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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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Kinetic characterization of the C-terminal domain of Malonyl-CoA reductase

Biochimica et biophysica acta. Proteins and proteomics, 2024-09, Vol.1872 (5), p.141033, Article 141033

2024

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A novel slow-tight binding serine protease inhibitor from eastern oyster ( Crassostrea virginica) plasma inhibits perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 2006-09, Vol.145 (1), p.16-26

2006

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A Biotin Analog Inhibits Acetyl-CoA Carboxylase Activity and Adipogenesis

The Journal of biological chemistry, 2002-05, Vol.277 (19), p.16347-16350

2002

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Complex Formation and Regulation of Escherichia coli Acetyl-CoA Carboxylase

Biochemistry (Easton), 2013-05, Vol.52 (19), p.3346-3357

2013

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A qualitative approach to enzyme inhibition

Biochemistry and molecular biology education, 2009-01, Vol.37 (1), p.11-15

Waldrop, Grover L.

2009

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Kinetic Mechanism and Structural Requirements of the Amine-Catalyzed Decarboxylation of Oxaloacetic Acid

Journal of organic chemistry, 2009-01, Vol.74 (1), p.144-152

2009

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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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Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase

The Journal of biological chemistry, 2004-04, Vol.279 (16), p.15772-15778

2004

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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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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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Mutations at Four Active Site Residues of Biotin Carboxylase Abolish Substrate-Induced Synergism by Biotin

Biochemistry (Easton), 1999-03, Vol.38 (11), p.3393-3400

1999

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Overexpression and Kinetic Characterization of the Carboxyltransferase Component of Acetyl-CoA Carboxylase

The Journal of biological chemistry, 1998-07, Vol.273 (30), p.19140-19145

1998

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Synthesis of a Reaction Intermediate Analogue of Biotin-Dependent Carboxylases via a Selective Derivatization of Biotin

Organic letters, 1999-07, Vol.1 (1), p.99-102

1999

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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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Site-directed mutagenesis of ATP binding residues of biotin carboxylase. Insight into the mechanism of catalysis

The Journal of biological chemistry, 2001-07, Vol.276 (27), p.24991-24996

2001

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Inhibition of Biotin Carboxylase by a Reaction Intermediate Analog: Implications for the Kinetic Mechanism

Biochemical and biophysical research communications, 1999-12, Vol.266 (2), p.466-471

1999

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

Kinetic characterization of the C-terminal domain of Malonyl-CoA reductase

A novel slow-tight binding serine protease inhibitor from eastern oyster ( Crassostrea virginica) plasma inhibits perkinsin, the major extracellular protease of the oyster protozoan parasite Perkinsus marinus

A Biotin Analog Inhibits Acetyl-CoA Carboxylase Activity and Adipogenesis

Complex Formation and Regulation of Escherichia coli Acetyl-CoA Carboxylase

A qualitative approach to enzyme inhibition

Kinetic Mechanism and Structural Requirements of the Amine-Catalyzed Decarboxylation of Oxaloacetic Acid

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

Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase

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

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

Mutations at Four Active Site Residues of Biotin Carboxylase Abolish Substrate-Induced Synergism by Biotin

Overexpression and Kinetic Characterization of the Carboxyltransferase Component of Acetyl-CoA Carboxylase

Synthesis of a Reaction Intermediate Analogue of Biotin-Dependent Carboxylases via a Selective Derivatization of Biotin

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

Site-directed mutagenesis of ATP binding residues of biotin carboxylase. Insight into the mechanism of catalysis

Inhibition of Biotin Carboxylase by a Reaction Intermediate Analog: Implications for the Kinetic Mechanism

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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