Literature summary for 3.5.1.1 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.

Search for more literature for 3.5.1.1

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pyrococcus furiosus

Protein Variants

Protein Variants	Comment	Organism
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
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]

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

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus furiosus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Pyrococcus furiosus

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms	Comment	Organism
L-asparaginase	-	Pyrococcus furiosus

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Release 2023.1 (January 2023)