Enzyme Papers
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Curated feed of scientific journal publications and pre-prints related to biocatalysis and enzymology. Posting is automated.
Imine Reductase‐Mediated Regio‐ and Stereoselective Reductive Amination of Diamines
Imine Reductase‐Mediated Regio‐ and Stereoselective Reductive Amination of Diamines
Imine reductases (IREDs) have been employed as biocatalysts for the regioselective modification of diamines via reductive amination. The use of racemic diamines resulted in both regio- and enantio-se...
chemistry-europe.onlinelibrary.wiley.com
Binding of Zinc(II) to Apo‐Metallo‐β‐Lactamases: Characterization by Isothermal Titration Calorimetry
Binding of Zinc(II) to Apo‐Metallo‐β‐Lactamases: Characterization by Isothermal Titration Calorimetry
The first ITC investigation of Zn(II) binding to apo-metallo-β-lactamases. Stoichiometry, binding constant, enthalpy, and entropy changes were determined for six MβLs. The binding mode depends on the...
chemistry-europe.onlinelibrary.wiley.com
Enhancing ω-transaminase catalysis of bulky substrates guided by binding mechanism
Enhancing ω-transaminase catalysis of bulky substrates guided by binding mechanism - Nature Communications
This study combines enhanced sampling with experiments to reveal how bulky substrates enter and bind to ω-transaminases. Distal-site engineering balanced tunnel access and binding stability, yielding 106-fold activity and >99% selectivity.
nature.com
Enantioselective Alcohol Oxidation Reactions Catalyzed by Unspecific Peroxygenases
Enantioselective Alcohol Oxidation Reactions Catalyzed by Unspecific Peroxygenases
AbstractThe enantioselective oxidation of alcohols can be achieved via kinetic resolution of racemic alcohols or the desymmetrization of meso-diols. Biocat
pubs.acs.org
Substrate Length Controls Atropopeptide Complexity and Triggers Excision-Driven Scaffold Hop to Diketopiperazine Alkaloids
Substrate Length Controls Atropopeptide Complexity and Triggers Excision-Driven Scaffold Hop to Diketopiperazine Alkaloids
Abstract. Atropopeptides are a family of ribosomally synthesized and posttranslationally modified peptides (RiPPs) that share conserved cross-link-forming
pubs.acs.org
Directed evolution of laccase from Thermus thermophilus HB27 reveals a variant with enhanced high temperature catalytic activity and electrochemical properties
Directed evolution of laccase from Thermus thermophilus HB27 reveals a variant with enhanced high temperature catalytic activity and electrochemical properties
Laccases belong to the multicopper oxidase family (MCO). Compared with fungal laccases, bacterial laccases have high stability and activity under extreme pH and temperature conditions. Because of these characteristics, bacterial laccases have become highly impactful in industrial processes. In the present work, we engineered the Thermus thermophilus HB27 laccase (Tth-Lac) by directed evolution. The library had a size of 1.2 x105 colonies, and we screened mutants by malachite green decolorizatio…
biorxiv.org
Identification and Functional Characterization of UbiA-Type Terpene Synthases in Inonotus obliquus
Identification and Functional Characterization of UbiA-Type Terpene Synthases in Inonotus obliquus
AbstractInonotus obliquus (Chaga mushroom) is a medicinal basidiomycete rich in structurally diverse terpenoids, yet the biosynthetic enzymes responsible f
pubs.acs.org
Chemoenzymatic Proline Isotope Labeling for Solution and Magic-Angle Spinning Protein Nuclear Magnetic Resonance
Chemoenzymatic Proline Isotope Labeling for Solution and Magic-Angle Spinning Protein Nuclear Magnetic Resonance
AbstractThe prevalence of proline residues in intrinsically disordered proteins, functional hinges of enzymes, and protein interaction sites highlights the
pubs.acs.org
Substrate-Engaged Formation of Reactive Oxygen Intermediates in Metalloenzymes: Mechanisms and Implications for Biocatalysis
Substrate-Engaged Formation of Reactive Oxygen Intermediates in Metalloenzymes: Mechanisms and Implications for Biocatalysis
Abstract. Reactive oxygen intermediates in metalloenzymes are generally viewed as products of metal-centered O2 or H2O2 activation that are tuned by the su
pubs.acs.org
Characterisation of thermostable CYP116B reductase domains as modular electron transfer units for redox biocatalysis
Characterisation of thermostable CYP116B reductase domains as modular electron transfer units for redox biocatalysis | ChemRxiv
Electron transfer is a common bottleneck in redox biocatalysis. Here, we report the isolation of five cytochrome P450 reductase (CPR) domains from the thermophilic, self-sufficient CYP116B family. These enzymes have considerable industrial potential ...
chemrxiv.org
Defining the Catalytic Boundaries of N-Nitrosourea-Forming StzF/SznF and Related Metalloenzymes through Genome Mining and Mechanistic Analysis
Defining the Catalytic Boundaries of N-Nitrosourea-Forming StzF/SznF and Related Metalloenzymes through Genome Mining and Mechanistic Analysis | ChemRxiv
Enzymatic N–N bond formation is a rare and chemically challenging transformation in natural product biosynthesis. The non-heme iron metalloenzyme SznF catalyzes the formation of the N-nitrosourea phar...
chemrxiv.org
An Immobilized Marine Glycosyltransferase Acts as a Stabilized Biocatalyst for the Synthesis of Mannosylated Phosphoisoprenoids
An Immobilized Marine Glycosyltransferase Acts as a Stabilized Biocatalyst for the Synthesis of Mannosylated Phosphoisoprenoids
Mannosylated phosphoisoprenoids are generated by an immobilised glycosyltransferase as a sustainable approach towards the functionalisation of complex molecules.
advanced.onlinelibrary.wiley.com
Predicting Functional Diversity Within Enzyme Families: A Practical Perspective
Predicting Functional Diversity Within Enzyme Families: A Practical Perspective
Integrating machine learning into enzyme discovery requires navigating the trade-offs between data quantity and quality. This article provides a best-practice framework for developing robust predicto...
chemistry-europe.onlinelibrary.wiley.com
Chemoenzymatic Synthesis of (4R,7R)‐Zingiberene Enables Construction of nor‐Sesquiterpene Semiochemical Analogs
Chemoenzymatic Synthesis of (4<i>R</i>,7<i>R</i>)‐Zingiberene Enables Construction of <i>nor</i>‐Sesquiterpene Semiochemical Analogs
A five-enzyme chemoenzymatic synthesis of the insect-repellent (4R,7R)-zingiberene from the wild tomato (Solanum habrochaites) has been developed. This approach enabled the elucidation of the sesquit...
chemistry-europe.onlinelibrary.wiley.com
Recent Progress in Understanding the Mechanism of Formate Dehydrogenases
Recent Progress in Understanding the Mechanism of Formate Dehydrogenases
A hydride transfer mechanism for the molybdenum- and tungsten-containing formate dehydrogenases.
chemistry-europe.onlinelibrary.wiley.com
Predicting Functional Diversity Within Enzyme Families: A Practical Perspective
Predicting Functional Diversity Within Enzyme Families: A Practical Perspective
Integrating machine learning into enzyme discovery requires navigating the trade-offs between data quantity and quality. This article provides a best-practice framework for developing robust predicto...
chemistry-europe.onlinelibrary.wiley.com
One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives
One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives
The terminal sulfido ligand in mononuclear molybdoenzymes has been appreciated for almost 125 years, with the characterization of Schardinger's enzyme in cow's milk, now known to be xanthine oxidase,...
chemistry-europe.onlinelibrary.wiley.com
A Substrate-Permissive Vanadium Haloperoxidase in Type II Polyketide Biosynthesis Unlocks Non-Native Halogenation across Diverse Substrate Scaffolds
A Substrate-Permissive Vanadium Haloperoxidase in Type II Polyketide Biosynthesis Unlocks Non-Native Halogenation across Diverse Substrate Scaffolds
Abstract. Halogenated compounds are prevalent in natural and synthetic molecules, profoundly affecting molecular stability, physicochemical properties, and
pubs.acs.org
General Asymmetric Synthesis of Noncanonical Amino Acids
General Asymmetric Synthesis of Noncanonical Amino Acids
Abstract. Noncanonical amino acids (ncAAs) are valuable building blocks with applications spanning biology, material science, and pharmaceutical developmen
pubs.acs.org
Switching ATP‐Forming Phosphoryl‐Transfer Chemistry With a Restricted Set of Amino Acids
Switching ATP‐Forming Phosphoryl‐Transfer Chemistry With a Restricted Set of Amino Acids
Constraints on amino acid composition relevant to prebiotic chemistry reshape enzyme chemistry by replacing the canonical mechanism within a conserved protein fold with a distinct ATP-forming reactio....
onlinelibrary.wiley.com
A Cytochrome P450 Enzyme‐Catalyzed Acetyl Migration in Cyanogramide Biosynthesis
A Cytochrome P450 Enzyme‐Catalyzed Acetyl Migration in Cyanogramide Biosynthesis
Cyanogramide, a spirooxindole alkaloid with an imidazolidin-4-one core, is shown to be biosynthesized via a novel pathway. The P450 enzyme CyaI is revealed to catalyze an unusual intramolecular cycli....
onlinelibrary.wiley.com
Directed evolution of a thermostable family-A DNA polymerase into a reverse transcriptase for 2'-modified RNA
Directed evolution of a thermostable family-A DNA polymerase into a reverse transcriptase for 2'-modified RNA
RNA-based therapeutics increasingly rely on nuclease-resistant xeno-nucleic acids (XNAs), but engineering polymerases capable of reading and amplifying these non-canonical substrates remains a major challenge. Natural DNA polymerases cannot process C2' sugar modifications, and the complete structural determinants governing this limitation remain poorly understood, limiting rational design strategies. In this study, we apply directed evolution methods to Thermus thermophilus DNA polymerase using…
biorxiv.org
Selective Ligand Replacement Leads to Carbene Complexes as Catalysts in Proteins
Selective Ligand Replacement Leads to Carbene Complexes as Catalysts in Proteins | ChemRxiv
Artificial metalloenzymes (ArMs) that incorporate organometallic fragments through direct metal–protein coordination open the door to unlock the full evolutionary potential of the protein scaffold to ...
chemrxiv.org
Unanticipated intermediates during isopenicillin N synthase catalysis identified by time-resolved X-ray free-electron laser studies
Unanticipated intermediates during isopenicillin N synthase catalysis identified by time-resolved X-ray free-electron laser studies - Nature Catalysis
The structural basis of key intermediates in isopenicillin N synthase catalysis, underlying β-lactam biosynthesis, has remained incomplete. Now time-resolved X-ray free-electron laser studies capture transient states and reveal how protein dynamics and solvent networks govern oxygen activation and ring formation.
nature.com
Publisher Correction: Several multiple sequence alignment-perturbing methods enhance AlphaFold3 sampling of alternative protein states
Publisher Correction: Several multiple sequence alignment-perturbing methods enhance AlphaFold3 sampling of alternative protein states - Communications Chemistry
Communications Chemistry - Publisher Correction: Several multiple sequence alignment-perturbing methods enhance AlphaFold3 sampling of alternative protein states
nature.com
Photobiocatalytic Diastereo- and Enantioselective Synthesis of Non-Canonical Amino Acids Bearing Challenging Stereochemical Dyads and Triads
Photobiocatalytic Diastereo- and Enantioselective Synthesis of Non-Canonical Amino Acids Bearing Challenging Stereochemical Dyads and Triads
Catalyst-controlled stereodivergent synthesis of acyclic molecules bearing multiple stereogenic centers remains a longstanding challenge in asymmetric catalysis, particularly through intermolecular radical C–C coupling. Here, we report the directed evolution of pyridoxal 5′-phosphate (PLP)-dependent biocatalysts for the stereodivergent synthesis of non canonical amino acids bearing either skipped α, γ-stereochemical dyads or contiguous α, β, γ-stereochemical triads. Starting from a thermophilic…
biorxiv.org
Exploring the substrate specificity and catalytic mechanism in a PAPS independent ASST from Salmonella typhimurium
Exploring the substrate specificity and catalytic mechanism in a PAPS independent ASST from Salmonella typhimurium
Sulfation plays an important role in many metabolic processes such as substrate detoxification, solubilization or activation. The enzymes responsible for these reactions, sulfotransferases, occur in all domains of life and can be classified in two major, evolutionary independent groups, PAPS dependent and PAPS independent or arysulfate sulfotransferases (ASST) enzymes. Besides the fact that they play key roles in biological functions, sulfotransferases can be interesting enzymatic tools to sele…
biorxiv.org
Sequence Similarity Network-Guided Discovery of a Sequence-Tolerant Cyanobactin Protease Clade for Site-Selective Peptide and Protein Modification
Sequence Similarity Network-Guided Discovery of a Sequence-Tolerant Cyanobactin Protease Clade for Site-Selective Peptide and Protein Modification
Abstract. Proteases responsible for leader peptide removal are ubiquitous in ribosomally synthesized and post-translationally modified peptide (RiPP) biosy
pubs.acs.org
Correction to “Experimental and Computational Elucidation of C( sp 3 )–H Fluorination Barriers in an Iron(II)- and 2-Oxoglutarate-Dependent Halogenase”
Correction to “Experimental and Computational Elucidation of C(sp3)–H Fluorination Barriers in an Iron(II)- and 2-Oxoglutarate-Dependent Halogenase”
Correction
pubs.acs.org
Asymmetric enzymatic hydrophosphorylation through O2 activation
Asymmetric enzymatic hydrophosphorylation through O2 activation
Enzymatic carbon-phosphorus bond formation is extremely rare in nature, limiting biocatalytic access to phosphorus-containing compounds that are widely used in pharmaceuticals and agrochemicals. Here,...
science.org