Results 211 to 220 of about 8,038 (247)
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Electrophoresis, 2010
AbstractIsomerases involved in the metabolism of D/L‐amino acids represent promising therapeutic targets for treatment of disease. Herein, we report a tunable platform for the assessment of enzymatic kinetics involving amino acid isomerization by CE that offers improved selectivity and sensitivity over traditional methods.
Turlough M Finan, Philip Britz-Mckibbin
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AbstractIsomerases involved in the metabolism of D/L‐amino acids represent promising therapeutic targets for treatment of disease. Herein, we report a tunable platform for the assessment of enzymatic kinetics involving amino acid isomerization by CE that offers improved selectivity and sensitivity over traditional methods.
Turlough M Finan, Philip Britz-Mckibbin
exaly +3 more sources
FEBS Letters, 1994 In addition to the major cyclophilin-like peptidyl-prolyl cis/trans isomerases (PPIases) of Escherichia coli an enzyme of very low relative molecular mass (10.1 kDa) was discovered in this organism which gave first indication of the existence of a novel ...
Jens-U Rahfeld +2 more
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Localization of the essential histidine and carboxylate group in d-xylose isomerases [PDF]
Biochemical Journal, 1990 D-Xylose isomerases from different bacterial strains were chemically modified with histidine and carboxylate-specific reagents. The active-site residues were identified by amino acid sequence analysis of peptides recognized by differential peptide ...
J Van Damme +2 more
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Insect Science, 2022
AbstractTemperature is one of the most important environmental factors that affect organisms, especially ectotherms, due to its effects on protein stability. Understanding the general rules that govern thermostability changes in proteins to adapt high‐temperature environments is crucial.
Jianing, Yang +7 more
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AbstractTemperature is one of the most important environmental factors that affect organisms, especially ectotherms, due to its effects on protein stability. Understanding the general rules that govern thermostability changes in proteins to adapt high‐temperature environments is crucial.
Jianing, Yang +7 more
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Proteins: Structure, Function, and Bioinformatics, 2013
It is generally assumed that the amino acids that exist in all homologous enzymes correspond to residues that participate in catalysis, or that are essential for folding and stability. Although this holds for catalytic residues, the function of conserved noncatalytic residues is not clear.
Yolanda Aguirre +10 more
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It is generally assumed that the amino acids that exist in all homologous enzymes correspond to residues that participate in catalysis, or that are essential for folding and stability. Although this holds for catalytic residues, the function of conserved noncatalytic residues is not clear.
Yolanda Aguirre +10 more
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Introduction of unnatural amino acids into chalcone isomerase
Bioconjugate Chemistry, 1991The active site cysteine residue of chalcone isomerase was rapidly and selectively modified under denaturing conditions with a variety of electrophilic reagents. These denatured and modified enzyme were renatured to produce enzyme derivatives containing a series of unnatural amino acids in the active site.
R A, Bednar, C, McCaffrey, K, Shan
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Amino acid sequence of peptidyl‐prolyl isomerase a of fusarium sporotrichioides
Natural Toxins, 1996AbstractPeptidyl‐prolyl‐cis‐trans isomerase catalyzes the interconversion of the cis and trans isomers of the proline‐containing polypeptides and the folding process of proteins. This protein was known to be cyclophilin which has high binding affinity for cyclosporin A, a cyclic undecapeptide of fungal origin with potent immunosuppressive property ...
L P, Chow, M, Kamo, Y, Ueno, A, Tsugita
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Separation of amino acids in glucose isomerase crystal: Insight from molecular dynamics simulations
Journal of Chromatography A, 2009The separation of amino acids (Arg, Phe and Trp) in a liquid chromatography is investigated using molecular dynamics simulations. A bioorganic nanoporous material--glucose isomerase crystal--is used as the stationary phase and water as the mobile phase.
Hu, Z., Jiang, J.
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European Journal of Biochemistry, 1967
Rabbit muscle phosphoglucose isomerase was subjected to methylene blue and rose bengal sensitized photooxidation. This treatment caused the enzyme to lose activity quite rapidly with half‐lives of 2 to 10 minutes under the following conditions: pH 7.1; ionie strength, 0.11; temperature, 10°; enzyme concentration, 2 mg per ml.
G C, Chatterjee, E A, Noltmann
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Rabbit muscle phosphoglucose isomerase was subjected to methylene blue and rose bengal sensitized photooxidation. This treatment caused the enzyme to lose activity quite rapidly with half‐lives of 2 to 10 minutes under the following conditions: pH 7.1; ionie strength, 0.11; temperature, 10°; enzyme concentration, 2 mg per ml.
G C, Chatterjee, E A, Noltmann
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Biosynthesis of d-amino acid-containing peptides: Exploring the role of peptide isomerases
1998The discovery of D-amino acid residues in a growing number of gene-encoded peptides suggests that such biochemical modifications are more common than initially thought. In fact, the extent to which D-amino acids are incorporated into peptides by multicellular organisms probably has not been fully realized, since routine Edman sequencing does not ...
R A, Volkmann, S D, Heck
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