2003 - Fellow of the American Academy of Arts and Sciences
2003 - Fellow of the American Association for the Advancement of Science (AAAS)
1998 - Member of the National Academy of Sciences
Perry A. Frey mostly deals with Stereochemistry, Biochemistry, Active site, Lysine 2,3-aminomutase and Lysine. His Stereochemistry research is multidisciplinary, incorporating elements of Biotin synthase, Bond cleavage, Radical SAM, Enzyme and Adenosylcobalamin. His work carried out in the field of Enzyme brings together such families of science as Decarboxylation and Carboxylation.
His research in Active site intersects with topics in Binding site, Isomerase, Leloir pathway, NAD+ kinase and Histidine. His Lysine 2,3-aminomutase research is multidisciplinary, incorporating perspectives in Cleavage, Photochemistry, Electron paramagnetic resonance, Substrate and Aldimine. His Lysine research incorporates themes from Dithionite and Methionine.
Perry A. Frey focuses on Stereochemistry, Biochemistry, Active site, Enzyme and Lysine 2,3-aminomutase. His research integrates issues of Lysine, Adenosylcobalamin, Cofactor, Substrate and NAD+ kinase in his study of Stereochemistry. His Active site study combines topics in areas such as Hydrolysis, Enzyme kinetics, Binding site and Pyrophosphate.
As part of one scientific family, Perry A. Frey deals mainly with the area of Enzyme, narrowing it down to issues related to the Covalent bond, and often Crystallography and Low-barrier hydrogen bond. His Lysine 2,3-aminomutase course of study focuses on Electron paramagnetic resonance and Steady state. His study looks at the relationship between Organic chemistry and topics such as Medicinal chemistry, which overlap with Inorganic chemistry, Hydrogen bond, Nuclear magnetic resonance spectroscopy and Chymotrypsin.
Perry A. Frey spends much of his time researching Stereochemistry, Biochemistry, Enzyme, Lysine and Lysine 2,3-aminomutase. His Stereochemistry study integrates concerns from other disciplines, such as Adenosylcobalamin, Cofactor, Active site, Radical and Radical SAM. His study in Adenosylcobalamin is interdisciplinary in nature, drawing from both Cleavage, Bond cleavage, Mutase, Photochemistry and Substrate.
His work in the fields of Enzyme, such as Enzyme catalysis, overlaps with other areas such as FHIT. He combines subjects such as Medicinal chemistry, Equilibrium constant, Intramolecular Transferases and Stereoisomerism with his study of Lysine. His Lysine 2,3-aminomutase research focuses on subjects like Amino acid, which are linked to Conserved sequence, A value and Methylamine.
Perry A. Frey mainly investigates Stereochemistry, Biochemistry, Lysine 2,3-aminomutase, Radical SAM and Lysine. Perry A. Frey has included themes like Crystallography, Adenosylcobalamin, Cofactor, Active site and Radical substitution in his Stereochemistry study. His work on Enzyme and Phosphate as part of general Biochemistry study is frequently connected to Alkyltransferase, therefore bridging the gap between diverse disciplines of science and establishing a new relationship between them.
He interconnects Photochemistry, Radical and Bond cleavage in the investigation of issues within Lysine 2,3-aminomutase. His study explores the link between Radical SAM and topics such as Cysteine that cross with problems in Molybdopterin. Perry A. Frey has researched Lysine in several fields, including Intramolecular Transferases and Methionine.
A low-barrier hydrogen bond in the catalytic triad of serine proteases
Perry A. Frey;Sean A. Whitt;John B. Tobin.
The Leloir pathway: a mechanistic imperative for three enzymes to change the stereochemical configuration of a single carbon in galactose
Perry A. Frey.
The FASEB Journal (1996)
The Radical SAM Superfamily
Perry A. Frey;Adrian D. Hegeman;Frank J. Ruzicka.
Critical Reviews in Biochemistry and Molecular Biology (2008)
Enzymatic reaction mechanisms
Perry A. Frey;Adrian D. Hegeman.
S-Adenosylmethionine: a wolf in sheep's clothing, or a rich man's adenosylcobalamin?
Perry A. Frey;Olafur Th. Magnusson.
Chemical Reviews (2003)
Radical mechanisms of enzymatic catalysis.
Perry A. Frey.
Annual Review of Biochemistry (2001)
A NEW CONCEPT FOR THE MECHANISM OF ACTION OF CHYMOTRYPSIN : THE ROLE OF THE LOW-BARRIER HYDROGEN BOND
Constance S. Cassidy;Jing Lin;Perry A. Frey.
S-adenosylmethionine as an oxidant : the radical SAM superfamily
Susan C. Wang;Perry A. Frey.
Trends in Biochemical Sciences (2007)
The ubiquity of iron.
Perry A. Frey;George H. Reed.
ACS Chemical Biology (2012)
The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale
Bryan W. Lepore;Frank J. Ruzicka;Perry A. Frey;Dagmar Ringe.
Proceedings of the National Academy of Sciences of the United States of America (2005)
If you think any of the details on this page are incorrect, let us know.