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discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: acetyl-CoA carboxylase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of acetyl-CoA carboxylase = [(AccA)2(AccD)2][(AccC)2][(AccB)2]
         acetyl-CoA carboxyltransferase = (AccA)2(AccD)2 (extended summary available)
                 acetyl-CoA carboxyltransferase, α subunit = AccA (summary available)
                 acetyl-CoA carboxyltransferase, β subunit = AccD (summary available)
         biotin carboxylase = (AccC)2
         biotin carboxyl carrier protein (dimer) = (AccB)2 (summary available)
                 biotinylated biotin-carboxyl carrier protein = AccB

Summary:
The enzyme acetyl-CoA carboxylase is one of the key enzymes in the biosynthesis of fatty acids (see superpathway of fatty acid biosynthesis initiation (E. coli)). The enzyme belongs to the family of enzymes that catalyze the intermolecular transfer of carboxyl groups via the transient formation of a carboxyphosphate intermediate covalently linked to a biotin prosthetic group [Barber05]. For a thorough discussion of this protein, please see the pathway biotin-carboxyl carrier protein assembly.

The E. coli enzyme complex is composed of two catalytic units and one carrier protein, encoded by four different genes. The catalytic units are biotin carboxylase (BC), a homodimer encoded by the accC gene, and acetyl-CoA carboxylase (ACCT), an α2β2 tetramer, encoded by the accA and accD genes. The carrier protein is the biotin carboxyl carrier protein (dimer) (BCCP), a homodimer encoded by the accB gene.

The BCCP monomer is biotinylated by the enzyme biotin-[acetyl-CoA-carboxylase] ligase. Following dimerization of the biotinylated monomers, biotin carboxylase (BC) catalyzes the addition of CO2 to the carrier protein dimer, forming a carboxylated-biotinylated [BCCP dimer] (carboxy-BCCP). a carboxylated-biotinylated [BCCP dimer] in turn is the substrate for ACCT, which transfers the carboxy group to acetyl-CoA, resulting in the formation of malonyl-CoA and the regeneration of biotin carboxyl carrier protein (dimer). Both biotinylation and carboxylation of the carrier protein require ATP, while the last step, transfer of the carboxy group to acetyl-CoA, does not [Barber05].

Coordinated overexpression of accA, accB, accC and accD increases the biosynthesis of fatty acids [Davis00a].

Review: [Cronan02a]

Reactions known to produce the compound:

Not in pathways:
an [acetyl-CoA carboxylase] phosphate + H2O → an [acetyl-CoA carboxylase] + phosphate + 2 H+

In Reactions of unknown directionality:

Not in pathways:
an [acetyl-CoA carboxylase] + ATP + H2O = an [acetyl-CoA carboxylase] phosphate + ADP + 2 H+

Gene-Reaction Schematic: ?

GO Terms:

Molecular Function: GO:0003989 - acetyl-CoA carboxylase activity Inferred from experiment [Soriano06]

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: acetyl-CoA carboxylase

EC Number: 6.4.1.2

ATP + acetyl-CoA + hydrogen carbonate <=> malonyl-CoA + ADP + phosphate + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of fatty acid biosynthesis I (E. coli) , superpathway of fatty acid biosynthesis initiation (E. coli) , superpathway of fatty acids biosynthesis (E. coli) , fatty acid biosynthesis initiation I

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
Acetyl-CoA carboxylase is inhibited by acylated derivatives of ACP. The inhibition is of a mixed type, i.e. a combination of competitive and noncompetitive inhibition. The competitive nature of the inhibition suggests an interaction with the acetyl-CoA binding site. This in turn suggests that the acyl-ACP is binding with the acetyl-CoA carboxyltransferase component of the enzyme complex. [Davis01a]

Cofactors or Prosthetic Groups: biotin

Inhibitors (Other): an apo-[acp] [Davis01a]

Kinetic Parameters:

Substrate
Km (μM)
Citations
acetyl-CoA
18.0
[Soriano06]
ATP
60.0
[Soriano06]


Component enzyme of acetyl-CoA carboxylase : AccA

Molecular Weight: 130.0 kD (experimental) [Li92b]

GO Terms:

Biological Process: GO:0017148 - negative regulation of translation Inferred from experiment [Meades10]
Molecular Function: GO:0003677 - DNA binding Inferred from experiment [Benson08]
GO:0003729 - mRNA binding Inferred from experiment [Meades10]
GO:0016743 - carboxyl- or carbamoyltransferase activity Inferred from experiment [Blanchard98]

Relationship Links: PDB:Structure:2F9Y

Catalyzes:
ATP + acetyl-CoA + a carboxylated-biotinylated [BCCP dimer] + H2O → malonyl-CoA + a biotinylated [BCCP dimer] + ADP + phosphate + H+

Summary:
Acetyl-CoA carboxyltransferase is part of the acetyl-CoA carboxylase complex, catalyzing the second half-reaction, the carboxylation of acetyl-CoA to form malonyl-CoA.

The enzyme is feedback inhibited by acyl-ACPs [Davis01a]. Potent inhibitors with antibacterial activity have been identified [Freiberg04].

A crystal structure of the enzyme has been solved at 3.2 Å resolution. The β subunit contains a Zn2+-binding domain, suggesting the ability to bind to DNA [Bilder06]. It was then shown that the enzyme is indeed able to bind DNA nonspecifically, and that DNA binding inhibits enzymatic activity [Benson08]. The Zn2+-binding domain of AccD is required both for catalytic activity and for binding to mRNA; the enzyme has higher specificity to mRNA and binds to the coding regions of accA and accD mRNA, inhibiting their translation [Meades10]. Because substrate binding and nucleotide binding appear to be mutually exclusive, the enzyme is able to regulate its own production and catalytic activity [Meades10].


Subunit of acetyl-CoA carboxyltransferase: acetyl-CoA carboxyltransferase, α subunit

Synonyms: AccA

Gene: accA Accession Numbers: EG11647 (MetaCyc), b0185, ECK0184

Locations: cytosol

Sequence Length: 319 AAs

Molecular Weight: 35.242 kD (from nucleotide sequence)

Molecular Weight: 35.0 kD (experimental) [Li92b]

pI: 6.05

GO Terms:

Biological Process: GO:0006633 - fatty acid biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Davis00a]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0042759 - long-chain fatty acid biosynthetic process Author statement [Benson08]
GO:2001295 - malonyl-CoA biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser14, Rajagopala14, Marsh13, Arifuzzaman06, Butland05]
GO:0042802 - identical protein binding Inferred from experiment [Rajagopala14, Marsh13]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003989 - acetyl-CoA carboxylase activity Inferred by computational analysis [GOA01, GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07, LopezCampistrou05]
GO:0009329 - acetate CoA-transferase complex Inferred from experiment [Li92b]
GO:0005737 - cytoplasm Inferred by curator Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, Davis00a]
GO:0009317 - acetyl-CoA carboxylase complex Inferred by computational analysis [GOA01a]

MultiFun Terms: metabolism biosynthesis of building blocks fatty acids and phosphatidic acid

Unification Links: DIP:DIP-35897N , EcoliWiki:b0185 , Mint:MINT-1228651 , PR:PRO_000022032 , Pride:P0ABD5 , Protein Model Portal:P0ABD5 , RefSeq:NP_414727 , SMR:P0ABD5 , String:511145.b0185 , UniProt:P0ABD5

Relationship Links: InterPro:IN-FAMILY:IPR001095 , InterPro:IN-FAMILY:IPR011763 , Panther:IN-FAMILY:PTHR22855:SF3 , PDB:Structure:2F9Y , Pfam:IN-FAMILY:PF03255 , Prints:IN-FAMILY:PR01069 , Prosite:IN-FAMILY:PS50989

Summary:
accA is an essential gene [Baba06]. Transcription of accA is growth rate-regulated [Li93].

AccA: "acetyl-CoA carboxylase A"


Subunit of acetyl-CoA carboxyltransferase: acetyl-CoA carboxyltransferase, β subunit

Synonyms: Usg, DedB, AccD

Gene: accD Accession Numbers: EG10217 (MetaCyc), b2316, ECK2310

Locations: cytosol

Sequence Length: 304 AAs

Molecular Weight: 33.322 kD (from nucleotide sequence)

Molecular Weight: 31.5 kD (experimental) [Li92b]

pI: 8.77

GO Terms:

Biological Process: GO:0006633 - fatty acid biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Davis00a]
GO:0017148 - negative regulation of translation Inferred from experiment [Meades10]
GO:0006417 - regulation of translation Inferred by computational analysis [UniProtGOA11a]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0042759 - long-chain fatty acid biosynthetic process Author statement [Benson08]
GO:2001295 - malonyl-CoA biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0003677 - DNA binding Inferred from experiment [Meades10]
GO:0003729 - mRNA binding Inferred from experiment [Meades10]
GO:0003989 - acetyl-CoA carboxylase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Davis00a]
GO:0005515 - protein binding Inferred from experiment [Zheng11, Hauser14, Rajagopala14, Marsh13, Arifuzzaman06, Butland05]
GO:0008270 - zinc ion binding Inferred from experiment Inferred by computational analysis [GOA06, Bilder06, Meades10]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003723 - RNA binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [Lasserre06]
GO:0009329 - acetate CoA-transferase complex Inferred from experiment [Li92b]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]
GO:0009317 - acetyl-CoA carboxylase complex Inferred by computational analysis [GOA01a]

MultiFun Terms: metabolism biosynthesis of building blocks fatty acids and phosphatidic acid

Unification Links: DIP:DIP-35878N , EcoliWiki:b2316 , Mint:MINT-1234646 , ModBase:P0A9Q5 , PR:PRO_000022035 , Pride:P0A9Q5 , Protein Model Portal:P0A9Q5 , RefSeq:NP_416819 , SMR:P0A9Q5 , String:511145.b2316 , UniProt:P0A9Q5

Relationship Links: InterPro:IN-FAMILY:IPR000022 , InterPro:IN-FAMILY:IPR000438 , InterPro:IN-FAMILY:IPR011762 , PDB:Structure:2F9Y , Pfam:IN-FAMILY:PF01039 , Prints:IN-FAMILY:PR01070 , Prosite:IN-FAMILY:PS50980

Summary:
The Zn2+-binding domain of AccD is required both for catalytic activity and for binding to mRNA [Meades10].

Transcription of accD is growth rate-regulated [Li93].

A lesson in gene naming:

DedB: "downstream E. coli DNA (from hisT)" [Nonet87]

Usg: "upstream gene" [Bognar87]

AccD: "acetyl-CoA carboxylase D" [Li92a]

Citations: [Nagano91]


Component enzyme of acetyl-CoA carboxylase : AccC

Synonyms: fabG

Gene: accC Accession Numbers: EG10276 (MetaCyc), b3256, ECK3243

Locations: cytosol

Subunit composition of biotin carboxylase = [AccC]2

Map Position: [3,403,939 -> 3,405,288]

Molecular Weight of Polypeptide: 49.321 kD (from nucleotide sequence)

pI: 7.08

GO Terms:

Biological Process: GO:0006633 - fatty acid biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Davis00a]
GO:0045717 - negative regulation of fatty acid biosynthetic process Inferred from experiment [AbdelHamid07]
GO:0006629 - lipid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0006631 - fatty acid metabolic process Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:2001295 - malonyl-CoA biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0004075 - biotin carboxylase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Davis00a]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06, Butland05]
GO:0042803 - protein homodimerization activity Inferred from experiment [Smith12]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0003989 - acetyl-CoA carboxylase activity Inferred by computational analysis [GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by curator [Davis00a]

MultiFun Terms: metabolism biosynthesis of building blocks fatty acids and phosphatidic acid

Unification Links: DIP:DIP-9035N , EcoliWiki:b3256 , Mint:MINT-1266968 , ModBase:P24182 , PR:PRO_000022034 , Pride:P24182 , Protein Model Portal:P24182 , RefSeq:NP_417722 , SMR:P24182 , String:511145.b3256 , UniProt:P24182

Relationship Links: InterPro:IN-FAMILY:IPR004549 , InterPro:IN-FAMILY:IPR005479 , InterPro:IN-FAMILY:IPR005481 , InterPro:IN-FAMILY:IPR005482 , InterPro:IN-FAMILY:IPR011054 , InterPro:IN-FAMILY:IPR011761 , InterPro:IN-FAMILY:IPR011764 , InterPro:IN-FAMILY:IPR013815 , InterPro:IN-FAMILY:IPR013816 , InterPro:IN-FAMILY:IPR016185 , PDB:Structure:1BNC , PDB:Structure:1DV1 , PDB:Structure:1DV2 , PDB:Structure:1K69 , PDB:Structure:2GPS , PDB:Structure:2GPW , PDB:Structure:2J9G , PDB:Structure:2V58 , PDB:Structure:2V59 , PDB:Structure:2V5A , PDB:Structure:2VR1 , PDB:Structure:2W6M , PDB:Structure:2W6N , PDB:Structure:2W6O , PDB:Structure:2W6P , PDB:Structure:2W6Q , PDB:Structure:2W6Z , PDB:Structure:2W70 , PDB:Structure:2W71 , PDB:Structure:3G8C , PDB:Structure:3G8D , PDB:Structure:3JZF , PDB:Structure:3JZI , PDB:Structure:3RUP , PDB:Structure:3RV3 , PDB:Structure:3RV4 , PDB:Structure:4HR7 , Pfam:IN-FAMILY:PF00289 , Pfam:IN-FAMILY:PF02785 , Pfam:IN-FAMILY:PF02786 , Prosite:IN-FAMILY:PS00866 , Prosite:IN-FAMILY:PS00867 , Prosite:IN-FAMILY:PS50975 , Prosite:IN-FAMILY:PS50979 , Smart:IN-FAMILY:SM00878

Catalyzes:
a biotinylated [BCCP dimer] + hydrogen carbonate + ATP → a carboxylated-biotinylated [BCCP dimer] + ADP + phosphate + H+

Summary:
Mutations in the homologous and functionally identical subunit in mammalian proprionyl-CoA carboxylase and 3-methylcrotonyl-CoA carboxylase result in the metabolic deficiency diseases of propionic acidemia or methylcrotonylglycinuria. Kinetic analysis of mutants analogous to the disease-causing mutants has been performed to determine the function of those residues [Sloane04].

Studies with dimerization-deficient accC mutants showed that only dimeric biotin carboxylase fulfills its physiological function in vivo [Smith12].


Subunit of acetyl-CoA carboxylase: biotin carboxyl carrier protein (dimer)

Synonyms: fabE, [acetyl-CoA:carbon-dioxide ligase (ADP forming)], BCCP-biotin (monomer), biotin-BCCP (monomer), BCCP

Gene: accB Accession Numbers: EG10275 (MetaCyc), b3255, ECK3242

Locations: cytosol

Subunit composition of biotin carboxyl carrier protein (dimer) = [AccB]2
         biotinylated biotin-carboxyl carrier protein = AccB

Map Position: [3,403,458 -> 3,403,928]

Molecular Weight of Polypeptide: 16.687 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006633 - fatty acid biosynthetic process Inferred from experiment [Dimroth70]
Molecular Function: GO:0009374 - biotin binding Inferred from experiment [Sutton77]
Cellular Component: GO:0009317 - acetyl-CoA carboxylase complex Inferred from experiment [Dimroth70]

MultiFun Terms: metabolism biosynthesis of macromolecules (cellular constituents) large molecule carriers biotin carboxyl carrier protein

Unification Links: RefSeq:NP_417721

Relationship Links: Pfam:IN-FAMILY:PF00364

Reactions known to consume the compound:

biotin-carboxyl carrier protein assembly :
2 a biotinylated [BCCP monomer] → a biotinylated [BCCP dimer]
a [biotin-carboxyl-carrier protein monomer] + biotin + ATP → AMP + a biotinylated [BCCP monomer] + diphosphate

biotin-carboxyl carrier protein assembly :
a [biotin-carboxyl-carrier protein monomer] + biotin + ATP → AMP + a biotinylated [BCCP monomer] + diphosphate

Reactions known to consume the compound:

biotin-carboxyl carrier protein assembly :
a biotinylated [BCCP dimer] + hydrogen carbonate + ATP → a carboxylated-biotinylated [BCCP dimer] + ADP + phosphate + H+

Reactions known to produce the compound:

biotin-carboxyl carrier protein assembly :
ATP + acetyl-CoA + a carboxylated-biotinylated [BCCP dimer] + H2O → malonyl-CoA + a biotinylated [BCCP dimer] + ADP + phosphate + H+
2 a biotinylated [BCCP monomer] → a biotinylated [BCCP dimer]

Summary:
Biotin carboxyl carrier protein (BCCP) plays a central role in the acetyl-CoA carboxylase complex. The overall carboxylase reaction takes place in two distinct half-reactions. BCCP, which contains a biotinyl prosthetic group covalently attached to a specific lysyl residue, is carboxylated in the first partial reaction. In the second partial reaction the carboxyl group is transferred to an acceptor and BCCP is regenerated for further carboxylation [Sutton77]. On the other hand, BCCP amino terminal is able to bind to DNA; this means, BCCP autoregulates its coding gene expression (the accBD operon) [James04].

Citations: [Blanchard99a]


References

AbdelHamid07: Abdel-Hamid AM, Cronan JE (2007). "Coordinate expression of the acetyl coenzyme A carboxylase genes, accB and accC, is necessary for normal regulation of biotin synthesis in Escherichia coli." J Bacteriol 189(2);369-76. PMID: 17056747

Arifuzzaman06: Arifuzzaman M, Maeda M, Itoh A, Nishikata K, Takita C, Saito R, Ara T, Nakahigashi K, Huang HC, Hirai A, Tsuzuki K, Nakamura S, Altaf-Ul-Amin M, Oshima T, Baba T, Yamamoto N, Kawamura T, Ioka-Nakamichi T, Kitagawa M, Tomita M, Kanaya S, Wada C, Mori H (2006). "Large-scale identification of protein-protein interaction of Escherichia coli K-12." Genome Res 16(5);686-91. PMID: 16606699

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Barber05: Barber MC, Price NT, Travers MT (2005). "Structure and regulation of acetyl-CoA carboxylase genes of metazoa." Biochim Biophys Acta 1733(1);1-28. PMID: 15749055

Benson08: Benson BK, Meades G, Grove A, Waldrop GL (2008). "DNA inhibits catalysis by the carboxyltransferase subunit of acetyl-CoA carboxylase: implications for active site communication." Protein Sci 17(1);34-42. PMID: 18156466

Bilder06: Bilder P, Lightle S, Bainbridge G, Ohren J, Finzel B, Sun F, Holley S, Al-Kassim L, Spessard C, Melnick M, Newcomer M, Waldrop GL (2006). "The structure of the carboxyltransferase component of acetyl-coA carboxylase reveals a zinc-binding motif unique to the bacterial enzyme." Biochemistry 45(6);1712-22. PMID: 16460018

Blanchard98: Blanchard CZ, Waldrop GL (1998). "Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase." J Biol Chem 273(30);19140-5. PMID: 9668099

Blanchard99a: Blanchard CZ, Chapman-Smith A, Wallace JC, Waldrop GL (1999). "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 1999;274(45);31767-9. PMID: 10542197

Bognar87: Bognar AL, Osborne C, Shane B (1987). "Primary structure of the Escherichia coli folC gene and its folylpolyglutamate synthetase-dihydrofolate synthetase product and regulation of expression by an upstream gene." J Biol Chem 262(25);12337-43. PMID: 3040739

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Cronan02a: Cronan JE, Waldrop GL (2002). "Multi-subunit acetyl-CoA carboxylases." Prog Lipid Res 41(5);407-35. PMID: 12121720

Davis00a: Davis MS, Solbiati J, Cronan JE (2000). "Overproduction of acetyl-CoA carboxylase activity increases the rate of fatty acid biosynthesis in Escherichia coli." J Biol Chem 275(37);28593-8. PMID: 10893421

Davis01a: Davis MS, Cronan, Jr. JE (2001). "Inhibition of Escherichia coli acetyl coenzyme A carboxylase by acyl-acyl carrier protein." J Bacteriol. 183(4):1499-503. PMID: 11157970

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Dimroth70: Dimroth P, Guchhait RB, Stoll E, Lane MD (1970). "Enzymatic carboxylation of biotin: molecular and catalytic properties of a component enzyme of acetyl CoA carboxylase." Proc Natl Acad Sci U S A 67(3);1353-60. PMID: 4922289

Freiberg04: Freiberg C, Brunner NA, Schiffer G, Lampe T, Pohlmann J, Brands M, Raabe M, Habich D, Ziegelbauer K (2004). "Identification and characterization of the first class of potent bacterial acetyl-CoA carboxylase inhibitors with antibacterial activity." J Biol Chem 279(25);26066-73. PMID: 15066985

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Hauser14: Hauser R, Ceol A, Rajagopala SV, Mosca R, Siszler G, Wermke N, Sikorski P, Schwarz F, Schick M, Wuchty S, Aloy P, Uetz P (2014). "A Second-generation Protein-Protein Interaction Network of Helicobacter pylori." Mol Cell Proteomics 13(5);1318-29. PMID: 24627523

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

James04: James ES, Cronan JE (2004). "Expression of two Escherichia coli acetyl-CoA carboxylase subunits is autoregulated." J Biol Chem 279(4);2520-7. PMID: 14594796

Lasserre06: Lasserre JP, Beyne E, Pyndiah S, Lapaillerie D, Claverol S, Bonneu M (2006). "A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis." Electrophoresis 27(16);3306-21. PMID: 16858726

Li92a: Li SJ, Rock CO, Cronan JE (1992). "The dedB (usg) open reading frame of Escherichia coli encodes a subunit of acetyl-coenzyme A carboxylase." J Bacteriol 174(17);5755-7. PMID: 1355086

Li92b: Li SJ, Cronan JE (1992). "The genes encoding the two carboxyltransferase subunits of Escherichia coli acetyl-CoA carboxylase." J Biol Chem 1992;267(24);16841-7. PMID: 1355089

Li93: Li SJ, Cronan JE (1993). "Growth rate regulation of Escherichia coli acetyl coenzyme A carboxylase, which catalyzes the first committed step of lipid biosynthesis." J Bacteriol 175(2);332-40. PMID: 7678242

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Marsh13: Marsh JA, Hernandez H, Hall Z, Ahnert SE, Perica T, Robinson CV, Teichmann SA (2013). "Protein complexes are under evolutionary selection to assemble via ordered pathways." Cell 153(2);461-70. PMID: 23582331

Meades10: Meades G, Benson BK, Grove A, Waldrop GL (2010). "A tale of two functions: enzymatic activity and translational repression by carboxyltransferase." Nucleic Acids Res 38(4);1217-27. PMID: 19965770

Nagano91: Nagano Y, Matsuno R, Sasaki Y (1991). "An essential gene of Escherichia coli that has sequence similarity to a chloroplast gene of unknown function." Mol Gen Genet 228(1-2);62-4. PMID: 1886618

Nonet87: Nonet ML, Marvel CC, Tolan DR (1987). "The hisT-purF region of the Escherichia coli K-12 chromosome. Identification of additional genes of the hisT and purF operons." J Biol Chem 262(25);12209-17. PMID: 3040734

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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