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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

(glutamat—amonijak-ligaza) adenililtransferaza
Identifikatori
EC broj2.7.7.42
CAS broj9077-66-1
Baze podataka
IntEnzIntEnz pregled
BRENDABRENDA pristup
ExPASyNiceZyme pregled
KEGGKEGG pristup
MetaCycmetabolički put
PRIAMprofil
Strukture PBPRCSB PDB PDBe PDBsum
ATP + [L-glutamat:amonijak ligaza (formira ADP)] difosfat + adenilil-[L-glutamat:amonijak ligaza (formira ADP)]

ReferenceУреди

  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. & 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. 

LiteraturaУреди

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