Cyanophycinase

[1][2][3] It catalyses the following chemical reaction The enzyme is highly specific for the branched polypeptide cyanophycin.

Site directed mutagenesis experiments confirmed that the enzyme is a serine protease and suggested that Ser 132 is the primary catalytic residue.

Other key residues for specificity include Gln101, Asp172, Gln173, Arg178, Arg180 and Arg183 which form a conserved pocket adjacent to Ser 132.

[5] Cyanophycin is highly resistant to degradation by all conventional proteases, and the only enzyme known to be capable of hydrolyzing it is cyanophycinase.

Cyanophycin is a non-ribosomally synthesized peptidyl polymer that is used for nitrogen storage by cyanobacteria and other select eubacteria.

Biological assembly of cyanophycinase determined from the organism Synechocystis sp. PCC6803
The catalytic triad of Cyanophycinase is Ser 132, His 174, and Glu 201. Other conserved residues which form a pocket around the serine include: Gln101, Asp172, Gln173, Arg178, Arg180 and Arg183