(Glutamat—amonijak-ligaza) adenililtransferaza
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| (glutamat—amonijak-ligaza) adenililtransferaza | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifikatori | |||||||||
| EC broj | 2.7.7.42 | ||||||||
| CAS broj | 9077-66-1 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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(glutamat—amonijak-ligaza) adenililtransferaza (EC 2.7.7.42, glutamin-sintetaza adenililtransferaza, ATP:glutamin sintetaza adenililtransferaza, adenozin trifosfat:glutamin sintetaza adenililtransferaza) je enzim sa sistematskim imenom ATP:(L-glutamat:amonijak ligaza (formira ADP)) adenililtransferaza.[1][2][3][4][5][6] Ovaj enzim katalizuje sledeću hemijsku reakciju
- ATP + [L-glutamat:amonijak ligaza (formira ADP)] difosfat + adenilil-[L-glutamat:amonijak ligaza (formira ADP)]
Reference[uredi | uredi kod]
- ↑ Ebner, E., Wolf, D., Gancedo, C., Elsasser, S. and Holzer, H. (1970). „ATP: glutamine synthetase adenylyltransferase from Escherichia coli B. Purification and properties”. Eur. J. Biochem. 14: 535-544. PMID 4920894.
- ↑ Kingdon, H.S., Shapiro, B.M. and Stadtman, E.R. (1967). „Regulation of glutamine synthetase. 8. ATP: glutamine synthetase adenylyltransferase, an enzyme that catalyzes alterations in the regulatory properties of glutamine synthetase”. Proc. Natl. Acad. Sci. USA 58: 1703-1710. PMID 4867671.
- ↑ Mecke, D., Wulff, K. and Holzer, H. (1966). „Characterization of a glutamine synthetase inactivating enzyme from Escherichia coli”. Biochem. Biophys. Res. Commun. 24: 452-458. PMID 5338440.
- ↑ Mecke, D., Wulff, K. and Holzer, H. (1966). „Metabolit-induzierte Inaktivierung von Glutaminsynthetase aus Escherichia coli im zellfreien System”. Biochim. Biophys. Acta 128: 559-567.
- ↑ Shapiro, B.M. and Stadtman, E.R. (1968). „5′-Adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli”. J. Biol. Chem. 243: 3769-3771. PMID 4298074.
- ↑ Wolf, D., Ebner, E. and Hinze, H. (1972). „Inactivation, stabilization and some properties of ATP: glutamine synthetase adenylyltransferase from Escherichia coli B”. Eur. J. Biochem. 25: 239-244. PMID 4402680.
Literatura[uredi | uredi kod]
- 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.