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Literature summary for 2.7.7.89 extracted from

  • Shapiro, B.M.
    The glutamine synthetase deadenylylating enzyme system from Escherichia coli. Resolution into two components, specific nucleotide stimulation, and cofactor requirements (1969), Biochemistry, 8, 659-670.
    View publication on PubMed
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Activating Compound

Activating Compound Comment Organism Structure
2-oxoglutarate activation Escherichia coli
adenosine activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli
GTP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli
ITP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
diphosphate
-
 Escherichia coli
glutamate
-
 Escherichia coli
glutamine
-
 Escherichia coli
SO42-
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.004
-
 Adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] calculated as adenylyl groups removed from substrate Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
arsenate activation Escherichia coli
Mg2+ activation Escherichia coli
Mn2+ activation Escherichia coli
additional information not activated by Ca2+, Cd2+, Zn2+, Ba2+ Escherichia coli
phosphate activation Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O Escherichia coli activation of adenylated glutamine synthetase, EC 6.3.1.2, which is less active in catalyzing glutamine biosynthesis ?
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.015
-
-
 Escherichia coli

Storage Stability

Storage Stability Organism
4°C, 2 weeks Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O
-
 Escherichia coli adenylate + [L-glutamate:ammonia ligase (ADP-forming)] the primary product may be ADP which is then degraded to AMP ir
adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] + H2O activation of adenylated glutamine synthetase, EC 6.3.1.2, which is less active in catalyzing glutamine biosynthesis Escherichia coli ?
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.3
-
-
 Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8 80% of maximal activity at pH 6.5, 50% of maximal activity at pH 8.0 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ADP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli
AMP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli
ATP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli
CTP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli
UTP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli