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Mechanistic insights into the dual activities of the single active site of l-lysine oxidase/monooxygenase from sp. AIU 813.
J Biol Chem
August 2020
Department of Biochemistry and Center for Excellence in Protein and Enzyme Technology, Faculty of Science, Mahidol University, Bangkok, Thailand
l-Lysine oxidase/monooxygenase (l-LOX/MOG) from sp. AIU 813 catalyzes the mixed bioconversion of l-amino acids, particularly l-lysine, yielding an amide and carbon dioxide by an oxidative decarboxylation ( apparent monooxygenation), as well as oxidative deamination (hydrolysis of oxidized product), resulting in α-keto acid, hydrogen peroxide (HO), and ammonia. Here, using high-resolution MS and monitoring transient reaction kinetics with stopped-flow spectrophotometry, we identified the products from the reactions of l-lysine and l-ornithine, indicating that besides decarboxylating imino acids ( 5-aminopentanamide from l-lysine), l-LOX/MOG also decarboxylates keto acids (5-aminopentanoic acid from l-lysine and 4-aminobutanoic acid from l-ornithine).
View Article and Find Full Text PDFA Protein-derived Oxygen Is the Source of the Amide Oxygen of Nitrile Hydratases.
J Biol Chem
April 2016
From the Department of Chemistry, University of Utah, Salt Lake City, Utah, 84112 and
Nitrile hydratase metalloenzymes are unique and important biocatalysts that are used industrially to produce high value amides from their corresponding nitriles. After more than three decades since their discovery, the mechanism of this class of enzymes is becoming clear with evidence from multiple recent studies that the cysteine-derived sulfenato ligand of the active site metal serves as the nucleophile that initially attacks the nitrile. Herein we describe the first direct evidence from solution phase catalysis that the source of the product carboxamido oxygen is the protein.
View Article and Find Full Text PDFHigh-resolution single-molecule fluorescence imaging of zeolite aggregates within real-life fluid catalytic cracking particles.
Angew Chem Int Ed Engl
February 2015
Debye Institute for Nanomaterials Science, Faculty of Science, Utrecht University, Universiteitsweg 99, 3584 CG, Utrecht (The Netherlands).
Fluid catalytic cracking (FCC) is a major process in oil refineries to produce gasoline and base chemicals from crude oil fractions. The spatial distribution and acidity of zeolite aggregates embedded within the 50-150 μm-sized FCC spheres heavily influence their catalytic performance. Single-molecule fluorescence-based imaging methods, namely nanometer accuracy by stochastic chemical reactions (NASCA) and super-resolution optical fluctuation imaging (SOFI) were used to study the catalytic activity of sub-micrometer zeolite ZSM-5 domains within real-life FCC catalyst particles.
View Article and Find Full Text PDFSuper-resolution mapping of photogenerated electron and hole separation in single metal-semiconductor nanocatalysts.
J Am Chem Soc
January 2014
Ames Laboratory, U.S. Department of Energy, and Department of Chemistry, Iowa State University, Ames, Iowa 50011, United States.
Metal-semiconductor heterostructures are promising visible light photocatalysts for many chemical reactions. Here, we use high-resolution superlocalization imaging to reveal the nature and photocatalytic properties of the surface reactive sites on single Au-CdS hybrid nanocatalysts. We experimentally reveal two distinct, incident energy-dependent charge separation mechanisms that result in completely opposite photogenerated reactive sites (e(-) and h(+)) and divergent energy flows on the hybrid nanocatalysts.
View Article and Find Full Text PDFAminolaevulinic acid synthase of Rhodobacter capsulatus: high-resolution kinetic investigation of the structural basis for substrate binding and catalysis.
Biochem J
April 2013
Institute of Microbiology, Technical University of Braunschweig, Spielmannstrasse 7, D-38106 Braunschweig, Germany.
The first enzyme of haem biosynthesis, ALAS (5-aminolaevulinic acid synthase), catalyses the pyridoxal 5'-phosphate-dependent condensation of glycine and succinyl-CoA to 5-aminolaevulinic acid, CO(2) and CoA. The crystal structure of Rhodobacter capsulatus ALAS provides the first snapshots of the structural basis for substrate binding and catalysis. To elucidate the functional role of single amino acid residues in the active site for substrate discrimination, substrate positioning, catalysis and structural protein rearrangements, multiple ALAS variants were generated.
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