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Cited by 25

The DOI matches its Crossref record; 11 of the 11 references it cites were found in a registry or an index.

Evolution of Enzymatic Activities in the Enolase Superfamily: Identification of the General Acid Catalyst in theActive Site of d-Glucarate Dehydratase from Escherichia coli,

Gulick, Andrew M., Hubbard, Brian K., Gerlt, John A., Rayment, Ivan·2001·Biochemistry
DOI 10.1021/bi010733b
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Abstract

D-Glucarate dehydratase from Escherichia coli (GlucD), a member of the enolase superfamily, catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (KDG). Previous mutagenesis and structural studies identified Lys 207 and the His 339-Asp 313 dyad as the general basic catalysts that abstract the C5 proton from L-idarate and D-glucarate, respectively, thereby initiating the reaction by formation of a stabilized enediolate anion intermediate [Gulick, A. M., Hubbard, B. K., Gerlt, J. A., and Rayment, I. (2000) Biochemistry 39, 4590-4602]. The vinylogous elimination of the 4-OH group from this intermediate presumably requires a general acid catalyst. The structure of GlucD with KDG and 4-deoxy-D-glucarate bound in the active site revealed that only His 339 and Asn 341 are proximal to the presumed position of the 4-OH leaving group. The N341D and N341L mutants of GlucD were constructed and subjected to both mechanistic and structural analyses. The N341L but not N341D mutant catalyzed the dehydrofluorination of 4-deoxy-4-fluoro-D-glucarate, demonstrating that in this mutant the initial proton abstraction from C5 can be decoupled from elimination of the leaving group from C4. The kinetic properties and structures of these mutants suggest that either Asn 341 participates in catalysis as the general acid that facilitates the departure of the 4-leaving group or is essential for proper positioning of His 339. In the latter scenario, His 339 would fu…

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Citations

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Research works printed but not linked: 19

  1. Babbitt P. C., 1996, Biochemistry 35, 16489−501
  2. Gerlt J. A., 1998, Curr. Opin. Chem. Biol. 2, 607−12
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  8. Hasson M. S., 1998, Proc. Natl. Acad. Sci. U.S.A. 95, 10396−401
  9. Gulick A. M., 1998, Biochemistry 37, 14358−68
  10. Thompson T. B., 2000, Biochemistry 39, 10662−76
  11. Gulick A. M., 2000, Biochemistry 39, 4590−602
  12. Landro J. A., 1994, Biochemistry 33, 635−43
  13. Larsen T. M., 1996, Biochemistry 35, 4349−58
  14. Palmer D. R., 1998, Biochemistry 37, 14350−7
  15. Withers S. G., 1986, Carbohydr. Res. 154, 127−44
  16. Otwinowski Z., 1997, Methods Enzymol. 276
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  18. Imperiali B., 1997, Acc. Chem. Res. 30, 452−59
  19. Abbreviations, d-galactonate dehydratase

Cited by

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Metadata

Authors
Gulick, A. M., Hubbard, B. K., Gerlt, J. A., & Rayment, I.
Affiliations
Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706, and Departments of Biochemistry and Chemistry, University of Illinois, Urbana, Illinois 61801
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2001-08-01
Volume
40
Issue
34
Pages
10054-10062
ISSN
  • 0006-2960
  • 1520-4995
DOI
10.1021/bi010733b
Cited by
25
References
11
Language
en

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CoChat. (2026). Citation check: Evolution of Enzymatic Activities in the Enolase Superfamily: Identification of the General Acid Catalyst in theActive Site of d-Glucarate Dehydratase from Escherichia coli,. https://app.cochat.ai/papers/10.1021/bi010733b
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Gulick, A. M., Hubbard, B. K., Gerlt, J. A., & Rayment, I. (2001). Evolution of Enzymatic Activities in the Enolase Superfamily: Identification of the General Acid Catalyst in theActive Site of d-Glucarate Dehydratase from Escherichia coli,. Biochemistry. https://doi.org/10.1021/bi010733b

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