Literature summary for 5.1.1.10 extracted from

Pozo-Dengra, J.; Martinez-Rodriguez, S.; Contreras, L.M.; Prieto, J.; Andujar-Sanchez, M.; Clemente-Jimenez, J.M.; Las Heras-Vazquez, F.J.; Rodriguez-Vico, F.; Neira, J.L.
Structure and conformational stability of a tetrameric thermostable N-succinylamino acid racemase (2009), Biopolymers, 91, 757-772.

Search for more literature for 5.1.1.10

Cloned(Commentary)

Cloned (Comment)	Organism
expressed as a His-taged fusion protein	Geobacillus kaustophilus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Co2+	enzyme requires a divalent cation for activity. Maximal enzymatic activity with Co2+	Geobacillus kaustophilus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
42300	-	molecular weight of monomeric subunit, SDS-PAGE	Geobacillus kaustophilus
170000	-	tetramer, analytical ultracentrifugation	Geobacillus kaustophilus
177300	-	tetramer, gel filtration	Geobacillus kaustophilus

Organism

Organism	UniProt	Comment	Textmining
Geobacillus kaustophilus	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
His-tag is removed by thrombin cleavage	Geobacillus kaustophilus

Subunits

Subunits	Comment	Organism
tetramer	gel filtration and analytical ultracentrifugation. Tetrameric structure in the absence or presence of Co2+, 4 * 42300 Da	Geobacillus kaustophilus

Synonyms

Synonyms	Comment	Organism
GkNSAAR	-	Geobacillus kaustophilus
N-succinylamino acid racemase	-	Geobacillus kaustophilus

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)