Literature summary for 3.4.15.6 extracted from

Ponndorf, D.; Broer, I.; Nausch, H.
Expression of CphB- and CphE-type cyanophycinases in cyanophycin-producing tobacco and comparison of their ability to degrade cyanophycin in plant and plant extracts (2017), Transgenic Res., 26, 491-499 .

Search for more literature for 3.4.15.6

Protein Variants

Protein Variants	Comment	Organism
additional information	coexpression of cyanophycin and CGPase in the same plant without substrate degradation in planta by transient expression of CGPase CphB either in the plastid or cytosol, or the Pseudomonas alcaligenes CGPase CphE in the cytosol of CGP-producing Nicotiana tabacum plants. No cyanophycin degradation appears prior to cell homogenization independent of the CGPase produced. In crude plant extracts, only cytosolic CphE leads to a fast degradation of cyanophycin. CphE also shows higher stability and in vitro activity compared to both CphB variants	Pseudomonas alcaligenes
additional information	coexpression of cyanophycin and CGPase in the same plant without substrate degradation in planta by transient expression of CGPase CphB either in the plastid or cytosol, or the Pseudomonas alcaligenes CGPase CphE in the cytosol of CGP-producing Nicotiana tabacum plants. No cyanophycin degradation appears prior to cell homogenization independent of the CGPase produced. In crude plant extracts, only cytosolic CphE leads to a fast degradation of cyanophycin. CphE also shows higher stability and in vitro activity compared to both CphB variants	Thermosynechococcus vestitus

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas alcaligenes	G8HR04	-	-
Thermosynechococcus vestitus	P0C8P3	-	-

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Release 2023.1 (January 2023)