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Literature summary for 6.3.1.1 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)

Crystallization (Comment) Organism
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

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Escherichia coli

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer crystallization Escherichia coli

Synonyms

Synonyms Comment Organism
ammonia-dependent asparagine synthetase
-
Escherichia coli
AsnA
-
Escherichia coli