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MetaCyc Protein: lipoamide dehydrogenase

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

Synonyms: dhl, lpdA, E3 subunit

Component of:
glycine cleavage system (extended summary available)
2-oxoglutarate dehydrogenase complex (summary available)
pyruvatedeh-cplx (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: pyruvatedeh-cplx, 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 [Li06a].

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 [Kim08a]. 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 [Sun12].

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]

Locations: plasma membrane, cytoplasm, cytosol

Map Position: [127,912 -> 129,336]

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 , DIP:DIP-6854N , 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

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reactions of [a [lipoyl-carrier protein] N6-dihydrolipoyl-L-lysine + NAD+ → a [lipoyl-carrier protein] N6-lipoyl-L-lysine + NADH + H+] (1.8.1.4):
i1: an [apo BCAA dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ ↔ an [apo BCAA dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+ (1.8.1.4)

i2: a [glycine-cleavage complex H protein] N6-dihydrolipoyl-L-lysine + NAD+ ↔ a [glycine-cleavage complex H protein] N6-lipoyl-L-lysine + NADH + H+ (1.8.1.4)

i3: a [2-oxoglutarate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ ↔ a [2-oxoglutarate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+ (1.8.1.4)

i4: a [pyruvate dehydrogenase E2 protein] N6-dihydrolipoyl-L-lysine + NAD+ ↔ a [pyruvate dehydrogenase E2 protein] N6-lipoyl-L-lysine + NADH + H+ (1.8.1.4)

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 [UniProtGOA11a, GOA01a, Allison88]
GO:0006096 - glycolytic process Inferred by computational analysis [UniProtGOA11a]
GO:0045454 - cell redox homeostasis Inferred by computational analysis [GOA01a]
GO:0050787 - detoxification of mercury ion 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:0016152 - mercury (II) reductase activity Inferred by computational analysis [GOA01a]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016668 - oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor Inferred by computational analysis [GOA01a]
GO:0045340 - mercury ion binding Inferred by computational analysis [GOA01a]
GO:0050661 - NADP binding Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, 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 [UniProtGOA11a, Lasserre06]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
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

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Subunit of: glycine cleavage system

Species: Escherichia coli K-12 substr. MG1655

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 in EcoCyc 04-Mar-2010 by Sarker M
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


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.

This reaction is reversible.

In Pathways: glycine cleavage , folate transformations I , N10-formyl-tetrahydrofolate biosynthesis

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International

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
0.21
[OkamuraIkeda99a, BRENDA14]
a 5,10-methylene-tetrahydrofolate
88.1
18.4
0.21
[OkamuraIkeda03, BRENDA14]


Subunit of: 2-oxoglutarate dehydrogenase complex

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of 2-oxoglutarate dehydrogenase complex = [(Lpd)2][(SucA)12][(SucB)24]
         lipoamide dehydrogenase = (Lpd)2 (extended summary available)
                 E3 monomer = Lpd
         2-oxoglutarate decarboxylase, thiamine-requiring = (SucA)12 (extended summary available)
                 subunit of E1(0) component of 2-oxoglutarate dehydrogenase = SucA
         e2o = (SucB)24 (extended summary available)

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].

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


Subunit of: pyruvatedeh-cplx

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

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].

Credits:
Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International


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 45, 50
[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;

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

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

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

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: 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

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."

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

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

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

Kim08a: 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

Krisko14: Kri Ko 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

Li06a: 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

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

OkamuraIkeda99a: 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

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

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

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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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