Cyanophycin synthase (L-aspartate-adding)

Cyanophycin synthase (L-aspartate-adding)
Cyanophycin synthase (L-aspartate-adding)
Identifiers
Organism	Synechocystis sp. PCC 6803
Symbol	cphA
Orthologs	OMA: entry
UniProt	P73833
Structures
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Structures	Swiss-model
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Cyanophycin synthase (L-aspartate-adding)
Cyanophycin synthase (L-aspartate-adding)
Identifiers
EC no.	6.3.2.29
CAS no.	131554-17-1
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

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

\rightleftharpoons

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

↑ 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. Bibcode:2000ArMic.174..297A. doi:10.1007/s002030000206. PMID 11131019.
↑ 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. Bibcode:2001ApEnM..67.2176A. doi:10.1128/AEM.67.5.2176-2182.2001. PMC 92852. PMID 11319097.
↑ 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. doi:10.1128/jb.141.2.687-693.1980. PMC 293676. PMID 6767688.
↑ 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.
↑ 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.
↑ 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)

[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. Bibcode:2000ArMic.174..297A. 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. Bibcode:2001ApEnM..67.2176A. 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. doi:10.1128/jb.141.2.687-693.1980. 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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Enzymes: CO CS and CN ligases (EC 6.1-6.3)
6.1: Carbon-Oxygen	Aminoacyl tRNA synthetase Alanine Arginine Asparagine Aspartate Cysteine D-Alanine—poly(phosphoribitol) ligase Glutamate Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine
6.2: Carbon-Sulfur	(2,2,3-trimethyl-5-oxocyclopent-3-enyl)acetyl-CoA synthase 2-furoate—CoA ligase 3-alpha,7-alpha-dihydroxy-5-beta-cholestanate—CoA ligase 3-hydroxybenzoate—CoA ligase 3-hydroxypropionyl-CoA synthase 4-chlorobenzoate—CoA ligase 4-Coumarate-CoA ligase 4-hydroxybenzoate—CoA ligase 6-carboxyhexanoate—CoA ligase Acetate—ACP ligase Acetate—CoA ligase (ADP-forming) Acetoacetate—CoA ligase Acetyl—CoA synthetase Acid—CoA ligase (GDP-forming) Anthranilate—CoA ligase Arachidonate—CoA ligase Benzoate—CoA ligase Biotin—CoA ligase (butirosin acyl-carrier protein)—L-glutamate ligase Butyrate—CoA ligase Cholate—CoA ligase Citrate—CoA ligase (citrate (pro-3S)-lyase) ligase Dicarboxylate—CoA ligase Glutarate—CoA ligase Long-chain-fatty-acid—ACP ligase Long-chain-fatty-acid—CoA ligase Malate—CoA ligase Malonate—CoA ligase o-Succinylbenzoate—CoA ligase Oxalate—CoA ligase Phenylacetate—CoA ligase Phytanate—CoA ligase Propionate—CoA ligase Succinate—CoA ligase (ADP-forming) Succinate—CoA ligase (GDP-forming) Succinyl—CoA synthetase trans-Feruloyl—CoA synthase
6.3: Carbon-Nitrogen	Glutamine synthetase Ubiquitin ligase Cullin Von Hippel–Lindau tumor suppressor UBE3A Mdm2 Anaphase-promoting complex UBR1 Glutathione synthetase CTP synthetase Adenylosuccinate synthase Argininosuccinate synthase Holocarboxylase synthetase GMP synthase Asparagine synthetase Carbamoyl phosphate synthetase I II Glutamate–cysteine ligase

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)