Cyanophycin synthase (L-arginine-adding)

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Cyanophycin synthase (L-arginine-adding)
Identifiers
EC no. 6.3.2.30
CAS no. 131554-17-1
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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 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.

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<span class="mw-page-title-main">Cyanophycin</span>

Cyanophycin, also known as CGP or multi-L-arginyl-poly, is a non-protein, non-ribosomally produced amino acid polymer composed of an aspartic acid backbone and arginine side groups.

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CPHA or CPhA may refer to:

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(ADP-ribosyl)hydrolase 1, also termed [Protein ADP-ribosylarginine] hydrolase and protein-Nω-(ADP-D-ribosyl)-L-arginine ADP-ribosylhydrolase (EC 3.2.2.19), is an enzyme that in humans is encoded by the ADPRH gene. This enzyme is a specific mono(ADP-ribosyl)hydrolase that catalyses the removal of an ADP-ribosyl modification from target arginine residues of protein substrates. The chemical reactions can formally be described as follows:

<span class="mw-page-title-main">Cyanophycinase</span> Class of enzymes

Cyanophycinase (EC 3.4.15.6, cyanophycin degrading enzyme, beta-Asp-Arg hydrolysing enzyme, CGPase, CphB, CphE, cyanophycin granule polypeptidase, extracellular CGPase) is an enzyme. It catalyses the following chemical reaction

Cyanophycin synthase (L-aspartate-adding) is an enzyme with systematic name cyanophycin:L-aspartate ligase (ADP-forming). This enzyme catalyses the following chemical reaction

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.