KEGG   ENZYME: 2.7.7.89Help
Entry
EC 2.7.7.89                 Enzyme                                 

Name
[glutamate---ammonia ligase]-adenylyl-L-tyrosine phosphorylase;
adenylyl-[glutamine---synthetase]-deadenylase
Class
Transferases;
Transferring phosphorus-containing groups;
Nucleotidyltransferases
BRITE hierarchy
Sysname
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine:phosphate adenylyltransferase
Reaction(IUBMB)
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine + phosphate = [L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine + ADP [RN:R03474]
Reaction(KEGG)
Substrate
[L-glutamate:ammonia ligase (ADP-forming)]-O4-(5'-adenylyl)-L-tyrosine [CPD:C01299];
phosphate [CPD:C00009]
Product
[L-glutamate:ammonia ligase (ADP-forming)]-L-tyrosine [CPD:C01281];
ADP [CPD:C00008]
Comment
This activity is carried out by a bacterial bifunctional enzyme that also adenylates glutamate---ammonia ligase (EC 2.7.7.42, [glutamate---ammonia-ligase] adenylyltransferase) [3,5]. The two activities are present on separate domains.
History
EC 2.7.7.89 created 1972 as EC 3.1.4.15, transferred 2015 to EC 2.7.7.89
Reference
1  [PMID:4920873]
  Authors
Anderson WB, Stadtman ER
  Title
Glutamine synthetase deadenylation: a phosphorolytic reaction yielding ADP as nucleotide product.
  Journal
Biochem. Biophys. Res. Commun. 41 (1970) 704-9.
Reference
2  [PMID:4934180]
  Authors
Anderson WB, Stadtman ER
  Title
Purification and functional roles of the P I and P II components of Escherichia coli glutamine synthetase deadenylylation system.
  Journal
Arch. Biochem. Biophys. 143 (1971) 428-43.
Reference
3  [PMID:9312015]
  Authors
Jaggi R, van Heeswijk WC, Westerhoff HV, Ollis DL, Vasudevan SG
  Title
The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction.
  Journal
EMBO. J. 16 (1997) 5562-71.
  Sequence
[eco:b3053]
Reference
4  [PMID:14766310]
  Authors
Xu Y, Wen D, Clancy P, Carr PD, Ollis DL, Vasudevan SG
  Title
Expression, purification, crystallization, and preliminary X-ray analysis of the  N-terminal domain of Escherichia coli adenylyl transferase.
  Journal
Protein. Expr. Purif. 34 (2004) 142-6.
  Sequence
[eco:b3053]
Reference
5  [PMID:15130478]
  Authors
Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL
  Title
Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase.
  Journal
Structure. 12 (2004) 861-9.
  Sequence
[eco:b3053]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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