Characterization of haloacid dehalogenase superfamily acid phosphatase from Staphylococcus lugdunensis.

Autor: Kaur H; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Rode S; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Kp S; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Mahto JK; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Alam MS; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Gupta DN; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Kar B; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Singla J; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India; Department of Computer Science and Engineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Kumar P; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India., Sharma AK; Department of Biosciences and Bioengineering, Indian Institute of Technology Roorkee, Roorkee-247667, India. Electronic address: ashwani.sharma@bt.iitr.ac.in.
Jazyk: angličtina
Zdroj: Archives of biochemistry and biophysics [Arch Biochem Biophys] 2024 Mar; Vol. 753, pp. 109888. Date of Electronic Publication: 2024 Jan 15.
DOI: 10.1016/j.abb.2024.109888
Abstrakt: The haloacid dehalogenase superfamily implicated in bacterial pathogenesis comprises different enzymes having roles in many metabolic pathways. Staphylococcus lugdunensis, a Gram-positive bacterium, is an opportunistic human pathogen causing infections in the central nervous system, urinary tract, bones, peritoneum, systemic conditions and cutaneous infection. The haloacid dehalogenase superfamily proteins play a significant role in the pathogenicity of certain bacteria, facilitating invasion, survival, and proliferation within host cells. The genome of S. lugdunensis encodes more than ten proteins belonging to this superfamily. However, none of them have been characterized. The present work reports the characterization of one of the haloacid dehalogenase superfamily proteins (SLHAD1) from Staphylococcus lugdunensis. The functional analysis revealed that SLHAD1 is a metal-dependent acid phosphatase, which catalyzes the dephosphorylation of phosphorylated metabolites of cellular pathways, including glycolysis, gluconeogenesis, nucleotides, and thiamine metabolism. Based on the substrate specificity and genomic analysis, the physiological function of SLHAD1 in thiamine metabolism has been tentatively assigned. The crystal structure of SLHAD1, lacking 49 residues at the C-terminal, was determined at 1.7 Å resolution with a homodimer in the asymmetric unit. It was observed that SLHAD1 exhibited time-dependent cleavage at a specific point, occurring through a self-initiated process. A combination of bioinformatics, biochemical, biophysical, and structural studies explored unique features of SLHAD1. Overall, the study revealed a detailed characterization of a critical enzyme of the human pathogen Staphylococcus lugdunensis, associated with several life-threatening infections.
(Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze: MEDLINE
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