Structural and biochemical characterization of the prenylated flavin mononucleotide-dependent indole-3-carboxylic acid decarboxylase.

Gahloth, Deepankar, Fisher, Karl, Payne, Karl AP ORCID: 0000-0002-6331-6374, Cliff, Matthew ORCID: 0000-0002-7482-0234, Levy, Colin ORCID: 0000-0002-9724-310X and Leys, David (2022) Structural and biochemical characterization of the prenylated flavin mononucleotide-dependent indole-3-carboxylic acid decarboxylase. The Journal of biological chemistry, 298 (4). 101771-.

Access the full-text of this item by clicking on the Open Access link.

PDF
Structural and biochemical characterization of the prenylated flavin mononucleotide-dependent indole-3-carboxylic acid decar.pdf - Published version
Download (2MB) | Preview

Official URL: http://dx.doi.org/10.1016/j.jbc.2022.101771

Abstract

The ubiquitous UbiD family of reversible decarboxylases is implicated in a wide range of microbial processes and depends on the prenylated flavin mononucleotide cofactor for catalysis. However, only a handful of UbiD family members have been characterized in detail, and comparison between these has suggested considerable variability in enzyme dynamics and mechanism linked to substrate specificity. In this study, we provide structural and biochemical insights into the indole-3-carboxylic acid decarboxylase, representing an UbiD enzyme activity distinct from those previously studied. Structural insights from crystal structure determination combined with small-angle X-ray scattering measurements reveal that the enzyme likely undergoes an open-closed transition as a consequence of domain motion, an event that is likely coupled to catalysis. We also demonstrate that the indole-3-carboxylic acid decarboxylase can be coupled with carboxylic acid reductase to produce indole-3-carboxyaldehyde from indole + CO<sub>2</sub> under ambient conditions. These insights provide further evidence for a common mode of action in the widespread UbiD enzyme family.

Item Type:	Article
Uncontrolled Keywords:	Flavin Mononucleotide, Carboxy-Lyases, Protein Structure, Tertiary, Structure-Activity Relationship, Substrate Specificity, Models, Molecular
Divisions:	Faculty of Health and Life Sciences Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User:	Symplectic Admin
Date Deposited:	17 Oct 2022 14:47
Last Modified:	18 Jan 2023 20:36
DOI:	10.1016/j.jbc.2022.101771
Open Access URL:	https://doi.org/10.1016/j.jbc.2022.101771
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3165554