Cyanophycin synthase (L-aspartate-adding)

Cyanophycin synthase (L-aspartate-adding) (EC 6.3.2.29, CphA, CphA1, CphA2, cyanophycin synthetase, multi-L-arginyl-poly-L-aspartate synthase) is an enzyme with systematic name cyanophycin:L-aspartate ligase (ADP-forming).^{[1][2][3][4][5][6]} This enzyme catalyses the following chemical reaction

ATP + [L-Asp(4-L-Arg)]n + L-Asp ${\displaystyle \rightleftharpoons }$ ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp

Cyanophycin synthase (L-aspartate-adding)
Identifiers
EC no.	6.3.2.29
CAS no.	131554-17-1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

Cyanophycin synthase (L-aspartate-adding)
Identifiers
Organism	Synechocystis sp. PCC 6803
Symbol	cphA
UniProt	P73833
Search for Structures Swiss-model Domains InterPro

This enzyme requires Mg²⁺ for activity. All enzymes known to have this activity also catalyze the addition of arginine, i.e. cyanophycin synthase (L-arginine-adding) activity. It is structurally similar to Muramyl ligases.

References

1. Aboulmagd E, Oppermann-Sanio FB, Steinbüchel A (November 2000). "Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308". Archives of Microbiology. 174 (5): 297–306. doi:10.1007/s002030000206. PMID 11131019.
2. Aboulmagd E, Oppermann-Sanio FB, Steinbüchel A (May 2001). "Purification of Synechocystis sp. strain PCC6308 cyanophycin synthetase and its characterization with respect to substrate and primer specificity". Applied and Environmental Microbiology. 67 (5): 2176–82. doi:10.1128/AEM.67.5.2176-2182.2001. PMC 92852. PMID 11319097.
3. Allen MM, Hutchison F, Weathers PJ (February 1980). "Cyanophycin granule polypeptide formation and degradation in the cyanobacterium Aphanocapsa 6308". Journal of Bacteriology. 141 (2): 687–93. PMC 293676. PMID 6767688.
4. Berg H, Ziegler K, Piotukh K, Baier K, Lockau W, Volkmer-Engert R (September 2000). "Biosynthesis of the cyanobacterial reserve polymer multi-L-arginyl-poly-L-aspartic acid (cyanophycin): mechanism of the cyanophycin synthetase reaction studied with synthetic primers". European Journal of Biochemistry. 267 (17): 5561–70. doi:10.1046/j.1432-1327.2000.01622.x. PMID 10951215.
5. Ziegler K, Deutzmann R, Lockau W (2002). "Cyanophycin synthetase-like enzymes of non-cyanobacterial eubacteria: characterization of the polymer produced by a recombinant synthetase of Desulfitobacterium hafniense". Zeitschrift für Naturforschung C. 57 (5–6): 522–9. doi:10.1515/znc-2002-5-621. PMID 12132696.
6. Ziegler K, Diener A, Herpin C, Richter R, Deutzmann R, Lockau W (May 1998). "Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin)". European Journal of Biochemistry. 254 (1): 154–9. doi:10.1046/j.1432-1327.1998.2540154.x. PMID 9652408.

External links

• Cyanophycin+synthase+(L-aspartate-adding) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)