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Literature summary for 2.6.1.1 extracted from

  • Zou, L.; Zhao, H.; Wang, D.; Wang, M.; Zhang, C.; Xiao, F.
    Expression and purification of a functional recombinant aspartate aminotransferase (AST) from Escherichia coli (2014), J. Microbiol. Biotechnol., 24, 998-1003.
    View publication on PubMed

Application

Application Comment Organism
synthesis codon-optimized expression in Escherichia coli with His6-tag and purification. The enzyme activity of purified aspartate aminotransferase reaches 150000 U/l. The preparation shows high stability during long-term storage at -20ยบC Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Homo sapiens 5739
-

Organism

Organism UniProt Comment Textmining
Homo sapiens P00505
-
-

Storage Stability

Storage Stability Organism
-20ยฐC, 50% glycerol, 64 weeks, less than 3% loss of activity Homo sapiens