Jump to content

Cyanophycinase

From Wikipedia, the free encyclopedia

This is an old revision of this page, as edited by Dcirovic (talk | contribs) at 04:36, 17 May 2016 (→‎top). The present address (URL) is a permanent link to this revision, which may differ significantly from the current revision.

Cyanophycinase
Identifiers
EC no.3.4.15.6
CAS no.131554-16-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Cyanophycinase (EC 3.4.15.6, cyanophycin degrading enzyme, beta-Asp-Arg hydrolysing enzyme, CGPase, CphB, CphE, cyanophycin granule polypeptidase, extracellular CGPase) is an enzyme.[1][2][3] It catalyses the following chemical reaction

[L-Asp(4-L-Arg)]n + H2O [L-Asp(4-L-Arg)]n-1 + L-Asp(4-L-Arg)

The enzyme is highly specific for the branched polypeptide cyanophycin.

References

  1. ^ Obst, M.; Krug, A.; Luftmann, H.; Steinbüchel, A. (2005). "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. doi:10.1128/aem.71.7.3642-3652.2005. PMID 16000772.
  2. ^ Obst, M.; Oppermann-Sanio, F.B.; Luftmann, H.; Steinbüchel, A. (2002). "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. doi:10.1074/jbc.m112267200. PMID 11986309.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  3. ^ Richter, R.; Hejazi, M.; Kraft, R.; Ziegler, K.; Lockau, W. (1999). "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. doi:10.1046/j.1432-1327.1999.00479.x. PMID 10429200.