Dhara Shah

Arizona State University - West campus
4701 W. Thunderbird Road
Glendale
Asst Professor
Faculty
WEST Campus
Mailcode
2352
Assistant Professor
Faculty
WEST Campus
Mailcode
2352
Asst Professor
Faculty
WEST Campus
Mailcode
2352
Assistant Professor
Faculty
WEST Campus
Mailcode
2352

Biography

Shah’s research interests are in the field of enzymology, chemical biology amd metabolomics. Her research focuses on enzymes involved in a variety of metabolic pathways found in human microbiome and in various human cancers. She is particularly interested in kinetic and mechanistic studies of the reactions catalyzed by these enzymes. Understanding basics of reaction catalyzed by these enzymes can enable development of tools to engineer a beneficial  microbiome and to combat different types of cancers.

Education

Postdoctoral Fellow. Brown University (2014-2017).

Ph.D. University of Wisconsin-Milwaukee

Google Scholar

Research Interests

My research focuses on enzymes involved in a variety of metabolic pathways found in human microbiome and in various human tumors. A description is below:

1. Human Microbiome: Human microbiome produces many unexplored metabolites. These metabolites can have variety of functions. These include: 1. Metabolites produced by one microbe that can either be beneficial or deterimental to another microbe of human microbiome or to the host. 2. Different microbes that can join forces to make a particular metabolite which can influence host metabolism. 

Metabolites produced by the microbiome are built by enzymes. The enzymes can either arise from one  single continuous metabolic pathway or can come from multiple metabolic pathways. These can be in the form of two or more pathways merging from two different microbes. Understanding the metabolic pathways and enzymatic activities can enable development of tools to engineer a beneficial  microbiome.

2. Cancer Biology: A malignant tumour can enhance its growth in two ways: (i) It can exploit certain inherent metabolites (generally produced by human host) to their advantage. Certain type of cancers are highly dependent on such metabolites. (ii) By modifying the outcome of a particular enzymatic reaction that produces a metabolite. For example, a mutation in an enzyme can change the output of the enzymatic activity and now will produce a completely different metabolite as an end product, which will be utilized prominently by cancer cells to their advantage or this metabolite can have detrimental effect to the human host. Understaning the basic nature of these enzyme catalyzed reactions can help in developing tools to combat different types of cancers.

Publications

  1. Dhara D. Shah, Young-OK You and David E. Cane (2017). Stereospecific Formation of E- and Z-Disubstituted Double Bonds by Dehydratase Domains from Modules 1 and 2 of the Fostriecin Polyketide Synthase. J. Am. Chem. Soc. (JACS) 139,14322-14330.
  2. Book chapter: Dhara D. Shah and Graham R. Moran (2015). 4-Hydroxyphenylpyruvate Dioxygenase and Hydroxymandelate Synthase: 2-Oxo Acid-Dependent Oxygenases of Importance to Agriculture and Medicine. 2-Oxoglutarate-Dependent Oxygenases, RSC metallobiology series vol 3, Schofield C. J. and Hausinger R. P. Eds.438-457.
  3. Brett A. Beaupre, Brenton R. Carmichael, Matthew R. Hoag, Dhara D. Shah and Graham R. Moran (2013) Renalase is an a-NAD(P)H Oxidase/Anomerase. J. Am. Chem. Soc. (JACS) 135,13980-13987. Article featured in JACS spotlights.
  4. Dhara D. Shah, John A. Conrad and Graham R. Moran (2013) Intermediate Partitioning Kinetic Isotope Effects for the NIH shift of 4-Hydroxyphenylpyruvate Dioxygenase and the Hydroxylation Reaction of Hydroxymandelate Synthase Reveal Mechanistic Complexity. Biochemistry 52,6097-6107.
  5. Dhara D. Shah, John A. Conrad, Brian Heinz, June M. Brownlee and Graham R. Moran (2011) Evidence for the Mechanism of Hydroxylation by 4-Hydroxyphenylpyruvate Dioxygenase and Hydroxymandelate Synthase from Intermediate Partitioning in Active Site Variants. Biochemistry 50,7694-7704.

Courses

Spring 2020
Course Number Course Title
BCH 371 Modern Concepts Biochemist
BCH 372 Modern Concepts Biochemist Lab
LSC 499 Individualized Instruction
Fall 2019
Course Number Course Title
BCH 371 Modern Concepts Biochemist
BCH 372 Modern Concepts Biochemist Lab
LSC 499 Individualized Instruction

Industry Positions

Scientist (Immuno-Oncology), Agios Pharmaceuticals (April 2018-August 2019)