Literature summary for 2.7.4.3 extracted from

Nguyen, P.Q.; Liu, S.; Thompson, J.C.; Silberg, J.J.
Thermostability promotes the cooperative function of split adenylate kinases (2008), Protein Eng. Des. Sel., 21, 303-310.

Search for more literature for 2.7.4.3

Protein Variants

Protein Variants	Comment	Organism
additional information	functional complemetation of temperature-sensitive Escherichia coli mutant by concomitant expression of isolated N-terminus, amino acids 179 and C-terminus, amino acids 80220. Reconstituted enzyme has 17fold lower activity compared with full-length native enzyme	Thermotoga neapolitana
additional information	no functional complemetation of temperature-sensitive Escherichia coli mutant by concomitant expression of isolated N-terminus, amino acids 1-76 and C-terminus, amino acids 77-217. Weak complementation after fusion with polypeptides that strongly associate	Bacillus subtilis
Q16L/Q199R	thermostabilization of full-length protein. Cells harboring the mutant fragment pair with concomitant expression of isolated N-terminus, amino acids 1-76 and C-terminus, amino acids 77-217 show weak complementation of Escherichia coli mutant after fusion with polypeptides that strongly associate	Bacillus subtilis

Organism

Organism	UniProt	Comment	Textmining
Bacillus subtilis	P16304	-	-
Thermotoga neapolitana	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)