EC 3.4.15.6 - Cyanophycinase

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IntEnz Enzyme Nomenclature
EC 3.4.15.6

Names

Accepted name:
cyanophycinase
Other names:
cyanophycin degrading enzyme
β-Asp-Arg hydrolysing enzyme
CGPase
CphB
CphE
cyanophycin granule polypeptidase
extracellular CGPase
Systematic name:
-

Reaction

Comments:

The enzyme is highly specific for the branched polypeptide cyanophycin and does not hydrolyse poly-L-aspartate or poly-L-arginine [3]. A serine-type exopeptidase that belongs in peptidase family S51.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , DIAGRAM , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
CAS Registry Number: 131554-16-0
UniProtKB/Swiss-Prot:

References

  1. Obst, M., Krug, A., Luftmann, H. and Steinbüchel, A.
    Degradation of cyanophycin by Sedimentibacter hongkongensis strain KI and Citrobacter amalonaticus strain G isolated from an anaerobic bacterial consortium.
    Appl. Environ. Microbiol. 71: 3642-3652 (2005). [PMID: 16000772]
  2. Obst, M., Oppermann-Sanio, F.B., Luftmann, H. and Steinbüchel, A.
    Isolation of cyanophycin-degrading bacteria, cloning and characterization of an extracellular cyanophycinase gene (cphE) from Pseudomonas anguilliseptica strain BI. The cphE gene from P. anguilliseptica BI encodes a cyanophycin-hydrolyzing enzyme.
    J. Biol. Chem. 277: 25096-25105 (2002). [PMID: 11986309]
  3. Richter, R., Hejazi, M., Kraft, R., Ziegler, K. and Lockau, W.
    Cyanophycinase, a peptidase degrading the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartic acid (cyanophycin): molecular cloning of the gene of Synechocystis sp. PCC 6803, expression in Escherichia coli, and biochemical characterization of the purified enzyme.
    Eur. J. Biochem. 263: 163-169 (1999). [PMID: 10429200]

[EC 3.4.15.6 created 2007]