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Mechanism of biotin carboxylase inhibition by ethyl 4-[[2-chloro-5-(phenylcarbamoyl)phenyl]sulphonylamino]benzoate

Journal of enzyme inhibition and medicinal chemistry, 2022-12, Vol.37 (1), p.100-108

2022

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Computational redesign of bacterial biotin carboxylase inhibitors using structure-based virtual screening of combinatorial libraries

Molecules (Basel, Switzerland), 2014-04, Vol.19 (4), p.4021-4045

2014

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Structural evidence for substrate‐induced synergism and half‐sites reactivity in biotin carboxylase

Protein science, 2008-10, Vol.17 (10), p.1706-1718

2008

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The enzymes of biotin dependent CO2 metabolism: What structures reveal about their reaction mechanisms

Protein science, 2012-11, Vol.21 (11), p.1597-1619

2012

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The Structure of the Carboxyltransferase Component of Acetyl-CoA Carboxylase Reveals a Zinc-Binding Motif Unique to the Bacterial Enzyme

Biochemistry (Easton), 2006-02, Vol.45 (6), p.1712-1722

2006

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Smaller Is Better for Antibiotic Discovery

ACS chemical biology, 2009-06, Vol.4 (6), p.397-399

Waldrop, Grover L

2009

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Three-Dimensional Structure of the Biotin Carboxylase Subunit of Acetyl-CoA Carboxylase

Biochemistry (Easton), 1994-08, Vol.33 (34), p.10249-10256

1994

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A tale of two functions: enzymatic activity and translational repression by carboxyltransferase

Nucleic acids research, 2010-03, Vol.38 (4), p.1217-1227

2010

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Behavior of the ATP grasp domain of biotin carboxylase monomers and dimers studied using molecular dynamics simulations

Proteins, structure, function, and bioinformatics, 2011-02, Vol.79 (2), p.622-632

2011

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DNA inhibits catalysis by the carboxyltransferase subunit of acetyl‐CoA carboxylase: Implications for active site communication

Protein science, 2008-01, Vol.17 (1), p.34-42

2008

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The utility of molecular dynamics simulations for understanding site‐directed mutagenesis of glycine residues in biotin carboxylase

Proteins, structure, function, and bioinformatics, 2009-03, Vol.74 (4), p.808-819

2009

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Movement of the Biotin Carboxylase B-domain as a Result of ATP Binding

The Journal of biological chemistry, 2000-05, Vol.275 (21), p.16183-16190

2000

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Function of Escherichia coli Biotin Carboxylase Requires Catalytic Activity of Both Subunits of the Homodimer

The Journal of biological chemistry, 2001-08, Vol.276 (32), p.29864-29870

2001

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Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine

Biochemistry (Easton), 1992-07, Vol.31 (28), p.6585-6591

1992

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Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase

Biochemistry (Easton), 1992-07, Vol.31 (28), p.6562-6569

1992

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The Biotin Domain Peptide from the Biotin Carboxyl Carrier Protein of Escherichia coli Acetyl-CoA Carboxylase Causes a Marked Increase in the Catalytic Efficiency of Biotin Carboxylase and Carboxyltransferase Relative to Free Biotin

The Journal of biological chemistry, 1999-11, Vol.274 (45), p.31767-31769

1999

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A 70‐amino acid zinc‐binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer

Protein science, 1994-06, Vol.3 (6), p.967-974

1994

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Mechanism of biotin carboxylase inhibition by ethyl 4-[[2-chloro-5-(phenylcarbamoyl)phenyl]sulphonylamino]benzoate

Computational redesign of bacterial biotin carboxylase inhibitors using structure-based virtual screening of combinatorial libraries

Structural evidence for substrate‐induced synergism and half‐sites reactivity in biotin carboxylase

The enzymes of biotin dependent CO2 metabolism: What structures reveal about their reaction mechanisms

The Structure of the Carboxyltransferase Component of Acetyl-CoA Carboxylase Reveals a Zinc-Binding Motif Unique to the Bacterial Enzyme

Smaller Is Better for Antibiotic Discovery

Three-Dimensional Structure of the Biotin Carboxylase Subunit of Acetyl-CoA Carboxylase

A tale of two functions: enzymatic activity and translational repression by carboxyltransferase

Behavior of the ATP grasp domain of biotin carboxylase monomers and dimers studied using molecular dynamics simulations

DNA inhibits catalysis by the carboxyltransferase subunit of acetyl‐CoA carboxylase: Implications for active site communication

The utility of molecular dynamics simulations for understanding site‐directed mutagenesis of glycine residues in biotin carboxylase

Movement of the Biotin Carboxylase B-domain as a Result of ATP Binding

Function of Escherichia coli Biotin Carboxylase Requires Catalytic Activity of Both Subunits of the Homodimer

Steady-state kinetics and isotope effects on the mutant catalytic trimer of aspartate transcarbamoylase containing the replacement of histidine 134 by alanine

Ionization of amino acid residues involved in the catalytic mechanism of aspartate transcarbamoylase

The Biotin Domain Peptide from the Biotin Carboxyl Carrier Protein of Escherichia coli Acetyl-CoA Carboxylase Causes a Marked Increase in the Catalytic Efficiency of Biotin Carboxylase and Carboxyltransferase Relative to Free Biotin

A 70‐amino acid zinc‐binding polypeptide fragment from the regulatory chain of aspartate transcarbamoylase causes marked changes in the kinetic mechanism of the catalytic trimer

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