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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

EC Number: 5.3.1.5

a D-xylopyranose <=> D-xylulose

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, 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
a 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 SRI International Pathway Tools version 19.0 on Tue Apr 21, 2015, biocyc14.