Three-Dimensional Structure of Thermostable D-Amino Acid Transaminase from the Archaeon Methanocaldococcus jannaschii DSM 2661

Autor:	T.N. Stekhanova, Alina K. Bakunova, E. Yu. Bezsudnova, Konstantin M. Boyko, A. Yu. Nikolaeva, Tatiana V. Rakitina, Vladimir Popov
Rok vydání:	2021
Předmět:	chemistry.chemical_classification biology Stereochemistry Thermophile Active site Methanocaldococcus jannaschii General Chemistry Condensed Matter Physics biology.organism_classification Transaminase Amino acid chemistry.chemical_compound Enzyme chemistry biology.protein General Materials Science Pyridoxal Amination
Zdroj:	Crystallography Reports. 66:802-807
ISSN:	1562-689X 1063-7745
Popis:	Pyridoxal 5′-phosphate (PLP)-dependent transaminases catalyze the stereospecific amino-group transfer from an amino acid or amine to ketone or keto acid. Transaminases are involved in amino acid metabolism in all organisms. Enzymes of this superfamily are widely used to develop biocatalysts for the stereoselective amination of organic compounds for fine organic synthesis. The brief biochemical characterization of thermostable fold type I PLP-dependent transaminase from the thermophilic archaeon Methanocaldococcus jannaschii DSM 2661 is reported. The crystal structure of this enzyme was determined at 1.8 A resolution. The structure of the functional dimer of the enzyme and the organization of its active site are compared with those of the close homologs.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::55ced141ca537b6f8a53bbda7eee0201 https://doi.org/10.1134/s1063774521050035 Zobrazit plný text záznamu Plný text ve formátu PDF Plný text ve formátu HTML
Nepřihlášeným uživatelům se plný text nezobrazuje	K zobrazení výsledku je třeba se přihlásit.