ArticlePloS one2019
Crystal structure of L-aspartate aminotransferase from Schizosaccharomyces pombe.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 9 citations in OpenAlex.
- Novel Bioproduction of 1,6-Hexamethylenediamine from l-Lysine Based on an Artificial One-Carbon Elongation Cycle.ACS omega · 2024Article
- Regulatory mechanisms of dopamine metabolism in a marineSynthetic and systems biotechnology · 2024Article
- Isolation and functional verification of an aspartate aminotransferase gene from Neoporphyra haitanensis.BMC plant biology · 2023Article
- Aspartate Transaminase AST2 Involved in Sporulation and Necrotrophic Pathogenesis in the HemibiotrophsFrontiers in microbiology · 2022Article
- Identification of key genes through the constructed CRISPR-dcas9 to facilitate the efficient production of O-acetylhomoserine inFrontiers in bioengineering and biotechnology · 2022Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
L-aspartate aminotransferase is a pyridoxal 5'-phosphate-dependent transaminase that catalyzes reversible transfer of an α-amino group from aspartate to α-ketoglutarate or from glutamate to oxaloacetate. L-aspartate aminotransferase not only mediates amino acid and carbohydrate metabolism but also regulates the cellular level of amino acids by catalyzing amino acid degradation and biosynthesis. To expand our structural information, we determined the crystal structure of L-aspartate aminotransferase from Schizosaccharomyces pombe at 2.1 Å resolution. A structural comparison between two yeast L-aspartate aminotransferases revealed conserved enzymatic mechanism mediated by the open-closed conformational change. Compared with higher eukaryotic species, L-aspartate aminotransferases showed distinguishable inter-subunit interaction between the N-terminal arm and a large domain of the opposite subunit. Interestingly, structural homology search showed varied conformation of the N-terminal arm among 71 structures of the family. Therefore, we classified pyridoxal 5'-phosphate-dependent enzymes into eight subclasses based on the structural feature of N-terminal arms. In addition, structure and sequence comparisons showed strong relationships among the eight subclasses. Our results may provide insights into structure-based evolutionary aspects of pyridoxal 5'-phosphate-dependent enzymes.
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