Species: Bifidobacterium adolescentis
Subunit composition of D-xylose isomerase = [D-xylose isomerase subunit]3
D-xylose isomerase was isolated from Bifidobacterium adolescentis and purified to homogeneity. The enzyme appears to be a homotrimer, and required bivalent cations for activity, with Mn2+ providing the highest activity. The N-terminal of the protein was sequenced, and the partial sequence obtained was not similar to similar enzymes from other organisms, such as the Escherichia coli K-12 xylose isomerase [Kawai94].
Molecular Weight of Polypeptide: 53 kD (experimental) [Kawai94]
Molecular Weight of Multimer: 168 kD (experimental) [Kawai94]
pI: 4.3 [Kawai94]
Relationship Links: InterPro:IN-FAMILY:IPR013022
Enzymatic reaction of: D-xylose isomerase
EC Number: 188.8.131.52D-xylopyranose ⇄ D-xylulose
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
This reaction is reversible.Activators (Allosteric): Mg2+ [Kawai94], Co2+ [Kawai94], Mn2+ [Kawai94]
pH(opt): 7 [Kawai94]
Kawai94: Kawai Y, Konishi H, Horitsu H, Sakurai H, Takamizawa K, Suzuki T, Kawai K (1994). "Purification and characterization of D-xylose isomerase from Bifidobacterium adolescentis." Biosci Biotechnol Biochem 58(4);691-4. PMID: 7764860
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493