Roles of Tyrosine 158 and Lysine 165 in the Catalytic Mechanism of InhA, the Enoyl-ACP Reductase fromMycobacterium tuberculosis

Sapan Parikh; Daniel P. Moynihan; Guoping Xiao; Peter J. Tonge

doi:10.1021/bi990529c

journal article Sep 23, 1999

Roles of Tyrosine 158 and Lysine 165 in the Catalytic Mechanism of InhA, the Enoyl-ACP Reductase fromMycobacterium tuberculosis

Sapan Parikh Daniel P. Moynihan Guoping Xiao Peter J. Tonge

Biochemistry Vol. 38 No. 41 pp. 13623-13634 · American Chemical Society (ACS)

View at Publisher Save 10.1021/bi990529c

Topics

No keywords indexed for this article. Browse by subject →

References

72

[1]

Crystal Structure of the Mycobacterium tuberculosis Enoyl-ACP Reductase, InhA, in Complex with NAD+ and a C16 Fatty Acyl Substrate

Denise A. Rozwarski, Catherine Vilchèze, Michele Sugantino et al.

Journal of Biological Chemistry 1999 10.1074/jbc.274.22.15582

[2]

Banerjee A. (1994)

[3]

Quemard A. (1995)

[4]

Johnsson K. J. Am. Chem. Soc. (1995) 10.1021/ja00122a038

[5]

Basso L. A. J. Am. Chem. Soc. (1996) 10.1021/ja962035y

[6]

Rozwarski D. A. Science (1998) 10.1126/science.279.5347.98

[7]

Basso L. A. J. Infect. Dis. (1998) 10.1086/515362

[8]

Kochi A. Tubercle (1991) 10.1016/0041-3879(91)90017-m

[9]

Bloom B. R. (1992)

[10]

Perlman, D. C., El Sadr, W. M., Heifets, L. B., Nelson, E. T., Matts, J. P., Chirgwin, K., Salomon, N., Telzak, E. E., Klein, O., Kreiswirth, B. N., Musser, J. M., and Hafner, R. (1997)AIDS11, 1473−1478. 10.1097/00002030-199712000-00011

[11]

Snider D. E., Jr. N. Engl. J. Med. (1992)

[12]

Heym B. (1994)

[13]

Baldock C. J. Mol. Biol. (1998) 10.1006/jmbi.1998.2271

[14]

Rafferty J. B. (1995)

[15]

Dessen A. (1995)

[16]

Quemard A. (1995)

[17]

Viola R. E. (1979)

[18]

Orr G. A. (1984)

[19]

Segel, I. H. (1975)Enzyme Kinetics. Behavior and Analysis of Rapid Equilibrium and Steady-State Systems, pp 355−385, Wiley, New York.

[20]

Glasoe P. F. J. Phys. Chem. (1960) 10.1021/j100830a521

[21]

Quinn D. M. (1991)

[22]

Cook P. F. (1981)

[23]

Kuliopulos A. (1989)

[24]

Austin J. C. (1995)

[25]

Menard R. (1995)

[26]

Labo M. J. Gen. Microbiol. (1998)

[27]

Fleischmann R. D. (1995)

[28]

Bergler H. J. Gen. Microbiol. (1992) 10.1099/00221287-138-10-2093

[29]

Turnowsky F. J. Bacteriol. (1989) 10.1128/jb.171.12.6555-6565.1989

[30]

Kater M. M. (1991)

[31]

Labesse G. Biochem. J. (1994) 10.1042/bj3040095

[32]

Baker M. E. Biochem. J. (1995) 10.1042/bj3091029

[33]

Ghosh D. (1994)

[34]

Ghosh D. (1995)

[35]

Thoden J. B. (1997)

[36]

Varughese K. I. (1992)

[37]

Jörnvall H. (1995)

[38]

Nakajin S. Biochem. J. (1998) 10.1042/bj3340553

[39]

Bennett M. J. (1997)

[40]

Koivuranta K. T. Biochem. J. (1994) 10.1042/bj3040787

[41]

Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E. r., Tekaia, F., Badcock, K., Basham, D., Brown, D., Chillingworth, T., Connor, R., Davies, R., Devlin, K., Feltwell, T., Gentles, S., Hamlin, N., Holroyd, S., Hornsby, T., Jagels, K., Barrell, B. G., et al. (1998)Nature393, 537−544. 10.1038/31159

[42]

Labò M. J. Gen. Microbiol. (1998)

[43]

Hoang T. T. (1998)

[44]

Kunst F. (1997)

[45]

Wei T. F. J. Bacteriol. (1993)

[46]

Uhlich G. A. (1997)

[47]

Andersson S. G. (1998)

[48]

The complete genome sequence of the gastric pathogen Helicobacter pylori

Jean-F. Tomb, Owen White, Anthony R. Kerlavage et al.

Nature 10.1038/41483

[49]

de Boer G. J. (1997)

[50]

Stephens R. S. (1998)

Showing 50 of 72 references

Cited By

108

Virtual screening assisted discovery of novel natural products to inhibit the catalytic mechanism of Mycobacterium tuberculosis InhA

Manikandan Jayaraman, Lakshmanan Loganathan · 2021

Journal of Molecular Liquids

Anti-tubercular activity and molecular docking studies of indolizine derivatives targeting mycobacterial InhA enzyme

Katharigatta N. Venugopala, Sandeep Chandrashekharappa · 2021

Journal of Enzyme Inhibition and Me...

InhA, the enoyl-thioester reductase from Mycobacterium tuberculosis forms a covalent adduct during catalysis

Bastian Vögeli, Raoul G. Rosenthal · 2018

Journal of Biological Chemistry

Efficient a Priori Identification of Drug Resistant Mutations Using Dead-End Elimination and MM-PBSA.

Maria Safi, Ryan H. Lilien · 2012

Journal of Chemical Information and...

Metrics

108

Citations

72

References

Details

Published: Sep 23, 1999
Vol/Issue: 38(41)
Pages: 13623-13634

Authors

S

Sapan Parikh

Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, and Graduate Program in Biophysics and Graduate Program in Molecular and Cellular Biochemistry, State University of New York at Stony Brook, Stony Brook, New York 11794

D

Daniel P. Moynihan

Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, and Graduate Program in Biophysics and Graduate Program in Molecular and Cellular Biochemistry, State University of New York at Stony Brook, Stony Brook, New York 11794

G

Guoping Xiao

Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, and Graduate Program in Biophysics and Graduate Program in Molecular and Cellular Biochemistry, State University of New York at Stony Brook, Stony Brook, New York 11794

P

Peter J. Tonge

Department of Chemistry, State University of New York at Stony Brook, Stony Brook, New York 11794-3400, and Graduate Program in Biophysics and Graduate Program in Molecular and Cellular Biochemistry, State University of New York at Stony Brook, Stony Brook, New York 11794

Cite This Article

Sapan Parikh, Daniel P. Moynihan, Guoping Xiao, et al. (1999). Roles of Tyrosine 158 and Lysine 165 in the Catalytic Mechanism of InhA, the Enoyl-ACP Reductase fromMycobacterium tuberculosis. Biochemistry, 38(41), 13623-13634. https://doi.org/10.1021/bi990529c

Roles of Tyrosine 158 and Lysine 165 in the Catalytic Mechanism of InhA, the Enoyl-ACP Reductase fromMycobacterium tuberculosis

You May Also Like