3.4.15.6: cyanophycinase
This is an abbreviated version!
For detailed information about cyanophycinase, go to the full flat file.
Word Map on EC 3.4.15.6
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3.4.15.6
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dipeptides
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cyanobacteria
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synechocystis
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anabaena
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cpha
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alcaligenes
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diazotrophic
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serine-type
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gxsxg
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eubacteria
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arginine-agarose
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asp-arg
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water-insoluble
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heterocyst-forming
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nitrogen-rich
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non-cyanobacterial
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heterocysts
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polyamide
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l-aspartic
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nutrition
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food industry
- 3.4.15.6
- dipeptides
- cyanobacteria
- synechocystis
- anabaena
- cpha
- alcaligenes
-
diazotrophic
-
serine-type
-
gxsxg
- eubacteria
-
arginine-agarose
- asp-arg
-
water-insoluble
-
heterocyst-forming
-
nitrogen-rich
-
non-cyanobacterial
- heterocysts
- polyamide
-
l-aspartic
- nutrition
- food industry
Reaction
Synonyms
CGPase, CphB, CphB1, CphB2, CphB3, CphB5, CphB6, CphE, CphEal, CphI, CphJ, cyanophycin granule polypeptidase, cyanophycinase, extracellular CGPase
ECTree
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Engineering
Engineering on EC 3.4.15.6 - cyanophycinase
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N100A
site-directed mutagenesis, 40% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
N158A
site-directed mutagenesis, 41% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
N172A
site-directed mutagenesis, 0.02% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
N17A
site-directed mutagenesis, 60% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
N202A
site-directed mutagenesis, 8% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
Q101A
site-directed mutagenesis, 0.02% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
Q173A
site-directed mutagenesis, 0.5% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
R178A
site-directed mutagenesis, 1% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
R180A
site-directed mutagenesis, 0.01% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
R183a
site-directed mutagenesis, 0.01% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
S132A
site-directed mutagenesis, 0.002% activity of the wild-type, measured with 75 microg/ml of [L-Asp(4-Arg)]n in phosphate buffer at pH 8.3 and 30°C
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
additional information
Gly101, Asp172, Gly173, Arg178, Arg180 and Arg183 form a conserved pocket adjacent to the catalytic Ser132, these are functionally critical residues. The cyanophycinase active site contains three absolutely conserved Arg residues (Arg178, Arg180 and Arg183), which line up along one side of the pocket
additional information
Thermosynechococcus vestitus
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
additional information
Thermosynechococcus vestitus
optimized transient expression in Nicotiana benthamiana plants to produce high amounts of active CGPase. Protein stability is increased by the translational fusion of CGPase to the green fluorescent protein or to the transit peptide of the small subunit of RuBisCO for peptide production in the chloroplasts