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Ronald J. Parry

Professor Emeritus of Chemistry and Biochemistry and Cell Biology

Research in our laboratory is focused upon the biosynthesis of secondary metabolites, otherwise known as natural products. Many of these compounds exhibit a high degree of chemical complexity as well as important biological activity. Examples of such compounds include the important antibiotics erythromycin, penicillin, and vancomycin. The goals of our research are to discover novel biochemical reactions associated with specific biosynthetic pathways and to engineer biosynthetic gene clusters to produce new compounds with desirable biological activity.  Several natural products are currently under intensive study in our laboratories.

parry_figureOne of these compounds is the antitumor antibiotic valanimycin, an azoxy compound produced by Streptomyces viridifaciens. Valanimycin is a member of a growing class of natural products that contain N-N bonds. Although compounds with N-N bonds are widespread, little is known at present about the biochemistry involved in N-N bond formation. A major goal of this project is to discover the nature of the N-N bond forming chemistry. The entire cluster of genes required for valanimycin biosynthesis has now been cloned and sequenced, but the genes encoding the proteins responsible for N-N bond formation have not yet been identified. Two other ongoing projects are concerned with the biosynthesis of the phytotoxin coronatine and the biosynthesis of the antibiotics of the pyrrolomycin complex. Coronatine and the pyrrolomycins possess unusual structural features indicating that novel biochemistry is involved in their biosynthesis.


R. J. Parry, S. Nishino, and J. Spain Naturally-occurring Nitro Compounds.  Nat. Prod. Rep., 28 2011: 152-167

Evan G. Johnson, Stuart B. Krasnoff, Dawn R. Bignell, Wen-Chuan Chung, Tao Tao, Ronald J. Parry, Rosemary Loria, and Donna M. Gibson 4-Nitrotryptophan is a Substrate for the Non-ribosomal Peptide Synthetase TxtB in the Thaxtomin A Biosynthetic Pathway .  Mol. Microbiol., 73 2009: 409-418

Ram P. Garg, Lawrence B. Alemany, Sean Moran, and Ronald J. Parry Identification, Characterization, and Bioconversion of a New Intermediate in Valanimycin Biosynthesis .  J. Am. Chem. Soc., 131 2009: 9608-9609

R. P. Garg, X. L. Qian, L. B. Alemany, S. Moran, R. J. Parry Investigations of Valanimycin Biosynthesis: Elucidation of the Role of Seryl-tRNA.  Proc. Natl. Acad. Sci. U.S.A., 105 2008: 6543-6547

Zhang, X., and Parry, R.J. Cloning and characterization of the pyrrolomycin biosynthetic gene clusters from Actinosporangium vitaminophilum ATCC 31673 and Streptomyces sp. UC 11065.  Antimicrob. Agents Chemother., 51 2007: 946-957

Ram P. Garg, Jose M. Gonzalez, and Ronald J. Parry Biochemical characterization of VlmL, a seryl tRNA synthetase encoded by the valanimycin biosynthetic gene cluster.  J. Biol. Chem., 281 2006: 26785-26791

Heather F. Seidle, Robin D. Couch, and Ronald J. Parry Characterization of a non-specific phosphopanthetheinyl transferase from Pseudomonas syringae pv syringae FF5.  Arch. Biochem. Biophys, 446 2006: 167-174

H. Seidle, V. Rangaswamy, R. Couch, C. L. Bender, and R. J. Parry Characterization of Cfa1, a monofunctional acyl carrier protein involved in the biosynthesis of the phytotoxin coronatine.  J. Bacteriol., 186 2004: 2499-2503

R. Couch, S. E. O'Connor, H. Seidle, C. T. Walsh, and R. J. Parry Characterization of CmaA, an adenylation/thiolation didomain enzyme involved in the biosynthesis of coronatine.  J. Bacteriol., 186 2004: 35-42

M. R. Buddha, T. Tao, R. J. Parry, and B. R. Crane Regioselective nitration of tryptophan by a complex between bacterial nitric-oxide synthase and tryptophanyl-tRNA synthetase.  J. Biol. Chem., 279 2004: 49567-49570

  • B.A. (1964) Occidental College Chemistry (1964)
  • Ph.D. (1968) Brandeis University Organic Chemistry (1968)
  • Department of Biochemistry and Cell Biology
  • Institute of Biosciences and Bioengineering
  • Biosynthesis, Mechanistic Enzymology, Molecular Biology
Email: parry@rice.edu
Phone: (713) 348-2446
Office: George R Brown Hall, E200D