Literature summary for 2.6.1.72 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.

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Application

Application	Comment	Organism
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	Pseudomonas stutzeri

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas stutzeri	Q6VY99	-	-
Pseudomonas stutzeri ST-201	Q6VY99	-	-

Synonyms

Synonyms	Comment	Organism
dpgA	-	Pseudomonas stutzeri
PhgAT	-	Pseudomonas stutzeri

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Release 2023.1 (January 2023)