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Literature summary extracted from

  • Garg, D.K.; Tomar, R.; Dhoke, R.R.; Srivastava, A.; Kundu, B.
    Domains of Pyrococcus furiosus L-asparaginase fold sequentially and assemble through strong intersubunit associative forces (2015), Extremophiles, 19, 681-691.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.5.1.1 expression in Escherichia coli Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
3.5.1.1 W301F mutation has no effect on secondary and tertiary structure of the protein. Initiation of unfolding transition of the W301F protein happens at a higher GdnCl concentration compared to W60F, indicated that the N-domain is more stable compared to the C-domain Pyrococcus furiosus
3.5.1.1 W60F mutation has no effect on secondary and tertiary structure of the protein. Initiation of unfolding transition of the W301F protein happens at a higher GdnCl concentration compared to W60F, indicated that the N-domain is more stable compared to the C-domain Pyrococcus furiosus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.5.1.1 36500
-
 1 * 36500, SDS-PAGE, MALDI mass spectrometry Pyrococcus furiosus

Organism

EC Number Organism UniProt Comment Textmining
3.5.1.1 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.5.1.1
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.1 L-asparagine + H2O
-
 Pyrococcus furiosus L-aspartate + NH3
-
 ?

Subunits

EC Number Subunits Comment Organism
3.5.1.1 monomer 1 * 36500, SDS-PAGE, MALDI mass spectrometry Pyrococcus furiosus

Synonyms

EC Number Synonyms Comment Organism
3.5.1.1 L-asparaginase
-
 Pyrococcus furiosus