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. 1990 Feb 1;265(3):699–705. doi: 10.1042/bj2650699

Localization of the essential histidine and carboxylate group in D-xylose isomerases.

W Vangrysperre 1, J Van Damme 1, J Vandekerckhove 1, C K De Bruyne 1, R Cornelis 1, H Kersters-Hilderson 1
PMCID: PMC1133690  PMID: 2306209

Abstract

D-Xylose isomerases from different bacterial strains were chemically modified with histidine and carboxylate-specific reagents. The active-site residues were identified by amino acid sequence analysis of peptides recognized by differential peptide mapping on ligand-protected and unprotected derivatized enzyme. Both types of modified residues were found to cluster in a region with consensus sequence: Phe-His-Asp-Xaa-Asp-Xaa-Xaa-Pro-Xaa-Gly, conserved in all D-xylose isomerases studied so far. These results are consistent with the recently published X-ray data of the enzyme active centre from Streptomyces rubiginosus showing hydrogen bond formation between Asp-57 and His-54 which locks the latter in one tautomeric form. A study of the pH-dependence of the kinetic parameters suggests the participation of a histidine group in the substrate-binding but not in the isomerization process. Comparison of the N-terminal amino acid sequences of several D-xylose isomerases further revealed a striking homology among the Actinomycetaceae enzymes and identifies them as a specific class of D-xylose isomerases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Callens M., Tomme P., Kersters-Hilderson H., Cornelis R., Vangrysperre W., De Bruyne C. K. Metal ion binding to D-xylose isomerase from Streptomyces violaceoruber. Biochem J. 1988 Feb 15;250(1):285–290. doi: 10.1042/bj2500285. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Carrell H. L., Glusker J. P., Burger V., Manfre F., Tritsch D., Biellmann J. F. X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4440–4444. doi: 10.1073/pnas.86.12.4440. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Dauter Z., Dauter M., Hemker J., Witzel H., Wilson K. S. Crystallisation and preliminary analysis of glucose isomerase from Streptomyces albus. FEBS Lett. 1989 Apr 10;247(1):1–8. doi: 10.1016/0014-5793(89)81227-x. [DOI] [PubMed] [Google Scholar]
  4. Drocourt D., Bejar S., Calmels T., Reynes J. P., Tiraby G. Nucleotide sequence of the xylose isomerase gene from Streptomyces violaceoniger. Nucleic Acids Res. 1988 Oct 11;16(19):9337–9337. doi: 10.1093/nar/16.19.9337. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Farber G. K., Glasfeld A., Tiraby G., Ringe D., Petsko G. A. Crystallographic studies of the mechanism of xylose isomerase. Biochemistry. 1989 Sep 5;28(18):7289–7297. doi: 10.1021/bi00444a022. [DOI] [PubMed] [Google Scholar]
  6. Hanes C. S. Studies on plant amylases: The effect of starch concentration upon the velocity of hydrolysis by the amylase of germinated barley. Biochem J. 1932;26(5):1406–1421. doi: 10.1042/bj0261406. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Henrick K., Collyer C. A., Blow D. M. Structures of D-xylose isomerase from Arthrobacter strain B3728 containing the inhibitors xylitol and D-sorbitol at 2.5 A and 2.3 A resolution, respectively. J Mol Biol. 1989 Jul 5;208(1):129–157. doi: 10.1016/0022-2836(89)90092-2. [DOI] [PubMed] [Google Scholar]
  8. Rey F., Jenkins J., Janin J., Lasters I., Alard P., Claessens M., Matthyssens G., Wodak S. Structural analysis of the 2.8 A model of Xylose isomerase from Actinoplanes missouriensis. Proteins. 1988;4(3):165–172. doi: 10.1002/prot.340040303. [DOI] [PubMed] [Google Scholar]
  9. Saari G. C., Kumar A. A., Kawasaki G. H., Insley M. Y., O'Hara P. J. Sequence of the Ampullariella sp. strain 3876 gene coding for xylose isomerase. J Bacteriol. 1987 Feb;169(2):612–618. doi: 10.1128/jb.169.2.612-618.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Schellenberg G. D., Sarthy A., Larson A. E., Backer M. P., Crabb J. W., Lidstrom M., Hall B. D., Furlong C. E. Xylose isomerase from Escherichia coli. Characterization of the protein and the structural gene. J Biol Chem. 1984 Jun 10;259(11):6826–6832. [PubMed] [Google Scholar]
  11. Sinha U., Brewer J. M. A spectrophotometric method for quantitation of carboxyl group modification of proteins using Woodward's Reagent K. Anal Biochem. 1985 Dec;151(2):327–333. doi: 10.1016/0003-2697(85)90183-6. [DOI] [PubMed] [Google Scholar]
  12. Sinha U., Brewer J. M. Yeast enolase carboxyl modification using Woodward's reagent K. Biochem Cell Biol. 1986 Oct;64(10):970–975. doi: 10.1139/o86-129. [DOI] [PubMed] [Google Scholar]
  13. Vangrysperre W., Ampe C., Kersters-Hilderson H., Tempst P. Single active-site histidine in D-xylose isomerase from Streptomyces violaceoruber. Identification by chemical derivatization and peptide mapping. Biochem J. 1989 Oct 1;263(1):195–199. doi: 10.1042/bj2630195. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Vangrysperre W., Callens M., Kersters-Hilderson H., De Bruyne C. K. Evidence for an essential histidine residue in D-xylose isomerases. Biochem J. 1988 Feb 15;250(1):153–160. doi: 10.1042/bj2500153. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Vangrysperre W., Kersters-Hilderson H., Callens M., De Bruyne C. K. Reaction of Woodward's reagent K with D-xylose isomerases. Modification of an active site carboxylate residue. Biochem J. 1989 May 15;260(1):163–169. doi: 10.1042/bj2600163. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Wilhelm M., Hollenberg C. P. Nucleotide sequence of the Bacillus subtilis xylose isomerase gene: extensive homology between the Bacillus and Escherichia coli enzyme. Nucleic Acids Res. 1985 Aug 12;13(15):5717–5722. doi: 10.1093/nar/13.15.5717. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Yamanaka K. Purification, crystallization and properties of the D-xylose isomerase from Lactobacillus brevis. Biochim Biophys Acta. 1968 Mar 25;151(3):670–680. doi: 10.1016/0005-2744(68)90015-6. [DOI] [PubMed] [Google Scholar]

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