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Literature summary 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

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.7.89 2-oxoglutarate activation Escherichia coli
2.7.7.89 adenosine activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli
2.7.7.89 GTP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli
2.7.7.89 ITP activation by nucleotides, most efficient in presence of two different nucleotides Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.89 diphosphate
-
Escherichia coli
2.7.7.89 glutamate
-
Escherichia coli
2.7.7.89 glutamine
-
Escherichia coli
2.7.7.89 SO42-
-
Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.7.89 0.004
-
Adenylyl-[L-glutamate:ammonia ligase (ADP-forming)] calculated as adenylyl groups removed from substrate Escherichia coli

Metals/Ions

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.89 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

EC Number Organism UniProt Comment Textmining
2.7.7.89 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.89
-
Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.7.89 0.015
-
-
Escherichia coli

Storage Stability

EC Number Storage Stability Organism
2.7.7.89 4°C, 2 weeks Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.89 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
2.7.7.89 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.7.89 7.3
-
-
Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.7.89 6.5 8 80% of maximal activity at pH 6.5, 50% of maximal activity at pH 8.0 Escherichia coli

Cofactor

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