Enzymes with extra talents: moonlighting functions and catalytic promiscuity
SD Copley - Current opinion in chemical biology, 2003 - Elsevier
Recent studies of moonlighting functions and catalytic promiscuity provide insights into the
structural and mechanistic bases of these phenomena. Moonlighting proteins that are …
structural and mechanistic bases of these phenomena. Moonlighting proteins that are …
Evolution of function in (β/α) 8-barrel enzymes
JA Gerlt, FM Raushel - Current opinion in chemical biology, 2003 - Elsevier
The (β/α) 8-barrel is the most common fold in structurally characterized enzymes. Whether
the functionally diverse enzymes that share this fold are the products of either divergent or …
the functionally diverse enzymes that share this fold are the products of either divergent or …
Evolutionary Potential of (β/α)8-Barrels: Functional Promiscuity Produced by Single Substitutions in the Enolase Superfamily
DMZ Schmidt, EC Mundorff, M Dojka, E Bermudez… - Biochemistry, 2003 - ACS Publications
The members of the mechanistically diverse,(β/α) 8-barrel fold-containing enolase
superfamily evolved from a common progenitor but catalyze different reactions using a …
superfamily evolved from a common progenitor but catalyze different reactions using a …
Enzymatic racemisation and its application to synthetic biotransformations
B Schnell, K Faber, W Kroutil - Advanced Synthesis & Catalysis, 2003 - Wiley Online Library
In contrast to kinetic resolution, where only 50% of the racemic starting material can be
converted into the desired product and where the remaining 'wrong'enantiomer has to be …
converted into the desired product and where the remaining 'wrong'enantiomer has to be …
Crystal structure of Mycobacterium tuberculosis MenB, a key enzyme in vitamin K2 biosynthesis
JJ Truglio, K Theis, Y Feng, R Gajda, C Machutta… - Journal of Biological …, 2003 - ASBMB
Bacterial enzymes of the menaquinone (Vitamin K 2) pathway are potential drug targets
because they lack human homologs. MenB, 1, 4-dihydroxy-2-naphthoyl-CoA synthase, the …
because they lack human homologs. MenB, 1, 4-dihydroxy-2-naphthoyl-CoA synthase, the …
Reactions of trans-3-Chloroacrylic Acid Dehalogenase with Acetylene Substrates: Consequences of and Evidence for a Hydration Reaction
SC Wang, MD Person, WH Johnson, CP Whitman - Biochemistry, 2003 - ACS Publications
Various soil bacteria use 1, 3-dichloropropene, a component of the commercially available
fumigants Shell DD and Telone II, as a sole source of carbon and energy. One enzyme …
fumigants Shell DD and Telone II, as a sole source of carbon and energy. One enzyme …
Definitions of enzyme function for the structural genomics era
PC Babbitt - Current opinion in chemical biology, 2003 - Elsevier
Questions are being asked about how enzyme function is described at the molecular level
and the strengths and weaknesses of the EC system for this purpose. A new approach to …
and the strengths and weaknesses of the EC system for this purpose. A new approach to …
The 4-Oxalocrotonate Tautomerase- and YwhB-Catalyzed Hydration of 3E-Haloacrylates: Implications for the Evolution of New Enzymatic Activities
SC Wang, WH Johnson… - Journal of the American …, 2003 - ACS Publications
4-Oxalocrotonate tautomerase (4-OT) catalyzes the conversion of 2-oxo-4 E-hexenedioate
to 2-oxo-3 E-hexenedioate through the intermediate, 2-hydroxy-2, 4 E-hexadienedioate. 4 …
to 2-oxo-3 E-hexenedioate through the intermediate, 2-hydroxy-2, 4 E-hexadienedioate. 4 …
Evolution of enzymatic activity in the enolase superfamily: structural and mutagenic studies of the mechanism of the reaction catalyzed by o-succinylbenzoate …
VA Klenchin, EA Taylor Ringia, JA Gerlt, I Rayment - Biochemistry, 2003 - ACS Publications
o-Succinylbenzoate synthase (OSBS) from Escherichia coli, a member of the enolase
superfamily, catalyzes an exergonic dehydration reaction in the menaquinone biosynthetic …
superfamily, catalyzes an exergonic dehydration reaction in the menaquinone biosynthetic …
Steady-State Kinetics and Molecular Evolution of Escherichia coli MenD [(1R,6R)-2-Succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate Synthase], an Anomalous …
M Bhasin, JL Billinsky, DRJ Palmer - Biochemistry, 2003 - ACS Publications
(1 R, 6 R)-2-Succinyl-6-hydroxy-2, 4-cyclohexadiene-1-carboxylate (SHCHC) synthase, or
MenD, catalyzes the thiamin diphosphate-(ThDP-) dependent decarboxylation of 2 …
MenD, catalyzes the thiamin diphosphate-(ThDP-) dependent decarboxylation of 2 …