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Incorporation of pyridoxal-5'-phosphate into the apoenzyme: A structural study of D-amino acid transaminase from Haliscomenobacter hydrossis.
Biochim Biophys Acta Proteins Proteom
January 2025
Bach Institute of Biochemistry, Research Centre of Biotechnology of the Russian Academy of Sciences, Moscow, Russia. Electronic address:
Pyridoxal-5'-phosphate (PLP)-dependent transaminases are key enzymes of amino acid metabolism in cells and remarkable biocatalysts of stereoselective amination for process chemistry applications. As cofactor-dependent enzymes, transaminases are prone to cofactor leakage. Here we discuss the holoenzyme-apoenzyme interconversion and the kinetics of PLP incorporation into the apo form of a PLP-dependent transaminase from Haliscomenobacter hydrossis.
View Article and Find Full Text PDFF-NMR Probing of Ion-Induced Conformational Changes in Detergent-Solubilized and Nanodisc-Reconstituted NCX_Mj.
Int J Mol Sci
June 2024
Department of Physiology and Pharmacology, Faculty of Medicine, Tel-Aviv University, Tel Aviv 69978, Israel.
Consecutive interactions of 3Na or 1Ca with the Na/Ca exchanger (NCX) result in an alternative exposure (access) of the cytosolic and extracellular vestibules to opposite sides of the membrane, where ion-induced transitions between the outward-facing (OF) and inward-facing (IF) conformational states drive a transport cycle. Here, we investigate sub-state populations of apo and ion-bound species in the OF and IF states by analyzing detergent-solubilized and nanodisc-reconstituted preparations of NCX_Mj with F-NMR. The F probe was covalently attached to the cysteine residues at entry locations of the cytosolic and extracellular vestibules.
View Article and Find Full Text PDFSide-chain dynamics of the α -adrenergic receptor determined by NMR via methyl relaxation.
Protein Sci
November 2023
Department of Chemistry, University of Zurich, Zurich, Switzerland.
G protein-coupled receptors (GPCRs) are medically important membrane proteins that sample inactive, intermediate, and active conformational states characterized by relatively slow interconversions (~μs-ms). On a faster timescale (~ps-ns), the conformational landscape of GPCRs is governed by the rapid dynamics of amino acid side chains. Such dynamics are essential for protein functions such as ligand recognition and allostery.
View Article and Find Full Text PDFVisualizing the transiently populated closed-state of human HSP90 ATP binding domain.
Nat Commun
December 2022
Univ. Grenoble Alpes, CNRS, CEA, Institut de Biologie Structurale (IBS), 71, avenue des martyrs, F-38044, Grenoble, France.
HSP90 are abundant molecular chaperones, assisting the folding of several hundred client proteins, including substrates involved in tumor growth or neurodegenerative diseases. A complex set of large ATP-driven structural changes occurs during HSP90 functional cycle. However, the existence of such structural rearrangements in apo HSP90 has remained unclear.
View Article and Find Full Text PDFBiophysical and Structural Characterization of Ribulose-5-phosphate Epimerase from .
ACS Omega
January 2022
Department of Biotechnology & Bioinformatics, School of Life Sciences, University of Hyderabad, Prof. C. R. Rao Road, Hyderabad 500046, India.
Pentose phosphate pathway (PPP) plays a crucial role in the maintenance of NADPH/NADP homeostasis and provides protection against oxidative stress through detoxification of the reactive oxygen species. Ribulose-5-phosphate epimerase (RPE) participates in catalysis of the interconversion of ribulose-5-phosphate (Ru5P) to xylulose-5-phosphate (Xu5P) during PPP, however the structural attributes of this enzyme are still underexplored in many human pathogens including leishmanial parasites. The present study focuses upon cloning, purification and characterization of RPE of (RPE) using various biophysical and structural approaches.
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