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Cyanophycin synthase (L-aspartate-adding)

(Redirected from Cyanophycin synthetase)

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

Cyanophycin synthase (L-aspartate-adding)
Identifiers
EC no.6.3.2.29
CAS no.131554-17-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins
Cyanophycin synthase (L-aspartate-adding)
Identifiers
OrganismSynechocystis sp. PCC 6803
SymbolcphA
UniProtP73833
Search for
StructuresSwiss-model
DomainsInterPro
ATP + [L-Asp(4-L-Arg)]n + L-Asp ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp

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

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  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.
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