Adenylyl-(glutamate-ammonia ligase) hydrolase

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In enzymology, an adenylyl-[glutamate---ammonia ligase] hydrolase (EC 3.1.4.15) is an enzyme that catalyzes the chemical reaction

adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H₂O $\rightleftharpoons$ adenylate + [L-glutamate:ammonia ligase (ADP-forming)]

Thus, the two substrates of this enzyme are [[adenylyl-[L-glutamate:ammonia ligase (ADP-forming)]]] and H₂O, whereas its two products are adenylate and [[[L-glutamate:ammonia ligase (ADP-forming)]]].

This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] adenylylhydrolase. Other names in common use include adenylyl-[glutamine-synthetase]hydrolase, and adenylyl(glutamine synthetase) hydrolase.

[edit] References

IUBMB entry for 3.1.4.15
BRENDA references for 3.1.4.15 (Recommended.)
PubMed references for 3.1.4.15
PubMed Central references for 3.1.4.15
Google Scholar references for 3.1.4.15
Heilmeyer L, Battig F and Holzer H (1968). "Characterization of a glutamine synthetase b activating (deadenylylating) enzyme system in Escherichia coli". Eur. J. Biochem. 9: 259–262. doi:10.1111/j.1432-1033.1969.tb00603.x.
Shapiro BM (1969). "The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements". Biochemistry. 8: 659–70. doi:10.1021/bi00830a030. PMID 4893578.
Shapiro BM, Stadtman ER (1968). "5'-adenylyl-O-tyrosine. The novel phosphodiester residue of adenylylated glutamine synthetase from Escherichia coli". J. Biol. Chem. 243: 3769–71. PMID 4298074.