(Glutamat—amonijak-ligaza) adenililtransferaza

(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
Pretraga
PMC	articles
PubMed	articles
NCBI Protein	search

(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)]

\rightleftharpoons

difosfat + adenilil-[L-glutamat:amonijak ligaza (formira ADP)]

Reference

↑ 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

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.

Spoljašnje veze

MeSH (glutamate---ammonia-ligase)+adenylyltransferase

[1] 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.

[2] 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.

[3] 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.

[4] 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.

[5] 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.

[6] 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.

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p r u Proteini: enzimi
Teme	Aktivno mesto • Alosterna regulacija • Mesto vezivanja • Katalitički perfektan enzim • Koenzim • Kofaktor • Kooperativnost • EC broj • Enzimska kataliza • Inhibicija enzima • Enzimska kinetika • Lajnviver–Burk dijagram • Mihaelis–Mentenova kinetika • Spisak enzima
Tipovi	EC1 Oksidoreduktaze/spisak • EC2 Transferaze/spisak • EC3 Hidrolaze/spisak • EC4 Lijaze/spisak • EC5 Izomeraze/spisak • EC6 Ligaze/spisak
B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6