Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.7.42 extracted from

  • Wohlhueter, R.M.; Ebner, E.; Wolf, D.H.
    Studies on the reaction mechanism of adenosine triphosphate: glutamine synthetase adenylyltransferase from Escherichia coli B. Evidence for an ordered mechanism (1972), J. Biol. Chem., 247, 4213-4218.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1
-
[L-glutamate:ammonia ligase (ADP-forming)] pH 7.5, 22°C Escherichia coli
3.9
-
ATP pH 7.5, 22°C Escherichia coli
3.9
-
ATP ATP in form of MgATP2- Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [L-glutamate:ammonia ligase (ADP-forming)] Escherichia coli inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)] Escherichia coli B / ATCC 11303 inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
r

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
B
-
Escherichia coli B / ATCC 11303
-
B
-

Reaction

Reaction Comment Organism Reaction ID
ATP + [glutamine synthetase]-L-tyrosine = diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [glutamine synthetase]-L-tyrosine
-
Escherichia coli diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
-
?
ATP + [glutamine synthetase]-L-tyrosine
-
Escherichia coli B / ATCC 11303 diphosphate + [glutamine synthetase]-O4-(5'-adenylyl)-L-tyrosine
-
?
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
-
Escherichia coli diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)]
-
Escherichia coli B / ATCC 11303 diphosphate + [L-glutamate:ammonia ligase (ADP-forming)]-(AMP)
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)] inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP Escherichia coli diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
r
ATP + [L-glutamate:ammonia ligase (ADP-forming)] inactivation of [L-glutamate:ammonia ligase (ADP-forming)] by attachment of the adenylyl moiety of ATP Escherichia coli B / ATCC 11303 diphosphate + [L-glutamate:ammonia ligase (ADP-forming)] -(AMP)
-
r
additional information enzyme also catalyzes a phosphate exchange between ATP and diphosphate, which is also stimulated by glutamine Escherichia coli ?
-
?
additional information enzyme also catalyzes a phosphate exchange between ATP and diphosphate, which is also stimulated by glutamine Escherichia coli B / ATCC 11303 ?
-
?

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli