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

Escherichia coli K-12 substr. MG1655 Enzyme: lipoamide dehydrogenase



Gene: lpd Accession Numbers: EG10543 (EcoCyc), b0116, ECK0115

Synonyms: dhl, lpdA, E3 subunit

Regulation Summary Diagram: ?

Component of:
2-oxoglutarate dehydrogenase complex (summary available)
glycine cleavage system (extended summary available)
pyruvate dehydrogenase (extended summary available)

Subunit composition of lipoamide dehydrogenase = [Lpd]2
         E3 monomer = Lpd

Summary:
Lipoamide dehydrogenase is the E3 component of three multicomponent enzyme complexes: pyruvate dehydrogenase, 2-oxoglutarate dehydrogenase complex, and the glycine cleavage system [Pettit67, Guest72, Steiert90]. It catalyzes the transfer of electrons to the ultimate acceptor, NAD.

Kinetics of the reaction have been studied and suggest a modified ping-pong mechanism [Wilkinson81]. Site-directed mutagenesis was used to identify and characterize the redox-active disulfide [Hopkins95, Hopkins95a] and a charged residue influencing the redox potential of the FAD cofactor [MaedaYorita94]. The insertion of the FAD cofactor is essential for dimerization and full activity [Lindsay00].

An lpd null mutant produces more pyruvate and L-glutamate under aerobic conditions. Metabolic flux analysis shows that the Entner-Doudoroff pathway I and the glyoxylate shunt are activated [Li06].

Another dihydrolipoate dehydrogenase activity has been detected in E. coli lpd mutants; thus, an isozyme may exist [Richarme89].

A mutation in the lpd gene in E. coli causes the pyruvate dehydrogenase complex to be less sensitive to NADH inhibition and active during anaerobic growth [Kim08c]. Amino acid substitutions at Glu354 that lowered the sensitivity of the enzyme to NADH inhibition were proposed to act by restricting the movement of NADH [Sun12a].

Suppressor mutations in lpd have been shown to restore growth to a redox-defective mutant that lacks both the thioredoxin and glutathione/glutaredoxin reduction pathways. The suppressor mutations reduced Lpd activity resulting in dihydrolipoamide accumulation, which could then serve as an electron donor via reduction of glutaredoxins. The reoxidation of Lpd restored TCA cycle function [Feeney11].

lpd shows differential codon adaptation, resulting in differential translation efficiency signatures, in aerotolerant compared to obligate anaerobic microbes. It was therefore predicted to play a role in the oxidative stress response. An lpd deletion mutant was shown to be more sensitive than wild-type specifically to hydrogen peroxide exposure, but not other stresses [Krisko14].

Reviews: [Carothers89, Reed01, Perham02], Stauffer, G.V. (2004) "Regulation of Serine, Glycine, and One-Carbon Biosynthesis" EcoSal 3.6.1.2 [ECOSAL]

Lpd: "lipoamide dehydrogenase" [Guest72]

Dhl: "dihydrolipoyl dehydrogenase" [Alwine73]

Gene Citations: [Cunningham98]

Locations: inner membrane, cytosol

Map Position: [127,912 -> 129,336] (2.76 centisomes)
Length: 1425 bp / 474 aa

Molecular Weight of Polypeptide: 50.688 kD (from nucleotide sequence), 56 kD (experimental) [Coggins76 ]

Molecular Weight of Multimer: 115 kD (experimental) [Coggins76]

pI: 6.12

Unification Links: ASAP:ABE-0000404 , CGSC:544 , EchoBASE:EB0538 , EcoGene:EG10543 , EcoliWiki:b0116 , EcoO157Cyc:LPDA , Entrez-gene:944854 , Mint:MINT-1242510 , ModBase:P0A9P0 , OU-Microarray:b0116 , PortEco:lpd , PR:PRO_000023109 , Pride:P0A9P0 , Protein Model Portal:P0A9P0 , RefSeq:NP_414658 , RegulonDB:EG10543 , SMR:P0A9P0 , String:511145.b0116 , Swiss-Model:P0A9P0 , UniProt:P0A9P0

Relationship Links: InterPro:IN-FAMILY:IPR001327 , InterPro:IN-FAMILY:IPR004099 , InterPro:IN-FAMILY:IPR006258 , InterPro:IN-FAMILY:IPR012999 , InterPro:IN-FAMILY:IPR013027 , InterPro:IN-FAMILY:IPR016156 , InterPro:IN-FAMILY:IPR023753 , Panther:IN-FAMILY:PTHR22912:SF20 , PDB:Structure:4JDR , Pfam:IN-FAMILY:PF00070 , Pfam:IN-FAMILY:PF02852 , Pfam:IN-FAMILY:PF07992 , Prints:IN-FAMILY:PR00368 , Prosite:IN-FAMILY:PS00076

In Paralogous Gene Group: 40 (11 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006090 - pyruvate metabolic process Inferred from experiment [Smith83, Alwine73]
GO:0006103 - 2-oxoglutarate metabolic process Inferred from experiment [Smith83, Alwine73]
GO:0006979 - response to oxidative stress Inferred from experiment [Krisko14]
GO:0019464 - glycine decarboxylation via glycine cleavage system Inferred from experiment [Steiert90]
GO:0055114 - oxidation-reduction process Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01a, Allison88]
GO:0006096 - glycolytic process Inferred by computational analysis [UniProtGOA11]
GO:0045454 - cell redox homeostasis Inferred by computational analysis [GOA01a]
Molecular Function: GO:0004148 - dihydrolipoyl dehydrogenase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Allison88]
GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Arifuzzaman06, Lasserre06, Butland05]
GO:0008270 - zinc ion binding Inferred from experiment [Katayama02]
GO:0015036 - disulfide oxidoreductase activity Inferred from experiment [Williams67]
GO:0042802 - identical protein binding Inferred from experiment [Lasserre06]
GO:0050660 - flavin adenine dinucleotide binding Inferred from experiment Inferred by computational analysis [GOA01a, Williams67]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0016668 - oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Williams67, Lasserre06]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Lasserre06]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]
GO:0005960 - glycine cleavage complex
GO:0045248 - cytosolic oxoglutarate dehydrogenase complex
GO:0045250 - cytosolic pyruvate dehydrogenase complex

MultiFun Terms: metabolism carbon utilization amino acids
metabolism carbon utilization carbon compounds
metabolism central intermediary metabolism formyl-THF biosynthesis
metabolism energy metabolism, carbon pyruvate dehydrogenase

Essentiality data for lpd knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
No [Feist07, Comment 4]

Credits:
Curated 13-Feb-2007 by Keseler I , SRI International
Last-Curated ? 25-Jun-2012 by Fulcher C , SRI International


Enzymatic reaction of: protein N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase (lipoamide dehydrogenase)

EC Number: 1.8.1.4

a [lipoyl-carrier protein] N6-dihydrolipoyl-L-lysine + NAD+ <=> a [lipoyl-carrier protein] N6-lipoyl-L-lysine + NADH + H+

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

Reversibility of this reaction is unspecified.


Enzymatic reaction of: H-Gcv-protein-(dihydrolipoyl)lysine:NAD+ oxidoreductase (lipoamide dehydrogenase)

EC Number: 1.8.1.4

a [glycine-cleavage complex H protein] N6-dihydrolipoyl-L-lysine + NAD+ <=> a [glycine-cleavage complex H protein] N6-lipoyl-L-lysine + NADH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

In Pathways: glycine cleavage


Enzymatic reaction of: lipoate acetyltransferase N6-(dihydrolipoyl)lysine:NAD+ oxidoreductase (lipoamide dehydrogenase)

EC Number: 1.8.1.4

a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ <=> a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + 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.

Alternative Substrates for a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine: dihydrolipoamide [Sahlman89 ]

In Pathways: pyruvate decarboxylation to acetyl CoA

Summary:
NADH acts both as a product inhibitor and by reducing a fraction of the enzyme to a catalytically inactive state [Sahlman89].

Enzymatic activity of lipoamide dehydrogenase is generally measured using dihydrolipoamide as the substrate.

Cofactors or Prosthetic Groups: FAD [Koike63]

Inhibitors (Unknown Mechanism): NADH [SchminckeOtt81, McGarry68]

Primary Physiological Regulators of Enzyme Activity: NADH

Kinetic Parameters:

Substrate
Km (μM)
Citations
NAD+
950.0
[Sahlman89]

pH(opt): 7.9 [Wilkinson81]


Enzymatic reaction of: dihydrolipoate dehydrogenase (lipoamide dehydrogenase)

Synonyms: E3 component of 2-oxoglutarate dehydrogenase complex

EC Number: 1.8.1.4

a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ <=> a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + 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: 2-oxoglutarate decarboxylation to succinyl-CoA

Cofactors or Prosthetic Groups: FAD [Pettit67]

Inhibitors (Unknown Mechanism): NADH [Scouten71]

Kinetic Parameters:

Substrate
Km (μM)
Citations
NAD+
1820.0
[Allison88]


Subunit of: 2-oxoglutarate dehydrogenase complex

Subunit composition of 2-oxoglutarate dehydrogenase complex = [(SucA)12][(SucB)24][(Lpd)2]
         2-oxoglutarate decarboxylase, thiamine-requiring = (SucA)12 (extended summary available)
                 subunit of E1(0) component of 2-oxoglutarate dehydrogenase = SucA
         dihydrolipoyltranssuccinylase = (SucB)24 (extended summary available)
         lipoamide dehydrogenase = (Lpd)2 (extended summary available)
                 E3 monomer = Lpd

Summary:
The 2-oxoglutarate (2-ketoglutarate) dehydrogenase complex is similar in enzyme composition and complex reactions to the pyruvate dehydrogenase complex reactions [Perham87, Stephens83, Perham89] (see 2-oxoglutarate decarboxylation to succinyl-CoA and pyruvate decarboxylation to acetyl CoA).

SUBREACTIONS: E1(o) + TPP = E1(o).TPP E1(o).TPP + succinate = E1(o).hydroxycarboxypropylTPP + CO(2) E1(o).hydroxycarboxypropylTPP + E2(o).lipoate(S2) = E1(o).TPP + E2(o).lipoate(SH)(S-succinyl) E2(o).lipoate(SH)(S-succinyl) + CoA = E2(o).lip(SH)2 + succinylCoA E3 + FAD = E3.FAD E3.FAD + E2(o).lip(SH)2 = E3.FADH(2) + E2(o).lip(S)2 E3.FADH(2) + NAD(+) = E3.FAD + NADH + H(+) (see [Steginsky85, Waskiewicz84].


Enzymatic reaction of: 2-oxoglutarate dehydrogenase

Synonyms: α-ketoglutarate dehydrogenase, 2-ketoglutarate dehydrogenase

2-oxoglutarate + coenzyme A + NAD+ <=> succinyl-CoA + CO2 + NADH

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: 2-oxoglutarate decarboxylation to succinyl-CoA , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass , superpathway of glyoxylate bypass and TCA , TCA cycle I (prokaryotic)

Summary:
The [Waskiewicz84] data are for E. coli B.

Cofactors or Prosthetic Groups: thiamin diphosphate [Frank07, Waskiewicz84], FAD [Lindsay00], Mg2+ [Frank07, Waskiewicz84]


Subunit of: glycine cleavage system

Subunit composition of glycine cleavage system = [(Lpd)2][(GcvP)2][GcvH][GcvT]
         lipoamide dehydrogenase = (Lpd)2 (extended summary available)
                 E3 monomer = Lpd
         glycine decarboxylase = (GcvP)2
                 glycine decarboxylase = GcvP
         lipoyl-GcvH-protein = GcvH
         aminomethyltransferase = GcvT (summary available)

Summary:
The glycine-cleavage system (GCV) is a multienzyme complex that catalyzes the reversible oxidation of glycine, yielding carbon dioxide, ammonia, 5,10-methylenetetrahydrofolate and a reduced pyridine nucleotide. Tetrahydrofolate serves as a recipient for one-carbon units generated during glycine cleavage to form the methylene group. The GCV system consists of four protein components, the P protein, H protein, T protein, and L protein. P protein catalyzes the pyridoxal phosphate-dependent liberation of CO2 from glycine, leaving a methylamine moiety. The methylamine moiety is transferred to the lipoic acid group of the H protein, which is bound to the P protein prior to decarboxylation of glycine. The T protein catalyzes the release of NH3 from the methylamine group and transfers the remaining C1 unit to THF, forming 5,10-mTHF. The L protein then oxidizes the lipoic acid component of the H protein and transfers the electrons to NAD+, forming NADH [OkamuraIkeda93].

Mutations that result in an enzymatic deficiency in the GCV enzyme system (gcvT, gcvH, and gcvP) do not result in auxotrophy. Mutations that result in an enzymatic deficiency in both the serine pathway and the GCV enzyme system can no longer use glycine as a serine source [Plamann83a].

Mutants that overproduce the GCV enzyme complex are partial glycine auxotrophs due to rapid glycine catabolism. [Ghrist95, Heil02].

One of the four subunits, lipoamide dehydrogenase (E3), is shared with pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase [Steiert90].

This topic has been reviewed in [Kikuchi08].

Credits:
Reviewed 04-Mar-2010 by Sarker M


Enzymatic reaction of: gcv system (glycine cleavage system)

Synonyms: glycine cleavage multienzyme system

glycine + a tetrahydrofolate + NAD+ <=> a 5,10-methylene-tetrahydrofolate + ammonium + CO2 + NADH

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is favored in the direction shown.

In Pathways: glycine cleavage , N10-formyl-tetrahydrofolate biosynthesis

Summary:
This reaction represents the net reaction catalyzed by the glycine cleavage system enzyme complex.

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
a 5,10-methylene-tetrahydrofolate
67.7
14.4
[OkamuraIkeda99, BRENDA14]
a 5,10-methylene-tetrahydrofolate
88.1
18.4
[OkamuraIkeda03, BRENDA14]


Subunit of: pyruvate dehydrogenase

Subunit composition of pyruvate dehydrogenase = [(AceE)2]12[AceF]24[(Lpd)2]6
         pyruvate dehydrogenase = (AceE)2 (summary available)
                 subunit of E1p component of pyruvate dehydrogenase complex = AceE
         lipoamide dehydrogenase = (Lpd)2 (extended summary available)
                 E3 monomer = Lpd

Summary:
Pyruvate dehydrogenase is one of the most complicated enzyme systems known. The self-assembling complex is composed of multiple copies of three enzymes: E1, E2 and E3, in stoichiometry of 24:24:12, respectively (12 AceE dimers, a 24-subunit AceF core, and 6 LpdA dimers) [Reed75, Bates77, Yang85, CaJacob85, Angelides79].

AceF, the "E2" or "core" component of the pyruvate dehydrogenase multienzyme complex, assembles into a 24-subunit [Angelides79] cube [Yang85, Wagenknecht90]. The E1 dimers of the pyruvate dehydrogenase multienzyme complex catalyze acetylation of the lipoate moieties that are attached to the E2 subunits [Danson78]. The E2 subunits (AceF) also exhibit transacetylation [Stanley81]. The structure of the pyruvate dehydrogenase multienzyme complex and the spatial distribution of the E2 lipoyl moieties have been studied by scanning transmission electron microscopy [Yang94]. Electron cryotomography showed that the E1 and E3 subunits are flexibly tethered to the E2 core [Murphy05].

The E3 component is shared with 2-oxoglutarate dehydrogenase and glycine cleavage multi-enzyme complexes. E1 and E2 differ slightly between 2-oxoglutarate and pyruvate complexes, and are designated (o) and (p) to distinguish them. Substrate is channeled through the catalytic reactions by attachment in thioester linkage to lipoyl groups via so-called 'swinging arm', carrying substrate molecules to successive active sites [Perham87].

The reaction catalyzed by the pyruvate dehydrogenase multienzyme complex is the gateway to the TCA cycle, producing acetylCoA for the first reaction. In animals, the reaction is regulated by phosphorylation of the E1 component, but not in E. coli [Patel90].


Enzymatic reaction of: pyruvate dehydrogenase

Synonyms: pyruvate dehydrogenase complex, pyruvate dehydrogenase, PDH complex

EC Number: 1.2.1.-

pyruvate + coenzyme A + NAD+ <=> acetyl-CoA + CO2 + NADH

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: pyruvate decarboxylation to acetyl CoA , superpathway of glycolysis, pyruvate dehydrogenase, TCA, and glyoxylate bypass

Cofactors or Prosthetic Groups: thiamin diphosphate [Kale07], FAD [Lindsay00], Mg2+ [Kale07]

Inhibitors (Competitive): fluoropyruvate [Saumweber81] , hydroxypyruvate [Bisswanger81] , 2-oxobutanoate [Saumweber81, Bisswanger81] , glyoxylate [Bisswanger81] , 3-bromopyruvate [Bisswanger81]

Inhibitors (Unknown Mechanism): NADH [Sun12a] , tellurite [Contreras10] , tetrahydro-TPP [Williams90, Helmward89] , thiamine thiothiazolone pyrophosphate [Williams90, Helmward89] , NAD+ [Graham89, Comment 5] , pyruvate [Helmward89, Williams90]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Link97, UniProt11]
UniProt: Removed.
Chain 2 -> 474
[UniProt09]
UniProt: Dihydrolipoyl dehydrogenase;
Nucleotide-Phosphate-Binding-Region 36 -> 45
[UniProt10a]
UniProt: FAD; Non-Experimental Qualifier: by similarity;
Disulfide-Bond-Site 50, 45
[UniProt10a]
UniProt: Redox-active; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 54
[UniProt10a]
UniProt: FAD; Non-Experimental Qualifier: by similarity;
Acetylation-Modification 111
[Yu08]
 
Amino-Acid-Sites-That-Bind 117
[UniProt10a]
UniProt: FAD; via amide nitrogen and carbonyl oxygen; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 182 -> 186
[UniProt10a]
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 205
[UniProt10a]
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Acetylation-Modification 220
[Zhang09, UniProt11]
UniProt: N6-acetyllysine.
Amino-Acid-Sites-That-Bind 238
[UniProt10a]
UniProt: NAD; via amide nitrogen; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 270 -> 273
[UniProt10a]
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Acetylation-Modification 299
[Yu08]
 
Amino-Acid-Sites-That-Bind 313
[UniProt10a]
UniProt: FAD; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 321
[UniProt10a]
UniProt: FAD; via amide nitrogen; Non-Experimental Qualifier: by similarity;
Active-Site 445
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0116 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10543; confirmed by SwissProt match.


References

Allison88: Allison N, Williams CH, Guest JR (1988). "Overexpression and mutagenesis of the lipoamide dehydrogenase of Escherichia coli." Biochem J 256(3);741-9. PMID: 3066354

Alwine73: Alwine JC, Russell RM, Murray KN (1973). "Characterization of an Escherichia coli mutant deficient in dihydrolipoyl dehydrogenase activity." J Bacteriol 115(1);1-8. PMID: 4197899

Angelides79: Angelides KJ, Akiyama SK, Hammes GG (1979). "Subunit stoichiometry and molecular weight of the pyruvate dehydrogenase multienzyme complex from Escherichia coli." Proc Natl Acad Sci U S A 1979;76(7);3279-83. PMID: 386335

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

Bates77: Bates DL, Danson MJ, Hale G, Hooper EA, Perham RN (1977). "Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli." Nature 268(5618);313-6. PMID: 329143

Bisswanger81: Bisswanger H (1981). "Substrate specificity of the pyruvate dehydrogenase complex from Escherichia coli." J Biol Chem 256(2);815-22. PMID: 7005225

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

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

CaJacob85: CaJacob CA, Frey PA, Hainfeld JF, Wall JS, Yang H (1985). "Escherichia coli pyruvate dehydrogenase complex: particle masses of the complex and component enzymes measured by scanning transmission electron microscopy." Biochemistry 1985;24(10);2425-31. PMID: 3925985

Carothers89: Carothers DJ, Pons G, Patel MS (1989). "Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases." Arch Biochem Biophys 1989;268(2);409-25. PMID: 2643922

Coggins76: Coggins JR, Hooper EA, Perham RN (1976). "Use of dimethyl suberimidate and novel periodate-cleavable bis(imido esters) to study the quaternary structure of the pyruvate dehydrogenase multienzyme complex of Escherichia coli." Biochemistry 15(12);2527-33. PMID: 779824

Contreras10: Contreras Ndel P, Vasquez CC (2010). "Tellurite-induced carbonylation of the Escherichia coli pyruvate dehydrogenase multienzyme complex." Arch Microbiol 192(11);969-73. PMID: 20821193

Cunningham98: Cunningham L, Guest JR (1998). "Transcription and transcript processing in the sdhCDAB-sucABCD operon of Escherichia coli." Microbiology 144 ( Pt 8);2113-23. PMID: 9720032

Danson78: Danson MJ, Hooper EA, Perham RN (1978). "Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complex of Escherichia coli." Biochem J 175(1);193-8. PMID: 367364

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

ECOSAL: "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition.

Feeney11: Feeney MA, Veeravalli K, Boyd D, Gon S, Faulkner MJ, Georgiou G, Beckwith J (2011). "Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli." Proc Natl Acad Sci U S A 108(19);7991-6. PMID: 21521794

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Frank07: Frank RA, Price AJ, Northrop FD, Perham RN, Luisi BF (2007). "Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex." J Mol Biol 368(3);639-51. PMID: 17367808

Ghrist95: Ghrist AC, Stauffer GV (1995). "Characterization of the Escherichia coli gcvR gene encoding a negative regulator of gcv expression." J Bacteriol 177(17);4980-4. PMID: 7665475

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."

Graham89: Graham LD, Packman LC, Perham RN (1989). "Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes." Biochemistry 1989;28(4);1574-81. PMID: 2655695

Guest72: Guest JR, Creaghan IT (1972). "Lipoamide dehydrogenase mutants of Escherichia coli K 12." Biochem J 130(1);8P. PMID: 4570348

Heil02: Heil G, Stauffer LT, Stauffer GV (2002). "Glycine binds the transcriptional accessory protein GcvR to disrupt a GcvA/GcvR interaction and allow GcvA-mediated activation of the Escherichia coli gcvTHP operon." Microbiology 148(Pt 7);2203-14. PMID: 12101307

Helmward89: Helmward Z "Handbook of Enzyme Inhibitors. 2nd, revised and enlarged edition." Weinheim, Federal Republic of Germany ; New York, NY, USA , 1989.

Hopkins95: Hopkins N, Williams CH (1995). "Characterization of lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S." Biochemistry 34(37);11757-65. PMID: 7547908

Hopkins95a: Hopkins N, Williams CH (1995). "Lipoamide dehydrogenase from Escherichia coli lacking the redox active disulfide: C44S and C49S. Redox properties of the FAD and interactions with pyridine nucleotides." Biochemistry 34(37);11766-76. PMID: 7547909

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

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kale07: Kale S, Arjunan P, Furey W, Jordan F (2007). "A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component." J Biol Chem 282(38);28106-16. PMID: 17635929

Katayama02: Katayama A, Tsujii A, Wada A, Nishino T, Ishihama A (2002). "Systematic search for zinc-binding proteins in Escherichia coli." Eur J Biochem 269(9);2403-13. PMID: 11985624

Kikuchi08: Kikuchi G, Motokawa Y, Yoshida T, Hiraga K (2008). "Glycine cleavage system: reaction mechanism, physiological significance, and hyperglycinemia." Proc Jpn Acad Ser B Phys Biol Sci 84(7);246-63. PMID: 18941301

Kim08c: Kim Y, Ingram LO, Shanmugam KT (2008). "Dihydrolipoamide dehydrogenase mutation alters the NADH sensitivity of pyruvate dehydrogenase complex of Escherichia coli K-12." J Bacteriol 190(11);3851-8. PMID: 18375566

Koike63: Koike M, Reed LJ, Carroll WR (1963). "alpha-Keto acid dehydrogenation complexes. IV. Resolution and reconstitution of the Escherichia coli pyruvate dehydrogenation complex." J Biol Chem 238;30-9. PMID: 14034257

Krisko14: Krisko A, Copi T, Gabaldon T, Lehner B, Supek F (2014). "Inferring gene function from evolutionary change in signatures of translation efficiency." Genome Biol 15(3);R44. PMID: 24580753

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

Li06: Li M, Ho PY, Yao S, Shimizu K (2006). "Effect of lpdA gene knockout on the metabolism in Escherichia coli based on enzyme activities, intracellular metabolite concentrations and metabolic flux analysis by 13C-labeling experiments." J Biotechnol 122(2);254-66. PMID: 16310273

Lindsay00: Lindsay H, Beaumont E, Richards SD, Kelly SM, Sanderson SJ, Price NC, Lindsay JG (2000). "FAD insertion is essential for attaining the assembly competence of the dihydrolipoamide dehydrogenase (E3) monomer from Escherichia coli." J Biol Chem 275(47);36665-70. PMID: 10970889

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

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

MaedaYorita94: Maeda-Yorita K, Russell GC, Guest JR, Massey V, Williams CH (1994). "Modulation of the oxidation-reduction potential of the flavin in lipoamide dehydrogenase from Escherichia coli by alteration of a nearby charged residue, K53R." Biochemistry 33(20);6213-20. PMID: 8193135

McGarry68: McGarry JD (1968). "A comparative study of the reversibility of the reaction catalysed by bacterial lipoamide dehydrogenase." Biochim Biophys Acta 159(1);9-18. PMID: 4384985

Murphy05: Murphy GE, Jensen GJ (2005). "Electron cryotomography of the E. coli pyruvate and 2-oxoglutarate dehydrogenase complexes." Structure 13(12);1765-73. PMID: 16338405

OkamuraIkeda03: Okamura-Ikeda K, Kameoka N, Fujiwara K, Motokawa Y (2003). "Probing the H-protein-induced conformational change and the function of the N-terminal region of Escherichia coli T-protein of the glycine cleavage system by limited proteolysis." J Biol Chem 278(12);10067-72. PMID: 12531904

OkamuraIkeda93: Okamura-Ikeda K, Ohmura Y, Fujiwara K, Motokawa Y (1993). "Cloning and nucleotide sequence of the gcv operon encoding the Escherichia coli glycine-cleavage system." Eur J Biochem 1993;216(2);539-48. PMID: 8375392

OkamuraIkeda99: Okamura-Ikeda K, Fujiwara K, Motokawa Y (1999). "Identification of the folate binding sites on the Escherichia coli T-protein of the glycine cleavage system." J Biol Chem 274(25);17471-7. PMID: 10364177

Patel90: Patel MS, Roche TE (1990). "Molecular biology and biochemistry of pyruvate dehydrogenase complexes." FASEB J 1990;4(14);3224-33. PMID: 2227213

Patrick07: Patrick WM, Quandt EM, Swartzlander DB, Matsumura I (2007). "Multicopy suppression underpins metabolic evolvability." Mol Biol Evol 24(12);2716-22. PMID: 17884825

Perham02: Perham RN, Jones DD, Chauhan HJ, Howard MJ (2002). "Substrate channelling in 2-oxo acid dehydrogenase multienzyme complexes." Biochem Soc Trans 30(2);47-51. PMID: 12023822

Perham87: Perham RN, Packman LC, Radford SE (1987). "2-Oxo acid dehydrogenase multi-enzyme complexes: in the beginning and halfway there." Biochem Soc Symp 1987;54;67-81. PMID: 3332999

Perham89: Perham RN, Packman LC (1989). "2-Oxo acid dehydrogenase multienzyme complexes: domains, dynamics, and design." Ann N Y Acad Sci 1989;573;1-20. PMID: 2699393

Pettit67: Pettit FH, Reed LJ (1967). "Alpha-keto acid dehydrogenase complexes. 8. Comparison of dihydrolipoyl dehydrogenases from pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli." Proc Natl Acad Sci U S A 58(3);1126-30. PMID: 4964085

Pettit73: Pettit FH, Hamilton L, Munk P, Namihira G, Eley MH, Willms CR, Reed LJ (1973). "Alpha-keto acid dehydrogenase complexes. XIX. Subunit structure of the Escherichia coli alpha-ketoglutarate dehydrogenase complex." J Biol Chem 248(15);5282-90. PMID: 4588679

Plamann83a: Plamann MD, Rapp WD, Stauffer GV (1983). "Escherichia coli K12 mutants defective in the glycine cleavage enzyme system." Mol Gen Genet 192(1-2);15-20. PMID: 6358793

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Reed01: Reed LJ (2001). "A trail of research from lipoic acid to alpha-keto acid dehydrogenase complexes." J Biol Chem 276(42);38329-36. PMID: 11477096

Reed75: Reed LJ, Pettit FH, Eley MH, Hamilton L, Collins JH, Oliver RM (1975). "Reconstitution of the Escherichia coli pyruvate dehydrogenase complex." Proc Natl Acad Sci U S A 1975;72(8);3068-72. PMID: 1103138

Richarme89: Richarme G (1989). "Purification of a new dihydrolipoamide dehydrogenase from Escherichia coli." J Bacteriol 1989;171(12);6580-5. PMID: 2687245

Russell92a: Russell GC, Machado RS, Guest JR (1992). "Overproduction of the pyruvate dehydrogenase multienzyme complex of Escherichia coli and site-directed substitutions in the E1p and E2p subunits." Biochem J 1992;287 ( Pt 2);611-9. PMID: 1445221

Sahlman89: Sahlman L, Williams CH (1989). "Lipoamide dehydrogenase from Escherichia coli. Steady-state kinetics of the physiological reaction." J Biol Chem 264(14);8039-45. PMID: 2498307

Saumweber81: Saumweber H, Binder R, Bisswanger H (1981). "Pyruvate dehydrogenase component of the pyruvate dehydrogenase complex from Escherichia coli K12. Purification and characterization." Eur J Biochem 1981;114(2);407-11. PMID: 7011811

SchminckeOtt81: Schmincke-Ott E, Bisswanger H (1981). "Dihydrolipoamide dehydrogenase component of the pyruvate dehydrogenase complex from Escherichia coli K12. Comparative characterization of the free and the complex-bound component." Eur J Biochem 114(2);413-20. PMID: 7011812

Scouten71: Scouten WH, McManus IR (1971). "Microbial lipoamide dehydrogenase. Purification and some characteristics of the enzyme derived from selected microorganisms." Biochim Biophys Acta 227(2);248-63. PMID: 4323856

Smith83: Smith MW, Neidhardt FC (1983). "2-Oxoacid dehydrogenase complexes of Escherichia coli: cellular amounts and patterns of synthesis." J Bacteriol 156(1);81-8. PMID: 6311808

Stanley81: Stanley CJ, Packman LC, Danson MJ, Henderson CE, Perham RN (1981). "Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complexes from bacterial and mammalian sources." Biochem J 195(3);715-21. PMID: 7032507

Steginsky85: Steginsky CA, Gruys KJ, Frey PA (1985). "alpha-Ketoglutarate dehydrogenase complex of Escherichia coli. A hybrid complex containing pyruvate dehydrogenase subunits from pyruvate dehydrogenase complex." J Biol Chem 260(25);13690-3. PMID: 3902822

Steiert90: Steiert PS, Stauffer LT, Stauffer GV (1990). "The lpd gene product functions as the L protein in the Escherichia coli glycine cleavage enzyme system." J Bacteriol 172(10);6142-4. PMID: 2211531

Stephens83: Stephens PE, Darlison MG, Lewis HM, Guest JR (1983). "The pyruvate dehydrogenase complex of Escherichia coli K12. Nucleotide sequence encoding the dihydrolipoamide acetyltransferase component." Eur J Biochem 1983;133(3);481-9. PMID: 6345153

Sun12a: Sun Z, Do PM, Rhee MS, Govindasamy L, Wang Q, Ingram LO, Shanmugam KT (2012). "Amino acid substitutions at glutamate-354 in dihydrolipoamide dehydrogenase of Escherichia coli lower the sensitivity of pyruvate dehydrogenase to NADH." Microbiology 158(Pt 5);1350-8. PMID: 22343352

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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

Wagenknecht90: Wagenknecht T, Grassucci R, Schaak D (1990). "Cryoelectron microscopy of frozen-hydrated alpha-ketoacid dehydrogenase complexes from Escherichia coli." J Biol Chem 265(36);22402-8. PMID: 2266132

Waskiewicz84: Waskiewicz DE, Hammes GG (1984). "Elementary steps in the reaction mechanism of the alpha-ketoglutarate dehydrogenase multienzyme complex from Escherichia coli: kinetics of succinylation and desuccinylation." Biochemistry 23(14);3136-43. PMID: 6380583

Wei03: Wei W, Li H, Nemeria N, Jordan F (2003). "Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase." Protein Expr Purif 28(1);140-50. PMID: 12651118

Wilkinson81: Wilkinson KD, Williams CH (1981). "NADH inhibition and NAD activation of Escherichia coli lipoamide dehydrogenase catalyzing the NADH-lipoamide reaction." J Biol Chem 256(5);2307-14. PMID: 7007381

Williams67: Williams CH, Zanetti G, Arscott LD, McAllister JK (1967). "Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and thioredoxin." J Biol Chem 242(22);5226-31. PMID: 4863745

Williams90: Williams KP, Leadlay PF, Lowe PN (1990). "Inhibition of pyruvate:ferredoxin oxidoreductase from Trichomonas vaginalis by pyruvate and its analogues. Comparison with the pyruvate decarboxylase component of the pyruvate dehydrogenase complex." Biochem J 1990;268(1);69-75. PMID: 2188649

Yang85: Yang HC, Hainfeld JF, Wall JS, Frey PA (1985). "Quaternary structure of pyruvate dehydrogenase complex from Escherichia coli." J Biol Chem 1985;260(30);16049-51. PMID: 3905803

Yang94: Yang YS, Datta A, Hainfeld JF, Furuya FR, Wall JS, Frey PA (1994). "Mapping the lipoyl groups of the pyruvate dehydrogenase complex by use of gold cluster labels and scanning transmission electron microscopy." Biochemistry 33(32);9428-37. PMID: 7520749

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508

Zhang09: Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8(2);215-25. PMID: 18723842

Other References Related to Gene Regulation

Constantinidou06: Constantinidou C, Hobman JL, Griffiths L, Patel MD, Penn CW, Cole JA, Overton TW (2006). "A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth." J Biol Chem 281(8);4802-15. PMID: 16377617

Cunningham98a: Cunningham L, Georgellis D, Green J, Guest JR (1998). "Co-regulation of lipoamide dehydrogenase and 2-oxoglutarate dehydrogenase synthesis in Escherichia coli: characterisation of an ArcA binding site in the lpd promoter." FEMS Microbiol Lett 1998;169(2);403-8. PMID: 9868788

Gohler11: Gohler AK, Kokpinar O, Schmidt-Heck W, Geffers R, Guthke R, Rinas U, Schuster S, Jahreis K, Kaleta C (2011). "More than just a metabolic regulator - elucidation and validation of new targets of PdhR in Escherichia coli." BMC Syst Biol 5(1);197. PMID: 22168595

Kumar11: Kumar R, Shimizu K (2011). "Transcriptional regulation of main metabolic pathways of cyoA, cydB, fnr, and fur gene knockout Escherichia coli in C-limited and N-limited aerobic continuous cultures." Microb Cell Fact 10;3. PMID: 21272324

Liu04: Liu X, De Wulf P (2004). "Probing the ArcA-P modulon of Escherichia coli by whole genome transcriptional analysis and sequence recognition profiling." J Biol Chem 279(13);12588-97. PMID: 14711822

Ogasawara07a: Ogasawara H, Ishida Y, Yamada K, Yamamoto K, Ishihama A (2007). "PdhR (pyruvate dehydrogenase complex regulator) controls the respiratory electron transport system in Escherichia coli." J Bacteriol 189(15);5534-41. PMID: 17513468

Olvera09: Olvera L, Mendoza-Vargas A, Flores N, Olvera M, Sigala JC, Gosset G, Morett E, Bolivar F (2009). "Transcription analysis of central metabolism genes in Escherichia coli. Possible roles of sigma38 in their expression, as a response to carbon limitation." PLoS One 4(10);e7466. PMID: 19838295

Quail94: Quail MA, Haydon DJ, Guest JR (1994). "The pdhR-aceEF-lpd operon of Escherichia coli expresses the pyruvate dehydrogenase complex." Mol Microbiol 12(1);95-104. PMID: 8057842

Quail95: Quail MA, Guest JR (1995). "Purification, characterization and mode of action of PdhR, the transcriptional repressor of the pdhR-aceEF-lpd operon of Escherichia coli." Mol Microbiol 1995;15(3);519-29. PMID: 7783622

Salmon03: Salmon K, Hung SP, Mekjian K, Baldi P, Hatfield GW, Gunsalus RP (2003). "Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR." J Biol Chem 278(32);29837-55. PMID: 12754220

Salmon05: Salmon KA, Hung SP, Steffen NR, Krupp R, Baldi P, Hatfield GW, Gunsalus RP (2005). "Global gene expression profiling in Escherichia coli K12: effects of oxygen availability and ArcA." J Biol Chem 280(15);15084-96. PMID: 15699038

Sarkar08: Sarkar D, Siddiquee KA, Arauzo-Bravo MJ, Oba T, Shimizu K (2008). "Effect of cra gene knockout together with edd and iclR genes knockout on the metabolism in Escherichia coli." Arch Microbiol 190(5);559-71. PMID: 18648770

Shimada11: Shimada T, Yamamoto K, Ishihama A (2011). "Novel Members of the Cra Regulon Involved in Carbon Metabolism in Escherichia coli." J Bacteriol 193(3);649-59. PMID: 21115656

Spencer85: Spencer ME, Guest JR (1985). "Transcription analysis of the sucAB, aceEF and lpd genes of Escherichia coli." Mol Gen Genet 1985;200(1);145-54. PMID: 3897791

Trotter11: Trotter EW, Rolfe MD, Hounslow AM, Craven CJ, Williamson MP, Sanguinetti G, Poole RK, Green J (2011). "Reprogramming of Escherichia coli K-12 metabolism during the initial phase of transition from an anaerobic to a micro-aerobic environment." PLoS One 6(9);e25501. PMID: 21980479

Zhang05: Zhang Z, Gosset G, Barabote R, Gonzalez CS, Cuevas WA, Saier MH (2005). "Functional interactions between the carbon and iron utilization regulators, Crp and Fur, in Escherichia coli." J Bacteriol 187(3);980-90. PMID: 15659676


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, BIOCYC13B.