Cyanophycin synthase (L-aspartate-adding)
| 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 | ||||||||
| |||||||||
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 system 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 ADP + phosphate + [L-Asp(4-L-Arg)]n-L-Asp
This enzyme requires Mg2+ for activity.
References
- ^ Aboulmagd, E., Oppermann-Sanio, F.B. and Steinbüchel, A. (2000). "Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308". Arch. Microbiol. 174 (5): 297–306. doi:10.1007/s002030000206. PMID 11131019.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Aboulmagd, E., Oppermann-Sanio, F.B. and Steinbüchel, A. (2001). "Purification of Synechocystis sp. strain PCC6308 cyanophycin synthetase and its characterization with respect to substrate and primer specificity". Appl. Environ. Microbiol. 67 (5): 2176–2182. doi:10.1128/AEM.67.5.2176-2182.2001. PMID 11319097.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Allen, M.M., Hutchison, F. and Weathers, P.J. (1980). "Cyanophycin granule polypeptide formation and degradation in the cyanobacterium Aphanocapsa 6308". J. Bacteriol. 141 (2): 687–693. PMID 6767688.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Berg, H., Ziegler, K., Piotukh, K., Baier, K., Lockau, W. and Volkmer-Engert, R. (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". Eur. J. Biochem. 267 (17): 5561–5570. doi:10.1046/j.1432-1327.2000.01622.x. PMID 10951215.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Ziegler, K., Deutzmann, R. and Lockau, W. (2002). "Cyanophycin synthetase-like enzymes of non-cyanobacterial eubacteria: characterization of the polymer produced by a recombinant synthetase of Desulfitobacterium hafniense". Z. Naturforsch. [C]. 57 (5–6): 522–529. PMID 12132696.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Ziegler, K., Diener, A., Herpin, C., Richter, R., Deutzmann, R. and Lockau, W. (1998). "Molecular characterization of cyanophycin synthetase, the enzyme catalyzing the biosynthesis of the cyanobacterial reserve material multi-L-arginyl-poly-L-aspartate (cyanophycin)". Eur. J. Biochem. 254: 154–159. doi:10.1046/j.1432-1327.1998.2540154.x. PMID 9652408.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
External links
- Cyanophycin+synthase+(L-aspartate-adding) at the U.S. National Library of Medicine Medical Subject Headings (MeSH)