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314 results on '"Jordan, Douglas B."'

9. B-d-Xylosidase from Selenomonas ruminantium: Catalyzed Reactions with Natural and Artificial Substrates

Author

Jordan, Douglas B., Mulchandani, Ashok, editor, Aizawa, M., editor, Arnold, M. A., editor, Bachas, L., editor, Bachmann, T. T., editor, Belkin, S., editor, Blanch, Harvey W., editor, Cha, H. J., editor, Chuan-Ling, Q., editor, Da Silva, Nancy A., editor, DeLisa, M., editor, Deshusses, M., editor, Dordick, J. S., editor, Eldefrawi, M. E., editor, Gu, M. B., editor, Jain, R. K., editor, Karanth, N. G., editor, Kelly, R., editor, Klibanov, A. M., editor, Krull, U. J., editor, Ladish, M. R., editor, Lee, K., editor, Lee, Y. Y., editor, Ligler, F. S., editor, Linhardt, R., editor, Pandey, A., editor, Pishko, M., editor, Renugopalakrishnan, V., editor, Ryu, D., editor, Seibert, M., editor, Tan, W., editor, Ueda, Mitsuyoshi, editor, Varfolomeyev, S. D., editor, Xu, J. -H., editor, Wang, P., editor, Wyman, C. E., editor, Zhao, H., editor, Chen, Wilfred, editor, Csoregi, Elisabeth, editor, Murhammer, David W., editor, Singh, Anup K., editor, Mulchandaui, Priti, editor, Adney, William S., editor, McMillan, James D., editor, Mielenz, Jonathan, editor, and Klasson, K. Thomas, editor

Published
2008
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18. Riboflavin Biosynthetic Enzymes

Author

Jordan, Douglas B., Bacot, Karen O., Carlson, Thomas J., Picollelli, Michael P., Wawrzak, Zdzislaw, Kessel, Martin, Viitanen, Paul V., and Garab, G., editor

Published
1998
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36. Crystal structure of phenylalanine ammonia lyase: Multiple helix dipoles implicated in catalysis

Author

Calabrese, Joseph C., Jordan, Douglas B., Boodhoo, Amechand, Sairaslani, Sima, and Vannelli, Todd

Subjects
Catalysis -- Methods, Lyases -- Research, Phenylalanine -- Structure, Biological sciences, Chemistry
Abstract

The first three dimensional structure of PAL is determined at 21 angstrom resolution of phenylalanine ammonia lyase (PAL) from Rhodosporidium toruloides. The enzyme is structurally similar to the mechanistically related histidine ammonia lyase (HAL) with PAL having an additional ~ 160 residues extending from the common fold.

Published
2004

37. Structural definition of the active site and catalytic mechanism of 3,4-dihydroxy-2-butanone-4-phosphate synthase

Author

Liao, Der-Ing, Zheng, Ya-Jun, Viitanen, Paul V., and Jordan, Douglas B.

Subjects
Biochemistry -- Research, Phosphates -- Physiological aspects, Enzymes -- Physiological aspects, Ligands -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the L-3,4-dihydroxy-2-butanone-4-phosphate synthase from Magnaporthe grisea. The X-ray crystal structures of this synthase has been examined and the high-resolution structures of the enzyme complexed with ligands are presented.

Published
2002

38. Roles of substrate distortion and intramolecular hydrogen bonding in enzymatic catalysis by scytalone dehydratase

Author

Zheng, Ya-Jun, Basarab, Gregory S., and Jordan, Douglas B.

Subjects
Hydrogen bonding -- Analysis, Catalysis -- Analysis, Enzymes -- Structure-activity relationship, Enzyme kinetics -- Analysis, Biological sciences, Chemistry
Abstract

Site-directed mutagenesis of the active-site residues and substrate substitution studies point out to the importance of hydroxyl group for substrate recognition and catalysis by scytalone dehydratase.

Published
2002

39. A structural account of substrate and inhibitor specificity differences between two naphthol reductases

Author

Liao, Der-Ing, Thompson, Lames E., Fahnestock, Stephen, Valent, Barbara, and Jordan, Douglas B.

Subjects
Biochemistry -- Research, Melanin -- Physiological aspects, Biosynthesis -- Analysis, Fungi -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the short chain dehtydrogenase/reductases that mediate naphthol reduction reactions in the biosynthesis of fungal melanin. Results indicate that the C-terminal residues of the two naphthol reductases are the inhibitor and substrate specificity determinants.

Published
2001

41. Tight binding inhibitors of scytalone dehydratase: effects of site-directed mutations

Author

Jordan, Douglas B., Basarab, Gregory S., Steffens, James J., Schwartz, Rand S., and Doughty, James G.

Subjects
Cytochemistry -- Research, Rice blast disease -- Physiological aspects, Amides -- Physiological aspects, Fungicides -- Physiological aspects, Amino acids -- Physiological aspects, Biological sciences, Chemistry
Abstract

The use of site-directed mutations of scytalone dehydratase (SD), the physiological target of new fungicides and the subject of inhibitor design/optimization, has been looked at as a way to study inhibitor binding interactions. The study complements insights from X-ray structures and structure-activity relationships of the wild-type enzyme for refining views of inhibitor recognition. Structures show that potent inhibitors interact mostly with 11 amino acid side chains and in some cases with one backbone amide. Two of the six hydrogen bonds are not important for inhibitor binding.

Published
2000

42. Stereochemistry of the enolization of scytalone by scytalone dehydratase

Author

Jordan, Douglas B., Zheng, Ya-Jun, Lockett, Bruce A., and Basarab, Gregory S.

Subjects
Enzymes -- Research, Stereochemistry -- Research, Biological sciences, Chemistry
Abstract

The fungal enzyme scytalone dehydratase catalyzes a syn elimination on scytalone by protonating the carbonyl to form an enol. Researches are creating inhibitors of this enzyme to control rice blast.

Published
2000

43. Trihydroxynaphthalene reductase from Magnaporthe grisea: realization of an active center inhibitor and elucidation of the kinetic mechanism

Author

Thompson, James E., Basarab, Gregory S., Andersson, Arnold, Lindqvist, Ylva, and Jordan, Douglas B.

Subjects
Enzymes -- Research, Chemical reaction, Rate of -- Research, Melanin -- Research, Spectrophotometry -- Usage, Biological sciences, Chemistry
Abstract

The kinetic mechanism of trihydroxynaphthalene reductase (3NHR), the enzyme that catalyzes the second reduction pathway in the synthesis of the melanin of the fungus Magnaporthe grisea, was studied using scytalone, U7278 and phenanthrenequinone as substrates. The results revealed that 3NHR follows a preferred ordered sequential mechanism with nucleotide binding first and leaving last. The amino acid sequence analysis of the protein, on the other hand, confirmed its classification under the short-chain dehydrogenase superfamily of enzymes.

Published
1997

46. Oxazolidinones: A New Class of Agricultural Fungicides

Author

Sternberg, Jeffrey A., primary, Geffken, Detlef, additional, Adams, John B., additional, Jordan, Douglas B., additional, Pöstages, Reiner, additional, Sternberg, Charlene G., additional, Campbell, Carlton L., additional, Moberg, William K., additional, and Livingston, Robert S., additional

Published
1998
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