Characterization of aminoacrylate intermediates of pyridoxal-5'-phosphate dependent enzymes.
Methods Enzymol
; 685: 199-224, 2023.
Article
em En
| MEDLINE
| ID: mdl-37245902
ABSTRACT
Pyridoxal-5'-phosphate (PLP) Schiff's bases of 2-aminoacrylate are intermediates in ß-elimination and ß-substitution reaction of PLP-dependent enzymes. These enzymes are found in two major families, the α-, or aminotransferase, superfamily, and the ß-family. While the α-family enzymes primarily catalyze ß-eliminations, the ß-family enzymes catalyze both ß-elimination and ß-substitution reactions. Tyrosine phenol-lyase (TPL), which catalyzes the reversible elimination of phenol from l-tyrosine, is an example of an α-family enzyme. Tryptophan synthase catalyzes the irreversible formation of l-tryptophan from l-serine and indole, and is an example of a ß-family enzyme. The identification and characterization of aminoacrylate intermediates in the reactions of both of these enzymes is discussed. The use of UV-visible absorption and fluorescence spectroscopy, X-ray and neutron crystallography, and NMR spectroscopy to identify aminoacrylate intermediates in these and other PLP enzymes is presented.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Triptofano Sintase
/
Tirosina Fenol-Liase
Limite:
Humans
Idioma:
En
Revista:
Methods Enzymol
Ano de publicação:
2023
Tipo de documento:
Article