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Literature summary extracted from

  • Javid, H.; Jomrit, J.; Chantarasiri, A.; Isarangkul, D.; Meevootisom, V.; Wiyakrutta, S.
    Effects of halophilic peptide fusion on solubility, stability, and catalytic performance of D-phenylglycine aminotransferase (2014), J. Microbiol. Biotechnol., 24, 597-604.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.6.1.72 synthesis N-terminus of PhgAT is genetically fused with short peptides from a ferredoxin enzyme of halophilic archaeon, Halobacterium salinarum. The fused enzymes display a reduced pI and increase in solubility in TEMP (pH 7.6) storage, and in CAPSO (pH 9.5) reaction buffers, respectively. All the fused PhgAT display higher enzymatic reaction rates than the wild-type at all concentrations of L-glutamate used. the halophilic fusion significantly increases the tolerance of PhgAT in the presence of NaCl and KCl Stutzerimonas stutzeri

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.72 Stutzerimonas stutzeri Q6VY99
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2.6.1.72 Stutzerimonas stutzeri ST-201 Q6VY99
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Synonyms

EC Number Synonyms Comment Organism
2.6.1.72 dpgA
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 Stutzerimonas stutzeri
2.6.1.72 PhgAT
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 Stutzerimonas stutzeri