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Chem Rev ; 118(1): 73-118, 2018 01 10.
Artículo en Inglés | MEDLINE | ID: mdl-28497955

RESUMEN

Ammonia-lyases and aminomutases are mechanistically and structurally diverse enzymes which catalyze the deamination and/or isomerization of amino acids in nature by cleaving or shifting a C-N bond. Of the many protein families in which these enzyme activities are found, only a subset have been employed in the synthesis of optically pure fine chemicals or in medical applications. This review covers the natural diversity of these enzymes, highlighting particular enzyme classes that are used within industrial and medical biotechnology. These highlights detail the discovery and mechanistic investigations of these commercially relevant enzymes, along with comparisons of their various applications as stand-alone catalysts, components of artificial biosynthetic pathways and biocatalytic or chemoenzymatic cascades, and therapeutic tools for the potential treatment of various pathologies.


Asunto(s)
Amoníaco-Liasas/metabolismo , Transaminasas/metabolismo , Amoníaco-Liasas/clasificación , Amoníaco-Liasas/uso terapéutico , Bacterias/enzimología , Biocatálisis , Humanos , Transferasas Intramoleculares/clasificación , Transferasas Intramoleculares/metabolismo , Transferasas Intramoleculares/uso terapéutico , Modelos Moleculares , Fenilanina Amoníaco-Liasa/química , Fenilanina Amoníaco-Liasa/clasificación , Fenilanina Amoníaco-Liasa/metabolismo , Especificidad por Sustrato , Transaminasas/clasificación , Transaminasas/uso terapéutico
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