# positions[].organizations[].parent[].label
College of Agriculture and Life Sciences

# overview
Evolution is the organizing principle of biology and provides the cornerstone of our approach to understand the relationships between protein structure and function. We combine bioinformatics, biochemistry, and genetics to address fundamental questions about protein evolution, such as: What structural and mechanistic features of enzymes increase their capacity to evolve new functions? How do new metabolic pathways evolve? Are there multiple evolutionary pathways to evolve new enzyme activities?

Our primary focus is on how catalytic promiscuity serves as the raw material for evolving new enzyme activities. Catalytic promiscuity is the ability to catalyze different chemical reactions using the same active site. Many enzymes in one branch of the protein family we are studying are catalytically promiscuous, and this activity has been incorporated into new metabolic pathways more than once. Comparing the sequences and structures of these proteins will identify characteristics that permitted them to evolve the second activity.

Our goal is to use results from our research to identify fundamental evolutionary principles that can can help decipher protein structure-function relationships, predict protein functions, and improve protein engineering methods.

# keywords[]
2.2 Factors Relating To The Physical Environment

# keywords[]
1.1 Normal Biological Development And Functioning

# educationAndTraining[].organization.label
Massachusetts Institute of Technology - (Cambridge, Massachusetts, United States)

# educationAndTraining[].organization.label
University of Wyoming - (Laramie, Wyoming, United States)

# awardsAndHonors[].label
Faculty Early Career Development (CAREER) Program

# publications[].label
Loss of quaternary structure is associated with rapid sequence divergence in the OSBS family

# publications[].publisher
Proceedings of the National Academy of Sciences

# publications[].label
Roles of the second-shell amino acid R266 in other members of the MLE subgroup of the enolase superfamily

# publications[].label
RNA-Catalyzed RNA Polymerization: Accurate and General RNA-Templated Primer Extension

# publications[].publisher
American Association for the Advancement of Science (AAAS)

# publications[].label
Role of an Active Site Loop in the Promiscuous Activities of Amycolatopsis sp. T‑1-60 NSAR/OSBS

# publications[].label
Second-Shell Amino Acid R266 Helps Determine N-Succinylamino Acid Racemase Reaction Specificity in Promiscuous N-Succinylamino Acid Racemase/o-Succinylbenzoate Synthase Enzymes.

# publications[].publisher
American Association for the Advancement of Science (AAAS)

# publications[].label
Ligand based clustering of alpha-beta barrel enzymes

# publications[].label
Mechanisms of protein evolution and their application to protein engineering

# publications[].publisher
American Association for the Advancement of Science (AAAS)

# publications[].label
Discovery of a dipeptide epimerase enzymatic function guided by homology modeling and virtual screening.

# publications[].label
Mechanisms of protein evolution and their application to protein engineering.

# publications[].label
Evolution of Enzymatic Activities in the Enolase Superfamily: d-Mannonate Dehydratase from Novosphingobium aromaticivorans † , ‡

# publications[].label
Evolution of Enzymatic Activities in the Enolase Superfamily: Stereochemically Distinct Mechanisms in Two Families of cis,cis-Muconate Lactonizing Enzymes

# publications[].label
How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation

# publications[].label
Divergent Evolution of Ligand Binding in the o‑Succinylbenzoate Synthase Family

# publications[].label
Oxidative opening of the aromatic ring: Tracing the natural history of a large superfamily of dioxygenase domains and their relatives.

# publications[].label
Residues required for activity in Escherichia coli o-succinylbenzoate synthase (OSBS) are not conserved in all OSBS enzymes.

# publications[].label
Promiscuity of Exiguobacterium sp. AT1b o-succinylbenzoate synthase illustrates evolutionary transitions in the OSBS family.

# publications[].label
Evolution of Enzymatic Activities in the Enolase Superfamily: l-Rhamnonate Dehydratase

# publications[].label
Prediction and assignment of function for a divergent N-succinyl amino acid racemase.

# publications[].label
Evolution of structure and function in the o-succinylbenzoate synthase family

# publications[].label
Target selection and annotation for the structural genomics of the amidohydrolase and enolase superfamilies.

# publications[].label
Evolution of structure and function in the o-succinylbenzoate synthase/N-acylamino acid racemase family of the enolase superfamily.

# publications[].label
Recognition of Nucleoside Triphosphates during RNA-Catalyzed Primer Extension †

# publications[].label
Metal Ion Requirements for Structure and Catalysis of an RNA Ligase Ribozyme †

# publications[].label
Evolution of Enzymatic Activities in the Enolase Superfamily: Stereochemically Distinct Mechanisms in Two Families of cis,cis-Muconate Lactonizing Enzymes (vol 48, pg 1445, 2009)

# publications[].label
MicroRNAs Regulate Brain Morphogenesis in Zebrafish

# publications[].publisher
American Association for the Advancement of Science (AAAS)

# publications[].label
Comparison of Alicyclobacillus acidocaldarius o-Succinylbenzoate Synthase to Its Promiscuous N-Succinylamino Acid Racemase/ o-Succinylbenzoate Synthase Relatives.

# publications[].label
Evolutionary Exploitation of Promiscuous NSAR/OSBS Enzymes

# researcherOn[].label
CAREER: Evolutionary Mechanisms for Recruiting Promiscuous Enzyme Activities into New Metabolic Pathways

# researcherOn[].awardedBy.label
National Science Foundation - (Arlington, Virginia, United States)

# researcherOn[].label
Biophysical Constraints on Evolution of Enzyme Specificity

# researcherOn[].awardedBy.label
National Institutes of Health - (Bethesda, Maryland, United States)

# researcherOn[].awardedBy.preferredLabel
DHHS-NIH-National Institute of General Medical Science

# streetAddress
Texas A&M University; Biochemistry & Biophysics; 2128 TAMU

# schools[]
College of Agriculture and Life Sciences

# etdChairOf[].label
Wang, Chenxi 1986- (2012-12). Variability of Specificity Determinants in the O- Succinylbenzoate Synthase Family. Master's Thesis.