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

(1990) BIOCHEMICAL JOURNAL. 265(3). p.699-705
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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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Citation

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MLA
Vangrysperre, Werner, et al. “Localization of the Essential Histidine and Carboxylate Group in D-Xylose Isomerases.” BIOCHEMICAL JOURNAL, vol. 265, no. 3, 1990, pp. 699–705.
APA
Vangrysperre, W., Van Damme, J., Vandekerckhove, J., De Bruyne, C. K., Cornelis, R., & Kersters-Hilderson, H. (1990). Localization of the essential histidine and carboxylate group in D-xylose isomerases. BIOCHEMICAL JOURNAL, 265(3), 699–705.
Chicago author-date
Vangrysperre, Werner, Jozef Van Damme, Joël Vandekerckhove, Clément K De Bruyne, Rita Cornelis, and Hilda Kersters-Hilderson. 1990. “Localization of the Essential Histidine and Carboxylate Group in D-Xylose Isomerases.” BIOCHEMICAL JOURNAL 265 (3): 699–705.
Chicago author-date (all authors)
Vangrysperre, Werner, Jozef Van Damme, Joël Vandekerckhove, Clément K De Bruyne, Rita Cornelis, and Hilda Kersters-Hilderson. 1990. “Localization of the Essential Histidine and Carboxylate Group in D-Xylose Isomerases.” BIOCHEMICAL JOURNAL 265 (3): 699–705.
Vancouver
1.
Vangrysperre W, Van Damme J, Vandekerckhove J, De Bruyne CK, Cornelis R, Kersters-Hilderson H. Localization of the essential histidine and carboxylate group in D-xylose isomerases. BIOCHEMICAL JOURNAL. 1990;265(3):699–705.
IEEE
[1]
W. Vangrysperre, J. Van Damme, J. Vandekerckhove, C. K. De Bruyne, R. Cornelis, and H. Kersters-Hilderson, “Localization of the essential histidine and carboxylate group in D-xylose isomerases,” BIOCHEMICAL JOURNAL, vol. 265, no. 3, pp. 699–705, 1990.
@article{8625473,
  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.},
  author       = {Vangrysperre, Werner and Van Damme, Jozef and Vandekerckhove, Joël and De Bruyne, Clément K and Cornelis, Rita and Kersters-Hilderson, Hilda},
  issn         = {0264-6021},
  journal      = {BIOCHEMICAL JOURNAL},
  language     = {eng},
  number       = {3},
  pages        = {699--705},
  title        = {Localization of the essential histidine and carboxylate group in D-xylose isomerases},
  url          = {http://dx.doi.org/10.1042/bj2650699},
  volume       = {265},
  year         = {1990},
}

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