Cijanoficinska sintaza (dodavanje L-aspartata)
Izgled
Cijanoficinska sintaza (dodavanje L-aspartata) | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifikatori | |||||||||
EC broj | 6.3.2.29 | ||||||||
CAS broj | 131554-17-1 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
|
Cijanoficinska sintaza (dodavanje L-aspartata) (EC 6.3.2.29, CphA, CphA1, CphA2, cijanoficinska sintetaza, multi-L-arginil-poli-L-aspartatna sintaza) je enzim sa sistematskim imenom cijanoficin:L-aspartat ligaza (formira ADP).[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
Za dejstvo ovog enzima je neophodan jon Mg2+.
- ↑ Aboulmagd, E., Oppermann-Sanio, F.B. and Steinbüchel, A. (2000). „Molecular characterization of the cyanophycin synthetase from Synechocystis sp. strain PCC6308”. Arch. Microbiol. 174: 297-306. PMID 11131019.
- ↑ 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: 2176-2182. PMID 11319097.
- ↑ Allen, M.M., Hutchison, F. and Weathers, P.J. (1980). „Cyanophycin granule polypeptide formation and degradation in the cyanobacterium Aphanocapsa 6308”. J. Bacteriol. 141: 687-693. PMID 6767688.
- ↑ 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: 5561-5570. PMID 10951215.
- ↑ 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: 522-529. PMID 12132696.
- ↑ 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. PMID 9652408.
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.