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Literature summary extracted from

  • Nakatsu, T.; Kato, H.; Oda, J.
    Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase (1998), Nat. Struct. Biol., 5, 15-19.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.3.1.1 crystal structure of native AsnA and complexed with L-asparagine and AMP at 2.5 A, 2.2 A and 2.2 A resolution, respectively Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
6.3.1.1 C315A no change in activity, necessary to improve crystallization Escherichia coli
6.3.1.1 C51A no change in activity, necessary to improve crystallization Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.3.1.1 Mg2+
-
 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.3.1.1 ATP + L-aspartate + NH3 Escherichia coli
-
 AMP + diphosphate + L-asparagine
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
6.3.1.1
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.3.1.1 ATP + L-aspartate + NH3
-
 Escherichia coli AMP + diphosphate + L-asparagine
-
 ?

Subunits

EC Number Subunits Comment Organism
6.3.1.1 dimer crystallization Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
6.3.1.1 ammonia-dependent asparagine synthetase
-
 Escherichia coli
6.3.1.1 AsnA
-
 Escherichia coli