Crystal structure of an aspartate aminotransferase Lpg0070 from Legionella pneumophila.
Biochem Biophys Res Commun
; 689: 149230, 2023 12 31.
Article
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| MEDLINE
| ID: mdl-37984176
ABSTRACT
Legionella pneumophila aspartate aminotransferase (Lpg0070) is a member of the transaminase and belongs to the pyridoxal 5'-phosphate (PLP)-dependent superfamily. It is responsible for the transfer of α-amino between aspartate and α-ketoglutarate to form glutamate and oxaloacetate. Here, we report the crystal structure of Lpg0070 at the resolution of 2.14 Å and 1.7 Å, in apo-form and PLP-bound, respectively. Our structural analysis revealed the specific residues involved in the PLP binding and free form against PLP-bound supported conformational changes before substrate recognition. In vitro enzyme activity proves that the absence of the N-terminal arm reduces the enzyme activity of Lpg0070. These data provide further evidence to support the N-terminal arm plays a crucial role in catalytic activity.
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Base de dados:
MEDLINE
Assunto principal:
Legionella pneumophila
Idioma:
En
Ano de publicação:
2023
Tipo de documento:
Article