Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

MetaCyc Enzyme: enterobactin synthase

Synonyms: enterobactin synthetase multienzyme complex

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of enterobactin synthase = [EntB isochorismatase / aryl-carrier protein][EntD][EntF][(EntE)2]
         phosphopantetheinyl transferase = EntD (extended summary available)
         aryl carrier protein / L-seryl-AMP synthase = EntF (extended summary available)
         2,3-dihydroxybenzoate-AMP ligase = (EntE)2 (extended summary available)

Summary:
Enterobactin contains three units of 2,3-dihydroxybenzoylserine joined in a cyclic structure by lactone linkages. Studies have suggested that the later steps of enterobactin synthesis are carried out by a multienzyme complex consisting of the entD, entE, entF and entB gene products [Hantash97].

Proteins EntB, EntD, EntE and EntF of the enterobactin synthase multienzyme complex have been purified and characterized, but no evidence has been obtained for the existence of a stable multienzyme complex. These proteins are required for the ATP-dependent conversion of three molecules each of 2,3-dihydroxybenzoate and L-serine to enterobactin [Gehring97, Gehring98, Drake06].

Proteins EntB, EntE and EntF together contain domains that comprise a nonribosomal peptide synthase (NRPS). EntE provides an adenylation domain, EntB provides an aryl carrier protein domain (located at its C-terminus), and EntF provides condensation, adenylation, peptidyl carrier protein, and chain-releasing thioesterase domains. Thus, six domains of three proteins comprise a two-module NRPS [Ehmann00]. EntD is a phosphopantetheinyl transferase that adds this cofactor to the peptidyl carrier protein domains of EntB and EntF [Gehring97]. The activities of EntE, the EntB C-terminal domain, and EntF assemble enterobactin in an iterative manner [Drake06, Ehmann00].

Gene-Reaction Schematic: ?

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


Enzymatic reaction of: enterobactin synthase

EC Number: 6.3.2.14

3 L-serine + 3 2,3-dihydroxybenzoate + 6 ATP <=> enterobactin + 6 AMP + 6 diphosphate + 3 H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

In Pathways: superpathway of chorismate metabolism , enterobactin biosynthesis

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


Component enzyme of enterobactin synthase : EntB isochorismatase / aryl-carrier protein

Synonyms: holo-EntB

Sequence Length: 285 AAs

GO Terms:

Biological Process: GO:0009239 - enterobactin biosynthetic process Inferred from experiment [Staab90, Gehring98]
Molecular Function: GO:0008908 - isochorismatase activity Inferred from experiment [Rusnak90, Staab90]
GO:0031177 - phosphopantetheine binding Inferred from experiment [Gehring97]
Cellular Component: GO:0009366 - enterobactin synthetase complex Inferred from experiment [Gehring98]

MultiFun Terms: cell structure membrane
information transfer protein related Non-ribosomal peptide synthetase
metabolism biosynthesis of building blocks cofactors, small molecule carriers enterochelin (enterobactin)

Catalyzes:
isochorismate + H2O → pyruvate + (2S,3S)-2,3-dihydroxy-2,3-dihydrobenzoate

Reactions known to produce the compound:

Not in pathways:
isochorismatase / aryl-carrier protein + coenzyme A → EntB isochorismatase / aryl-carrier protein + adenosine 3',5'-bisphosphate

Summary:
The EntB protein is bifunctional, the N-terminal domain contains the isochorismate lyase (isochorismatase) activity and the C-terminus contains the aryl carrier protein (ArCP) domain. The isochorismatase activity of the entB gene product catalyzes the second step in both the overall enterobactin biosynthetic pathway (see pathway enterobactin biosynthesis) and in the first part of the pathway, the conversion of chorismate to 2,3-dihydroxybenzoate (see pathway 2,3-dihydroxybenzoate biosynthesis) [Rusnak90, Staab90].

The ArCP domain of apo-EntB becomes phosphopantetheinylated in a reaction catalyzed by the entD gene product, phosphopantetheinyl transferase. The EntB isochorismatase / aryl-carrier protein (holo-EntB) formed can now serve as a substrate for the entE product, a 2,3-dihydroxybenzoate-AMP ligase that activates 2,3-dihydroxybenzoate as the acyl-AMP derivative and transfers the acyl moiety onto holo-EntB. The arylated holo-EntB product (aryl-EntB) then serves as the aryl donor for the amide bond formation in enterobactin assembly [Gehring97, Gehring98].

The crystal structure of this two domain protein has been determined at 2.3 Å resolution. Its two functionally independent domains are joined by a proline-rich linker. Functional analysis of EntB and EntE mutants probed the interaction between these two proteins [Drake06].

Based on gel filtration data, EntB was originally suggested to be a pentamer [Rusnak90] and later suggested to be a trimer [Gehring98]. However subsequent gel filtration and crystallographic data showed it to be a dimer [Drake06]. Cell lysis and fractionation studies have led to the proposal that a large fraction of the Ent synthase proteins EntB, EntE and EntF is in contact with membranes, or in close proximity to membranes [Hantash00].

A biophysical study of EntE substrate binding and the interaction between EntE and EntB showed that complex formation is most efficient in the presence of 2,3-dihydroxybenzoate [Khalil09]. The thioesterase EntH has been proposed to potentially function in the prevention or reversal of EntB misacylation events [Chen09, Guo09a]. Using combinatorial mutagenesis and selection, the interaction surface between the ArCP domain of holo-EntB and holo-EntF was mapped [Lai06, Lai06a].

Studies of a reduced-genome E. coli suggested that genes entB, marR, dosC, mcbR and yahK were involved in biofilm formation. Overproduction of entB and yahK promoted biofilm development and maturation [May11].

Review: [Koglin09]


Component enzyme of enterobactin synthase : EntD

Synonyms: EntD, enterobactin synthetase component D, enterochelin synthase D

Gene: entD Accession Numbers: EG10262 (MetaCyc), b0583, ECK0575

Locations: cytosol, inner membrane

Sequence Length: 206 AAs

Molecular Weight: 23.259 kD (from nucleotide sequence)

pI: 6.23

GO Terms:

Biological Process: GO:0009239 - enterobactin biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA01a, Luke71]
GO:0009059 - macromolecule biosynthetic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0008897 - holo-[acyl-carrier-protein] synthase activity Inferred from experiment Inferred by computational analysis [GOA01a, Gehring98, Gehring97]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016780 - phosphotransferase activity, for other substituted phosphate groups Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0009366 - enterobactin synthetase complex Inferred from experiment Inferred by computational analysis [GOA01a, Gehring98]
GO:0031226 - intrinsic component of plasma membrane Inferred from experiment [Armstrong89]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: cell structure membrane
metabolism biosynthesis of building blocks cofactors, small molecule carriers enterochelin (enterobactin)

Unification Links: DIP:DIP-9514N , EcoliWiki:b0583 , ModBase:P19925 , PR:PRO_000022522 , Protein Model Portal:P19925 , RefSeq:NP_415115 , SMR:P19925 , String:511145.b0583 , UniProt:P19925

Relationship Links: InterPro:IN-FAMILY:IPR003542 , InterPro:IN-FAMILY:IPR008278 , Pfam:IN-FAMILY:PF01648 , Prints:IN-FAMILY:PR01399

Catalyzes:
isochorismatase / aryl-carrier protein + coenzyme A → EntB isochorismatase / aryl-carrier protein + adenosine 3',5'-bisphosphate

Summary:
AcpS is the founding member of a 4'-phosphopantetheinyl (P-pant) transferase protein family that includes E. coli EntD, E. coli o195 protein, and Bacillus subtilis Sfp; family members share two conserved motifs but relatively low sequence identity overall [Lambalot96].

During enterobactin biosynthesis EntD catalyzes a posttranslational modification by transferring the phosphopantetheinyl moiety of coenzyme A onto a serine side chain in both the C-terminal apo-aryl carrier protein domain of EntB, and a homologous apo-aryl carrier protein domain of EntF. Thus, EntD mediates conversion of the apo-forms of EntB and EntF to their phosphopantetheinylated holo-forms, which primes them for their roles in acyl activation and transfer during enterobactin assembly [Gehring97, Lambalot96] (see pathway enterobactin biosynthesis).

EntD has been reported to be associated with the inner leaflet of the cytoplasmic membrane [Armstrong89].

Studies have shown that overexpressed EntD (and potentially other Sfp-type phosphopantetheinyl transferases) can complement a heterologous Shewanella pfaE-deficient gene clone comprising pfaA, pfaB, pfaC and pfaD that is involved in long-chain n-3 polyunsaturated fatty acid biosynthesis [Sugihara10].


Component enzyme of enterobactin synthase : EntF

Synonyms: EntF, enterochelin synthase F, enterobactin synthetase component F, aryl carrier protein / serine activating enzyme

Gene: entF Accession Numbers: EG10264 (MetaCyc), b0586, ECK0579

Sequence Length: 1293 AAs

Molecular Weight: 141.99 kD (from nucleotide sequence)

Molecular Weight: 142.0 kD (experimental) [Gehring98]

GO Terms:

Biological Process: GO:0009239 - enterobactin biosynthetic process Inferred from experiment [Gehring98]
GO:0043041 - amino acid activation for nonribosomal peptide biosynthetic process Inferred from experiment [Rusnak91]
Molecular Function: GO:0031177 - phosphopantetheine binding Inferred from experiment [Lambalot96]
Cellular Component: GO:0009366 - enterobactin synthetase complex Inferred from experiment [Gehring98]

MultiFun Terms: cell processes adaptations Fe aquisition
cell structure membrane
information transfer protein related Non-ribosomal peptide synthetase
metabolism biosynthesis of building blocks cofactors, small molecule carriers Coenzyme A and its modification
metabolism biosynthesis of building blocks cofactors, small molecule carriers enterochelin (enterobactin)

Unification Links: RefSeq:NP_415118

Relationship Links: Pfam:IN-FAMILY:PF00668

Catalyzes:
3 2,3-dihydroxybenzoyl-AMP + 3 L-seryl-AMP = enterobactin + 6 AMP + 6 H+ ,
L-serine + ATP ↔ L-seryl-AMP + diphosphate

Summary:
apo-serine activating enzyme, the entF gene product, activates L-serine through an ATP-pyrophosphate exchange reaction at the carboxylate group of L-serine. The resulting aminoacyladenylate remains enzyme-bound for further reactions in the enterobactin biosynthesis pathway. The enzyme also contains a covalently bound phosphopantetheine moiety that is the result of an EntD catalyzed activation reaction. In this reaction the apo-serine activating enzyme is phosphopantetheinylated posttranslationally by EntD resulting in the active aryl carrier protein / L-seryl-AMP synthase form [Pettis87, Rusnak91, Reichert92, Lambalot96, Hantash97].

An enterobactin synthase reconstitution assay demonstrated that EntE acylates EntB isochorismatase / aryl-carrier protein (holo-EntB) with 2,3-dihydroxybenzoate, forming aryl-EntB which functions as an acyl donor substrate for aryl carrier protein / L-seryl-AMP synthase. The latter enzyme catalyzes formation of the three amide and three ester bonds in enterobactin using ATP, L-serine, and aryl-EntB as substrates [Gehring98].

EntF is a four-domain protein that contains an N-terminal elongation/condensatin domain, an adenylation domain, a peptidyl carrier protein domain, and a C-terminal thioesterase domain [Ehmann00]. An NMR solution structure of a thiolation-thioesterase (peptidyl carrier protein-thioesterase) di-domain fragment of EntF as been determined [Frueh08].

EntF can be released from the cell by osmotic shock, but not by formation of spheroplasts; it was therefore suggested that the enzyme is membrane-associated [Hantash97]. Subsequent cell lysis and fractionation studies have led to the proposal that a large fraction of the Ent synthase proteins EntF, EntE and EntB is in contact with membranes, or in close proximity to membranes [Hantash00].

Review: [Koglin09]


Component enzyme of enterobactin synthase : 2,3-dihydroxybenzoate-AMP ligase

Synonyms: enterobactin synthetase component E, enterochelin synthase E, enterobactin synthase component E

Gene: entE Accession Numbers: EG10263 (MetaCyc), b0594, ECK0587

Locations: inner membrane, cytosol, membrane

Subunit composition of 2,3-dihydroxybenzoate-AMP ligase = [EntE]2

Map Position: [625,293 -> 626,903]

Molecular Weight of Polypeptide: 59.112 kD (from nucleotide sequence), 58.0 kD (experimental) [Nahlik87 ]

Molecular Weight of Multimer: 115.0 kD (experimental) [Rusnak89]

pI: 6.15

GO Terms:

Biological Process: GO:0009239 - enterobactin biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, Luke71]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0019290 - siderophore biosynthetic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0008668 - (2,3-dihydroxybenzoyl)adenylate synthase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Rusnak89]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016746 - transferase activity, transferring acyl groups Inferred by computational analysis [UniProtGOA11a]
GO:0016874 - ligase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Hantash00]
GO:0016020 - membrane Inferred from experiment [Hantash00]
GO:0005737 - cytoplasm
GO:0005886 - plasma membrane

MultiFun Terms: cell structure membrane
metabolism biosynthesis of building blocks cofactors, small molecule carriers enterochelin (enterobactin)

Unification Links: DIP:DIP-9515N , EcoliWiki:b0594 , Mint:MINT-1228110 , ModBase:P10378 , PR:PRO_000022523 , Pride:P10378 , Protein Model Portal:P10378 , RefSeq:NP_415126 , SMR:P10378 , String:511145.b0594 , Swiss-Model:P10378 , UniProt:P10378

Relationship Links: InterPro:IN-FAMILY:IPR000873 , InterPro:IN-FAMILY:IPR011963 , InterPro:IN-FAMILY:IPR020845 , InterPro:IN-FAMILY:IPR025110 , PDB:Structure:3RG2 , PDB:Structure:4IZ6 , Pfam:IN-FAMILY:PF00501 , Pfam:IN-FAMILY:PF13193 , Prosite:IN-FAMILY:PS00455

Catalyzes:
2,3-dihydroxybenzoate + ATP + H+ → 2,3-dihydroxybenzoyl-AMP + diphosphate ,
ATP + ATP + H+ = 5',5'''-diadenosine tetraphosphate + diphosphate

Summary:
EntE is an enzyme of the enterobactin biosynthesis pathway that catalyzes the ATP-dependent condensation of 2,3-dihydroxybenzoate (DHB) and EntB isochorismatase / aryl-carrier protein (holo-EntB) to form the covalently arylated form of EntB, aryl-EntB. EntE activity has been characterized as a two-step adenylation-ligation reaction. In the first step it catalyzes the condensation of DHB with ATP to form the adenylate intermediate 2,3-dihydroxybenzoyl-AMP. In the second step DHB is ligated onto the phosphopantetheinyl cofactor of holo-entB to form aryl-entB [Sikora10].

Initial studies showed that EntE is a 2,3-dihydroxybenzoate-AMP ligase, and kinetic data suggested that the (2,3-dihydroxybenzoyl)adenylate intermediate remains bound to the enzyme [Rusnak89]. Later, EntE was found to catalyze a second half-reaction, transfer of the aryl fragment, 2,3-dihydroxybenzoate, via a thioester linkage to the phosphopantetheinyl moiety of holo-EntB [Gehring97]. The kinetic mechanism has been studied in detail, suggesting a bi-uni-uni-b ping pong mechanism [Sikora10]. The adenylation activity of EntE is specific for holo-EntB [Ehmann00]. The interaction between EntE and holo-EntB is remarkably tolerant to point mutations in the predicted interaction surface of EntB [Drake06] and is most efficient in the presence of DHB [Khalil09]. In the absence of holo-EntB, EntE can transfer the adenylate moiety of the (2,3-dihydroxybenzoyl)adenylate intermediate to ATP, generating the stress signaling molecule Ap4A and releasing 2,3-dihydroxybenzoate [Sikora09]. Enhancement of the DHB-AMP ligase activity of EntE by interaction with the DHB-producing enzyme EntA has been demonstrated [Khalil11].

EntE can be released from the cell by osmotic shock, but not by formation of spheroplasts; it was therefore suggested that the enzyme is membrane-associated [Hantash97]. Subsequent cell lysis and fractionation studies have led to the proposal that a large fraction of the Ent synthase proteins EntE, EntB and EntF is in contact with membranes, or in close proximity to membranes [Hantash00]. Gel filtration data disagree on whether EntE is a monomer [Gehring98] or a dimer [Rusnak89] in solution. No stable interaction between the components of the "enterobactin synthase multienzyme complex" can be detected [Gehring98].

Expression of entE is induced under conditions of iron deficiency [Fleming83].


References

Armstrong89: Armstrong SK, Pettis GS, Forrester LJ, McIntosh MA (1989). "The Escherichia coli enterobactin biosynthesis gene, entD: nucleotide sequence and membrane localization of its protein product." Mol Microbiol 3(6);757-66. PMID: 2526281

Chen09: Chen D, Wu R, Bryan TL, Dunaway-Mariano D (2009). "In vitro kinetic analysis of substrate specificity in enterobactin biosynthetic lower pathway enzymes provides insight into the biochemical function of the hot dog-fold thioesterase EntH." Biochemistry 48(3);511-3. PMID: 19119850

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

Drake06: Drake EJ, Nicolai DA, Gulick AM (2006). "Structure of the EntB multidomain nonribosomal peptide synthetase and functional analysis of its interaction with the EntE adenylation domain." Chem Biol 13(4);409-19. PMID: 16632253

Ehmann00: Ehmann DE, Shaw-Reid CA, Losey HC, Walsh CT (2000). "The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates." Proc Natl Acad Sci U S A 97(6);2509-14. PMID: 10688898

Fleming83: Fleming TP, Nahlik MS, McIntosh MA (1983). "Regulation of enterobactin iron transport in Escherichia coli: characterization of ent::Mu d(Apr lac) operon fusions." J Bacteriol 156(3);1171-7. PMID: 6227609

Frueh08: Frueh DP, Arthanari H, Koglin A, Vosburg DA, Bennett AE, Walsh CT, Wagner G (2008). "Dynamic thiolation-thioesterase structure of a non-ribosomal peptide synthetase." Nature 454(7206);903-6. PMID: 18704088

Gehring97: Gehring AM, Bradley KA, Walsh CT (1997). "Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate." Biochemistry 1997;36(28);8495-503. PMID: 9214294

Gehring98: Gehring AM, Mori I, Walsh CT (1998). "Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF." Biochemistry 1998;37(8);2648-59. PMID: 9485415

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."

Guo09a: Guo ZF, Sun Y, Zheng S, Guo Z (2009). "Preferential hydrolysis of aberrant intermediates by the type II thioesterase in Escherichia coli nonribosomal enterobactin synthesis: substrate specificities and mutagenic studies on the active-site residues." Biochemistry 48(8);1712-22. PMID: 19193103

Hantash00: Hantash FM, Earhart CF (2000). "Membrane association of the Escherichia coli enterobactin synthase proteins EntB/G, EntE, and EntF." J Bacteriol 182(6);1768-73. PMID: 10692387

Hantash97: Hantash FM, Ammerlaan M, Earhart CF (1997). "Enterobactin synthase polypeptides of Escherichia coli are present in an osmotic-shock-sensitive cytoplasmic locality." Microbiology 1997;143 ( Pt 1);147-56. PMID: 9025288

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

Khalil09: Khalil S, Pawelek PD (2009). "Ligand-induced conformational rearrangements promote interaction between the Escherichia coli enterobactin biosynthetic proteins EntE and EntB." J Mol Biol 393(3);658-71. PMID: 19699210

Khalil11: Khalil S, Pawelek PD (2011). "Enzymatic adenylation of 2,3-dihydroxybenzoate is enhanced by a protein-protein interaction between Escherichia coli 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (EntA) and 2,3-dihydroxybenzoate-AMP ligase (EntE)." Biochemistry 50(4);533-45. PMID: 21166461

Koglin09: Koglin A, Walsh CT (2009). "Structural insights into nonribosomal peptide enzymatic assembly lines." Nat Prod Rep 26(8);987-1000. PMID: 19636447

Lai06: Lai JR, Fischbach MA, Liu DR, Walsh CT (2006). "A protein interaction surface in nonribosomal peptide synthesis mapped by combinatorial mutagenesis and selection." Proc Natl Acad Sci U S A 103(14);5314-9. PMID: 16567620

Lai06a: Lai JR, Fischbach MA, Liu DR, Walsh CT (2006). "Localized protein interaction surfaces on the EntB carrier protein revealed by combinatorial mutagenesis and selection." J Am Chem Soc 128(34);11002-3. PMID: 16925399

Lambalot96: Lambalot RH, Gehring AM, Flugel RS, Zuber P, LaCelle M, Marahiel MA, Reid R, Khosla C, Walsh CT (1996). "A new enzyme superfamily - the phosphopantetheinyl transferases." Chem Biol 1996;3(11);923-36. PMID: 8939709

Luke71: Luke RK, Gibson F (1971). "Location of three genes concerned with the conversion of 2,3-dihydroxybenzoate into enterochelin in Escherichia coli K-12." J Bacteriol 107(2);557-62. PMID: 4939766

May11: May T, Okabe S (2011). "Enterobactin is required for biofilm development in reduced-genome Escherichia coli." Environ Microbiol 13(12);3149-62. PMID: 21980953

Nahlik87: Nahlik MS, Fleming TP, McIntosh MA (1987). "Cluster of genes controlling synthesis and activation of 2,3-dihydroxybenzoic acid in production of enterobactin in Escherichia coli." J Bacteriol 1987;169(9);4163-70. PMID: 3040680

Pettis87: Pettis GS, McIntosh MA (1987). "Molecular characterization of the Escherichia coli enterobactin cistron entF and coupled expression of entF and the fes gene." J Bacteriol 1987;169(9);4154-62. PMID: 3040679

Reichert92: Reichert J, Sakaitani M, Walsh CT (1992). "Characterization of EntF as a serine-activating enzyme." Protein Sci 1992;1(4);549-56. PMID: 1338974

Rusnak89: Rusnak F, Faraci WS, Walsh CT (1989). "Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product." Biochemistry 1989;28(17);6827-35. PMID: 2531000

Rusnak90: Rusnak F, Liu J, Quinn N, Berchtold GA, Walsh CT (1990). "Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase." Biochemistry 1990;29(6);1425-35. PMID: 2139796

Rusnak91: Rusnak F, Sakaitani M, Drueckhammer D, Reichert J, Walsh CT (1991). "Biosynthesis of the Escherichia coli siderophore enterobactin: sequence of the entF gene, expression and purification of EntF, and analysis of covalent phosphopantetheine." Biochemistry 1991;30(11);2916-27. PMID: 1826089

Sikora09: Sikora AL, Cahill SM, Blanchard JS (2009). "Enterobactin synthetase-catalyzed formation of P(1),P(3)-diadenosine-5'-tetraphosphate." Biochemistry 48(46);10827-9. PMID: 19852513

Sikora10: Sikora AL, Wilson DJ, Aldrich CC, Blanchard JS (2010). "Kinetic and inhibition studies of dihydroxybenzoate-AMP ligase from Escherichia coli." Biochemistry 49(17);3648-57. PMID: 20359185

Staab90: Staab JF, Earhart CF (1990). "EntG activity of Escherichia coli enterobactin synthetase." J Bacteriol 1990;172(11);6403-10. PMID: 2172214

Sugihara10: Sugihara S, Orikasa Y, Okuyama H (2010). "The Escherichia coli highly expressed entD gene complements the pfaE deficiency in a pfa gene clone responsible for the biosynthesis of long-chain n-3 polyunsaturated fatty acids." FEMS Microbiol Lett 307(2);207-11. PMID: 20636978

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, biocyc12.