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MetaCyc Enzyme: D-xylose isomerase

Species: Bifidobacterium adolescentis

Subunit composition of D-xylose isomerase = [D-xylose isomerase subunit]3

Summary:
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]

Unification Links: Protein Model Portal:Q7M0V2, UniProt:Q7M0V2

Relationship Links: InterPro:IN-FAMILY:IPR013022

Gene-Reaction Schematic

Gene-Reaction Schematic

Credits:
Created 07-Mar-2007 by Caspi R, SRI International


Enzymatic reaction of: D-xylose isomerase

Inferred from experiment

EC Number: 5.3.1.5

D-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]

Primary Physiological Regulators of Enzyme Activity: Mg2+, Mn2+

Kinetic Parameters:
Substrate Km (μM) Citations
D-xylopyranose 4000.0 [Kawai94]

pH(opt): 7 [Kawai94]


References

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by Pathway Tools version 19.5 (software by SRI International) on Thu Feb 11, 2016, biocyc12.