Biology:Cyanophycin synthase (L-arginine-adding)
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Short description: Class of enzymes
| Cyanophycin synthase (L-arginine-adding) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.3.2.30 | ||||||||
| CAS number | 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 | ||||||||
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Cyanophycin synthase (L-arginine-adding) (EC 6.3.2.30, CphA, CphA1, CphA2, cyanophycin synthetase, multi-L-arginyl-poly-L-aspartate synthase) is an enzyme with systematic name cyanophycin:L-arginine 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 + L-Arg [math]\displaystyle{ \rightleftharpoons }[/math] ADP + phosphate + [L-Asp(4-L-Arg)]n + 1
This enzyme requires Mg2+ for activity. This enzyme requires Mg2+ for activity. All enzymes known to have this activity also catalyze the addition of aspartate, i.e. cyanophycin synthase (L-aspartate-adding) activity. It is structurally similar to Muramyl ligases.
References
- ↑ "Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308". Archives of Microbiology 174 (5): 297–306. November 2000. doi:10.1007/s002030000206. PMID 11131019.
- ↑ "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. May 2001. doi:10.1128/AEM.67.5.2176-2182.2001. PMID 11319097.
- ↑ "Cyanophycin granule polypeptide formation and degradation in the cyanobacterium Aphanocapsa 6308". Journal of Bacteriology 141 (2): 687–93. February 1980. PMID 6767688.
- ↑ "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. September 2000. doi:10.1046/j.1432-1327.2000.01622.x. PMID 10951215.
- ↑ "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. 2002. doi:10.1515/znc-2002-5-621. PMID 12132696.
- ↑ "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. May 1998. doi:10.1046/j.1432-1327.1998.2540154.x. PMID 9652408.
External links
- Cyanophycin+synthase+(L-arginine-adding) at the US National Library of Medicine Medical Subject Headings (MeSH)
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