Results 11 to 20 of about 632 (113)
, 2023 ɑ-Hydroxy acids are organic compounds omnipresent in the living world and can be considered as building blocks in organic synthesis. However, racemases and epimerases of ɑ-hydroxy acids are poorly known. Among them, lactate racemase (LarA) was shown to require a unique nickel-containing cofactor, the nickel-pincer nucleotide(NPN.
Urdiain-Arraiza, Julian +1 more
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Frontispiece: Through the Looking Glass: Chiral Recognition of Substrates and Products at the Active Sites of Racemases and Epimerases [PDF]
Chemistry – A European Journal, 2020 Stephen L. Bearne
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Structure and inhibition of diaminopimelic acid epimerase by slow-binding α-methyl amino acids. [PDF]
Protein SciAbstract Cofactor‐independent racemases and epimerases produce D‐amino acids from their L‐isomers for a variety of biological processes. These enzymes operate via an unusual mechanism that relies on an active site cysteine thiolate (pKa ~ 8.5) to deprotonate an amino acid α‐carbon (pKa ~ 29) and are of interest not only because of their biocatalytic ...
Lamer T +8 more
europepmc +2 more sources
Hydroxy acids (HAs) are organic carboxylic acids omnipresent in the living world, and are essential to various industries, including food, cosmetics, and pharmaceuticals. Recently, a superfamily of nickel-dependent HA racemases and epimerases using the nickel-pincer nucleotide (NPN) cofactor was discovered: the LarA superfamily. These enzymes, known as
Urdiain-Arraiza, Julian
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Genomic context analysis enables the discovery of an unusual NAD-dependent racemase in phosphonate catabolism. [PDF]
FEBS JThe authors identify PbfF (previously annotated as a NAD‐dependent dehydrogenase) as a hitherto unknown enzyme in phosphonate catabolism. Guided by genome context analysis, they show that PbfF is actually a racemase, serving to degrade the natural compound (S)‐2‐amino‐1‐hydroxyethylphosphonate (S‐HAEP).
Ruffolo F +8 more
europepmc +2 more sources
The conundrum in enzymatic reactions related to biosynthesis of d-amino acids in bacteria. [PDF]
FEBS J, 2022 The synthesis of peptidoglycan in the hyperthermophile and anaerobic Gram‐negative bacterium Thermotoga maritima requires the d‐enantiomer of the amino acid glutamate. Since this bacterium does not possess a broad‐spectrum racemase to convert l‐amino acids into d‐amino acids, a versatile enzyme, named TM0831, evolved the ability to catalyse both a d ...
Pollegioni L, Molla G.
europepmc +2 more sources
Structural Basis for the Catalysis and Substrate Specificity of a LarA Racemase with a Broad Substrate Spectrum. [PDF]
ACS CatalThe LarA family consists of diverse racemases/epimerases that interconvert the diastereomers of α-hydroxyacids by using a nickel-pincer nucleotide (NPN) cofactor.
Gatreddi S +4 more
europepmc +2 more sources
Biocatalytic Synthesis Using Self‐Assembled Polymeric Nano‐ and Microreactors
Angewandte Chemie, Volume 134, Issue 52, December 23, 2022., 2022 The use of polymeric systems for bioconversion is an efficient and recyclable technology for the future industry due to its zero‐pollution features. This Review focuses on self‐assembled polymeric nano‐ and micro‐sized structures and their application as biocatalytic reactors for chemical synthesis, including polymersomes, reverse micelles, polymer ...
Yangxin Wang +3 more
wiley +2 more sources
Mycobacterium tuberculosis: Pathogenesis and therapeutic targets
MedComm, Volume 4, Issue 5, October 2023., 2023 In this review, we summarize the pathogenesis of TB infection, therapeutic targets, and corresponding modulators, including first‐line medications, current clinical trial drugs and molecules in preclinical assessment. Our review provides valuable insights for future antituberculosis drug development efforts.
Jiaxing Yang +3 more
wiley +1 more source
リボソームペプチドの複数アミノ酸残基を異性化する新規エピメラーゼ [PDF]
, 2023 Salinipeptins, grisemycin, and cypemycin are ribosomally synthesized and post-translationally modified peptides (RiPPs). Among these, salinipeptins were reported to comprise 22 amino acid residues with multiple D-amino acids, and its biosynthetic gene ...
Xiao, Wanlu
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