Search Results - "Gerlt, JA"
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DIVERGENT EVOLUTION OF ENZYMATIC FUNCTION: Mechanistically Diverse Superfamilies and Functionally Distinct Suprafamilies
Published in Annual review of biochemistry (01-01-2001)“…The protein sequence and structure databases are now sufficiently representative that strategies nature uses to evolve new catalytic functions can be…”
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Divergent evolution in the enolase superfamily: the interplay of mechanism and specificity
Published in Archives of biochemistry and biophysics (2005)“…The members of the mechanistically diverse enolase superfamily catalyze different overall reactions. Each shares a partial reaction in which an active site…”
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The Low Barrier Hydrogen Bond in Enzymatic Catalysis
Published in The Journal of biological chemistry (02-10-1998)Get full text
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Understanding enzyme superfamilies. Chemistry As the fundamental determinant in the evolution of new catalytic activities
Published in The Journal of biological chemistry (05-12-1997)Get full text
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Evolution of Enzymatic Activities in the Enolase Superfamily: l-Fuconate Dehydratase from Xanthomonas campestris
Published in Biochemistry (Easton) (12-12-2006)“…Many members of the mechanistically diverse enolase superfamily have unknown functions. In this report we use both genome (operon) context and screening of a…”
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Mechanistic Diversity in the RuBisCO Superfamily: The “Enolase” in the Methionine Salvage Pathway in Geobacillus kaustophilus
Published in Biochemistry (Easton) (03-04-2007)“…d-Ribulose 1,5-bisphosphate carboxylase/oxygenase (RuBisCO), the most abundant enzyme, is the paradigm member of the recently recognized mechanistically…”
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The Crotonase Superfamily: Divergently Related Enzymes That Catalyze Different Reactions Involving Acyl Coenzyme A Thioesters
Published in Accounts of chemical research (01-02-2001)“…Synergistic investigations of the reactions catalyzed by several members of an enzyme superfamily provide a more complete understanding of the relationships…”
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Evolution of Structure and Function in the o-Succinylbenzoate Synthase/ N-Acylamino Acid Racemase Family of the Enolase Superfamily
Published in Journal of molecular biology (30-06-2006)“…Understanding how proteins evolve to provide both exquisite specificity and proficient activity is a fundamental problem in biology that has implications for…”
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Utilization of l-Ascorbate by Escherichia coli K-12: Assignments of Functions to Products of the yjf-sga and yia-sgb Operons
Published in Journal of Bacteriology (01-01-2002)“…Article Usage Stats Services JB Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley…”
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Discovering New Enzymes and Metabolic Pathways: Conversion of Succinate to Propionate by Escherichia coli
Published in Biochemistry (Easton) (25-04-2000)“…The Escherichia coli genome encodes seven paralogues of the crotonase (enoyl CoA hydratase) superfamily. Four of these have unknown or uncertain functions;…”
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Evolution of Enzymatic Activities in the Enolase Superfamily: l-Talarate/Galactarate Dehydratase from Salmonella typhimurium LT2
Published in Biochemistry (Easton) (21-08-2007)“…We assigned l-talarate dehydratase (TalrD) and galactarate dehydratase (GalrD) functions to a group of orthologous proteins in the mechanistically diverse…”
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Evolution of Enzymatic Activities in the Enolase Superfamily: N-Succinylamino Acid Racemase and a New Pathway for the Irreversible Conversion of d- to l-Amino Acids
Published in Biochemistry (Easton) (11-04-2006)“…Members of the mechanistically diverse enolase superfamily catalyze reactions that are initiated by abstraction of the α-proton of a carboxylate anion to…”
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The crystal structure of benzoylformate decarboxylase at 1.6 Angstrom resolution: Diversity of catalytic residues in thiamin diphosphate-dependent enzymes
Published in Biochemistry (Easton) (14-07-1998)“…The crystal structure of the thiamin diphosphate (ThDP)-dependent enzyme benzoylformate decarboxylase (BFD), the third enzyme in the mandelate pathway of…”
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Evolution of Enzymatic Activities in the Enolase Superfamily: d-Tartrate Dehydratase from Bradyrhizobium japonicum
Published in Biochemistry (Easton) (12-12-2006)“…We focus on the assignment of function to and elucidation of structure−function relationships for a member of the mechanistically diverse enolase superfamily…”
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The Enolase Superfamily: A General Strategy for Enzyme-Catalyzed Abstraction of the α-Protons of Carboxylic Acids
Published in Biochemistry (Easton) (24-12-1996)“…We have discovered a superfamily of enzymes related by their ability to catalyze the abstraction of the α-proton of a carboxylic acid to form an enolic…”
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Evolution of Enzymatic Activity in the Enolase Superfamily: Functional Studies of the Promiscuous o-Succinylbenzoate Synthase from Amycolatopsis
Published in Biochemistry (Easton) (13-01-2004)“…o-Succinylbenzoate synthase (OSBS) from Amycolatopsis, a member of the enolase superfamily, catalyzes the Mn2+-dependent exergonic dehydration of…”
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Evolution of Enzymatic Activities in the Enolase Superfamily: Functional Assignment of Unknown Proteins in Bacillus subtilis and Escherichia coli as l-Ala-d/l-Glu Epimerases
Published in Biochemistry (Easton) (25-12-2001)“…The members of the mechanistically diverse enolase superfamily catalyze different overall reactions by using a common catalytic strategy and structural…”
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Evolution of Enzymatic Activities in the Orotidine 5‘-Monophosphate Decarboxylase Suprafamily: Enhancing the Promiscuous d-arabino-Hex-3-ulose 6-Phosphate Synthase Reaction Catalyzed by 3-Keto-l-gulonate 6-Phosphate Decarboxylase
Published in Biochemistry (Easton) (15-02-2005)“…3-Keto-l-gulonate 6-phosphate decarboxylase (KGPDC) and d-arabino-hex-3-ulose 6-phosphate synthase (HPS) are members of the orotidine 5‘-monophosphate…”
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3‘- and 5‘-Strand Cleavage Reactions Catalyzed by the Fpg Protein from Escherichia coli Occur via Successive β- and δ-Elimination Mechanisms, Respectively
Published in Biochemistry (Easton) (16-01-1996)“…The Fpg protein from Escherichia coli is a multifunctional protein that excises damaged purine bases from DNA to generate aldehydic abasic sites and then…”
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