L-arginine as the substrate. The cata-lytic properties of Li-rLAO could be rationalized in terms of its three-dimensional structure.

Item Type: Journal Article
Publication: Current Science
Publisher: Indian Academy of Sciences
Additional Information: The copyright for this article belongs to the Indian Academy of Sciences.
Keywords: Amino acid oxidase, dimeric enzyme, homologous structures, Leptospira interrogans, structural analysis.
Department/Centre: Division of Biological Sciences > Molecular Biophysics Unit
Division of Interdisciplinary Sciences > Computational and Data Sciences
Division of Interdisciplinary Sciences > Centre for Nano Science and Engineering
Date Deposited: 09 Nov 2022 09:01
Last Modified: 09 Nov 2022 09:01
URI: https://eprints.iisc.ac.in/id/eprint/77832

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