2.1.3.15	744173	 Acetyl-CoA carboxylase from Escherichia coli exhibits a pronounced hysteresis when inhibited by palmitoyl-acyl carrier protein	Arch. Biochem. Biophys.	 636	 100-109 	2017	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=29100983&form=6&db=m	
2.1.3.15	758050	 Biotin attachment domain-containing proteins irreversibly inhibit acetyl CoA carboxylase	Plant Physiol.	 177	 208-215 	2018	Arabidopsis thaliana	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=29626162&form=6&db=m	
2.1.3.15	756040	 Crystal structure of carboxyltransferase from Staphylococcus aureus bound to the antibacterial agent moiramide B	Biochemistry	 55	 4666-4674 	2016	Staphylococcus aureus	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=27471863&form=6&db=m	
2.1.3.15	758056	 Non-catalytic subunits facilitate quaternary organization of plastidic acetyl-CoA carboxylase	Plant Physiol.	 182	 756-775 	2020	Arabidopsis thaliana	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=31792149&form=6&db=m	
2.1.3.15	744336	 Structural analysis of substrate, reaction intermediate, and product binding in Haemophilus influenzae biotin carboxylase	Biochemistry	 54	 3860-3870 	2015	Haemophilus influenzae	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=26020841&form=6&db=m	
2.1.3.15	744496	 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	Homo sapiens	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=19359168&form=6&db=m	
2.1.3.15	745266	 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	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=10542197&form=6&db=m	
2.1.3.15	758409	 The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium	Sci. Rep.	 7	 42692 	2017	Mycobacterium tuberculosis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28205597&form=6&db=m	
2.1.3.15	758409	 The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium	Sci. Rep.	 7	 42692 	2017	Mycolicibacterium smegmatis	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28205597&form=6&db=m	
2.1.3.15	758409	 The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium	Sci. Rep.	 7	 42692 	2017	Mycobacterium tuberculosis H37Rv	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28205597&form=6&db=m	
2.1.3.15	758409	 The influence of AccD5 on AccD6 carboxyltransferase essentiality in pathogenic and non-pathogenic Mycobacterium	Sci. Rep.	 7	 42692 	2017	Mycolicibacterium smegmatis mc(2)155	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=28205597&form=6&db=m	
2.1.3.15	744305	 The structure of the carboxyltransferase component of acetyl-CoA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme	Biochemistry	 45	 1712-1722 	2006	Staphylococcus aureus	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16460018&form=6&db=m	
2.1.3.15	744305	 The structure of the carboxyltransferase component of acetyl-CoA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme	Biochemistry	 45	 1712-1722 	2006	Escherichia coli	http://www.ncbi.nlm.nih.gov/htbin-post/Entrez/query?uid=16460018&form=6&db=m