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13 Amino Acid Racemases and Epimerases

The Enzymes, 1972
Publisher Summary This chapter describes the assay methods and mechanism of action of amino acid racemases and epimerases. Amino acid racemases catalyze the formation of a racemic mixture from either the D or L form of a free amino acid by equilibrating configuration at the α-carbon.
Elijah Adams
exaly   +3 more sources

Through the Looking Glass: Chiral Recognition of Substrates and Products at the Active Sites of Racemases and Epimerases

Chemistry - A European Journal, 2020
AbstractUnlike most enzymes, which exhibit stereospecific substrate binding, racemases and epimerases bind and catalyze the reversible interconversion of enantiomeric and epimeric pairs of substrates. Over the past 15 years, a growing number of racemase and epimerase structures have been solved, furnishing insights into the nature of chiral recognition
Stephen L Bearne
exaly   +4 more sources

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Application of circular dichroism-based assays to racemases and epimerases: Recognition and catalysis of reactions of chiral substrates by mandelate racemase

Methods in Enzymology, 2023
Racemases and epimerases have attracted much interest because of their astonishing ability to catalyze the rapid α-deprotonation of carbon acid substrates with high pKa values (∼13-30) leading to the formation of d-amino acids or various carbohydrate diastereomers that serve important roles in both normal physiology and pathology.
Stephen L Bearne, Joshua A Hayden
exaly   +3 more sources

Design and evaluation of substrate–product analog inhibitors for racemases and epimerases utilizing a 1,1-proton transfer mechanism

Methods in Enzymology, 2023
Racemases and epimerases catalyze the inversion of stereochemistry at asymmetric carbon atoms to generate stereoisomers that often play important roles in normal and pathological physiology. Consequently, there is interest in developing inhibitors of these enzymes for drug discovery.
Stephen L Bearne
exaly   +3 more sources

Common catalytic features among cofactor independent racemases and epimerases: A computational perspective

, 2010
STENTA, MARCO, ALTOE', PIERO, Dal Peraro M., GARAVELLI, MARCO, BOTTONI, ANDREA   +4 more
openaire   +2 more sources

Crystal structure of substrate-bound bifunctional proline racemase/hydroxyproline epimerase from a hyperthermophilic archaeon

Biochemical and Biophysical Research Communications, 2019
The hypothetical OCC_00372 protein from Thermococcus litoralis is a member of the ProR superfamily from hyperthermophilic archaea and exhibits unique bifunctional proline racemase/hydroxyproline 2-epimerase activity. However, the molecular mechanism of the broad substrate specificity and extreme thermostability of this enzyme (TlProR) remains unclear ...
Yasunori Watanabe, Seiya Watanabe, Yoshika Itoh, Yasuo Watanabe   +3 more
openaire   +2 more sources

Crystal structure of the novel amino-acid racemase isoleucine 2-epimerase fromLactobacillus buchneri

Acta Crystallographica Section D Structural Biology, 2017
Crystal structures ofLactobacillus buchneriisoleucine 2-epimerase, a novel branched-chain amino-acid racemase, were determined for the enzyme in the apo form, in complex with pyridoxal 5′-phosphate (PLP), in complex withN-(5′-phosphopyridoxyl)-L-isoleucine (PLP-L-Ile) and in complex withN-(5′-phosphopyridoxyl)-D-allo-isoleucine (PLP-D-allo-Ile) at ...
Junji, Hayashi, Yuta, Mutaguchi, Yume, Minemura, Noriko, Nakagawa, Kazunari, Yoneda, Taketo, Ohmori, Toshihisa, Ohshima, Haruhiko, Sakuraba   +7 more
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Crystal Structure of Diaminopimelate Epimerase from Arabidopsis thaliana, an Amino Acid Racemase Critical for l-Lysine Biosynthesis

Journal of Molecular Biology, 2009
Diaminopimelate (DAP) epimerase is a key enzyme for the biosynthesis of lysine in plants. Lysine is an essential dietary nutrient for mammals. In both plants and bacteria, DAP epimerase catalyzes the interconversion of LL-DAP and DL(meso)-DAP. The absence of a mammalian homolog makes DAP epimerase a promising target for the design of novel herbicides ...
Bindu, Pillai, Vijayalakshmi A, Moorthie, Marco J, van Belkum, Sandra L, Marcus, Maia M, Cherney, Christopher M, Diaper, John C, Vederas, Michael N G, James   +7 more
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Homology of 1-Aminocyclopropane-1-carboxylate Synthase, 8-Amino-7-oxononanoate Synthase, 2-Amino-6-caprolactam Racemase, 2,2-Dialkylglycine Decarboxylase, Glutamate-1-semialdehyde 2,1-Aminomutase and Isopenicillin-N-Epimerase with Aminotransferases

Biochemical and Biophysical Research Communications, 1994
Profile analysis showed the title enzymes to be homologous with the aminotransferases. 1-Aminocyclopropane-1-carboxylate synthase is closely related to subgroup I of aminotransferases which includes aspartate, alanine, histidinol-phosphate, tyrosine and phenylalanine aminotransferase.
Mehta PK, Christen P
openaire   +3 more sources

Biochemical Tools for NMR Structural Elucidation of Peptides and Investigations of Cofactor-Independent Racemases and Epimerases

Proteins and peptides produced by the ribosome are initially composed of the 20 proteinogenic amino acids, 19 of which are chiral and have an L-configuration. One class of ribosomally synthesized peptides of interest are called bacteriocins. Bacteriocins are antibacterial peptides and exert their effects through a wide variety of mechanisms.
openaire   +1 more source