The Uncommon Active Site of D-Amino Acid Transaminase from <i>Haliscomenobacter hydrossis</i>: Biochemical and Structural Insights into the New Enzyme

The Uncommon Active Site of D-Amino Acid Transaminase from <i>Haliscomenobacter hydrossis</i>: Biochemical and Structural Insights into the New Enzyme

Among industrially important pyridoxal-5’-phosphate (PLP)-dependent transaminases of fold type IV D-amino acid transaminases are the least studied. However, the development of cascade enzymatic processes, including the synthesis of D-amino acids, renewed interest in their study. Here, we describe th...

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Bibliographic Details
Main Authors: Alina K. Bakunova, Alena Yu. Nikolaeva, Tatiana V. Rakitina, Tatiana Y. Isaikina, Maria G. Khrenova, Konstantin M. Boyko, Vladimir O. Popov, Ekaterina Yu. Bezsudnova
Format: Article
Language:English
Published: MDPI AG 2021-08-01
Series:Molecules
Subjects:
D-amino acid transaminase
enzyme catalysis
substrate specificity
X-ray analysis
arginine residues
sequence-structure-function relationships
Online Access:https://www.mdpi.com/1420-3049/26/16/5053

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