2007 - Fellow of the American Association for the Advancement of Science (AAAS)
1981 - Fellow of Alfred P. Sloan Foundation
His main research concerns Stereochemistry, Biochemistry, Enzyme, Mandelate racemase and Enolase superfamily. His Stereochemistry research includes themes of Cleavage, Catalysis, Active site, Isomerase and Phosphodiester bond. His work deals with themes such as Genetics, Function, Operon and Protein superfamily, which intersect with Enzyme.
His Mandelate racemase study combines topics from a wide range of disciplines, such as Racemization and Homology. His study in Enolase superfamily is interdisciplinary in nature, drawing from both Divergent evolution, Lysine racemase and Enzyme kinetics. His Divergent evolution study incorporates themes from Protein sequencing and Computational biology.
His primary scientific interests are in Stereochemistry, Crystal structure, Biochemistry, Binding protein and Enzyme. His Stereochemistry research incorporates elements of Orotidine, Catalysis, Active site, Substrate and Mandelate racemase. His Active site research is multidisciplinary, incorporating elements of Protein structure and Lyase.
His Crystal structure research is multidisciplinary, incorporating perspectives in Glutathione S-transferase, Glutathione and Glutathione transferase. All of his Biochemistry and Enolase superfamily, Escherichia coli, Pseudomonas putida, Isomerase and ATP synthase investigations are sub-components of the entire Biochemistry study. He interconnects Mutant and Function in the investigation of issues within Enzyme.
John A. Gerlt spends much of his time researching Crystal structure, Stereochemistry, Biochemistry, Binding protein and Periplasmic space. His biological study spans a wide range of topics, including Glutathione S-transferase, Glutathione, Glutathione transferase and Molecular biology. His work in Stereochemistry addresses issues such as Substrate, which are connected to fields such as Orotidine.
In general Biochemistry study, his work on Enzyme and Enolase superfamily often relates to the realm of Mycobacterium smegmatis, thereby connecting several areas of interest. Within one scientific family, John A. Gerlt focuses on topics pertaining to Transporter under Binding protein, and may sometimes address concerns connected to Carbohydrate. His research on Periplasmic space frequently links to adjacent areas such as Glucuronate.
John A. Gerlt mostly deals with Crystal structure, Stereochemistry, Biochemistry, Binding protein and Enzyme. In his work, Protein subunit is strongly intertwined with Glutathione, which is a subfield of Crystal structure. His Stereochemistry research is multidisciplinary, relying on both Orotidine, Active site, Phosphate, Substrate and ATP synthase.
His Biochemistry study frequently intersects with other fields, such as Metabolomics. His research in Enzyme focuses on subjects like Genome, which are connected to Protein family. The various areas that John A. Gerlt examines in his Enolase superfamily study include Homology, Sugar acids, Dehydratase and Mandelate racemase.
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The Low Barrier Hydrogen Bond in Enzymatic Catalysis
W. Wallace Cleland;Perry A. Frey;John A. Gerlt.
Journal of Biological Chemistry (1998)
Divergent Evolution of Enzymatic Function: Mechanistically Diverse Superfamilies and Functionally Distinct Suprafamilies
John A. Gerlt;Patricia C. Babbitt.
Annual Review of Biochemistry (2001)
Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks.
John A. Gerlt;Jason T. Bouvier;Daniel B. Davidson;Heidi J. Imker.
Biochimica et Biophysica Acta (2015)
Understanding the rates of certain enzyme-catalyzed reactions: Proton abstraction from carbon acids, acyl transfer reactions, and displacement reactions of phosphodiesters
John A. Gerlt;Paul G. Gassman.
The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids†
Patricia C. Babbitt;Miriam S. Hasson;Miriam S. Hasson;Joseph E. Wedekind;Joseph E. Wedekind;David R.J. Palmer.
An explanation for rapid enzyme-catalyzed proton abstraction from carbon acids: importance of late transition states in concerted mechanisms
John Alan Gerlt;Paul G. Gassman.
Journal of the American Chemical Society (1993)
Understanding Enzyme Superfamilies CHEMISTRY AS THE FUNDAMENTAL DETERMINANT IN THE EVOLUTION OF NEW CATALYTIC ACTIVITIES
Patricia C. Babbitt;John A. Gerlt.
Journal of Biological Chemistry (1997)
Understanding enzymic catalysis: the importance of short, strong hydrogen bonds.
John A. Gerlt;Maurice M. Kreevoy;W.W. Cleland;Perry A. Frey.
Chemistry & Biology (1997)
Evolution of enzyme superfamilies
Margaret E Glasner;John A Gerlt;Patricia C Babbitt.
Current Opinion in Chemical Biology (2006)
Discovering new enzymes and metabolic pathways: conversion of succinate to propionate by Escherichia coli.
Toomas Haller;Thomas Buckel;János Rétey;John A. Gerlt.
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