Literature summary extracted from

Zecchinon, L.; Oriol, A.; Netzel, U.; Svennberg, J.; Gerardin-Otthiers, N.; Feller, G.
Stability domains, substrate-induced conformational changes and hinge-bending motions in a psychrophilic phosphoglycerate kinase: A microcalorimetric study (2005), J. Biol. Chem., 280, 41307-41314.

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.2.3	Pseudomonas sp.	-	TACII18	-
2.7.2.3	Pseudomonas sp. TACII18	-	TACII18	-

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
2.7.2.3	additional information	-	the psychrophilic enzyme enzyme exhibits two distinct stability domains in the free, open conformation. These stability domains do not match the structural N- and C-domains as the heat-stable domain corresponds to about 80 residues of the C-domain, including the nucleotide binding site, whereas the remaining of the protein contributes to the main heat-labile domain	Pseudomonas sp.

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)