Search Reference

2.1.3.15

Acetyl-CoA carboxylase from Escherichia coli exhibits a pronounced hysteresis when inhibited by palmitoyl-acyl carrier protein

Arch. Biochem. Biophys.

636

100-109

2017

2.1.3.15

Biotin attachment domain-containing proteins irreversibly inhibit acetyl CoA carboxylase

Plant Physiol.

177

208-215

2018

2.1.3.15

Crystal structure of carboxyltransferase from Staphylococcus aureus bound to the antibacterial agent moiramide B

Biochemistry

55

4666-4674

2016

2.1.3.15

Non-catalytic subunits facilitate quaternary organization of plastidic acetyl-CoA carboxylase

Plant Physiol.

182

756-775

2020

2.1.3.15

Structural analysis of substrate, reaction intermediate, and product binding in Haemophilus influenzae biotin carboxylase

Biochemistry

54

3860-3870

2015

2.1.3.15

Synthesis and characterization of a BODIPY-labeled derivative of Soraphen A that binds to acetyl-CoA carboxylase

Bioorg. Med. Chem. Lett.

19

2804-2807

2009

2.1.3.15

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

J. Biol. Chem.

274

31767-31769

1999

2.1.3.15

The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium

Sci. Rep.

7

42692

2017

2.1.3.15

The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium

Sci. Rep.

7

42692

2017

2.1.3.15

The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium

Sci. Rep.

7

42692

2017