Cyanophycinase

Cyanophycinase
Cyanophycinase
Identifiers
Organism	Synechocystis sp. PCC 6803
Symbol	cphB
PDB	3EN0
UniProt	P73832
Structures
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Structures	Swiss-model
Domains	InterPro

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Cyanophycinase
Cyanophycinase
Identifiers
EC no.	3.4.15.6
CAS no.	131554-16-0
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

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

\rightleftharpoons

[L-Asp(4-L-Arg)]_n-1 + L-Asp(4-L-Arg)

The enzyme is highly specific for the branched polypeptide cyanophycin. It is similar to Dipeptidase E, another S51 family serine protease.

References

^ Obst M, Krug A, Luftmann H, Steinbüchel A (July 2005). "Degradation of cyanophycin by Sedimentibacter hongkongensis strain KI and Citrobacter amalonaticus strain G Isolated from an anaerobic bacterial consortium". Applied and Environmental Microbiology. 71 (7): 3642–52. doi:10.1128/aem.71.7.3642-3652.2005. PMC 1169039. PMID 16000772.
^ Obst M, Oppermann-Sanio FB, Luftmann H, Steinbüchel A (July 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 cyanophycinhydrolyzing enzyme". The Journal of Biological Chemistry. 277 (28): 25096–105. doi:10.1074/jbc.m112267200. PMID 11986309.
^ Richter R, Hejazi M, Kraft R, Ziegler K, Lockau W (July 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". European Journal of Biochemistry. 263 (1): 163–9. doi:10.1046/j.1432-1327.1999.00479.x. PMID 10429200.

External links

Cyanophycinase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Obst M, Krug A, Luftmann H, Steinbüchel A (July 2005). "Degradation of cyanophycin by Sedimentibacter hongkongensis strain KI and Citrobacter amalonaticus strain G Isolated from an anaerobic bacterial consortium". Applied and Environmental Microbiology. 71 (7): 3642–52. doi:10.1128/aem.71.7.3642-3652.2005. PMC 1169039. PMID 16000772.

[2] Obst M, Oppermann-Sanio FB, Luftmann H, Steinbüchel A (July 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 cyanophycinhydrolyzing enzyme". The Journal of Biological Chemistry. 277 (28): 25096–105. doi:10.1074/jbc.m112267200. PMID 11986309.

[3] Richter R, Hejazi M, Kraft R, Ziegler K, Lockau W (July 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". European Journal of Biochemistry. 263 (1): 163–9. doi:10.1046/j.1432-1327.1999.00479.x. PMID 10429200.

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[2]

[3]

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)