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Escherichia coli K-12 substr. MG1655 Enzyme: aldehyde-alcohol dehydrogenase



Gene: adhE Accession Numbers: EG10031 (EcoCyc), b1241, ECK1235

Synonyms: adhC, ana, pyruvate-formate-lyase deactivase

Regulation Summary Diagram: ?

Subunit composition of aldehyde-alcohol dehydrogenase = [AdhE]40

Summary:
AdhE is a homopolymeric protein with three Fe2+-dependent catalytic functions: alcohol dehydrogenase, coenzyme A-dependent acetaldehyde dehydrogenase, and pyruvate formate-lyase deactivase. However, the existence of the pyruvate formate-lyase deactivase activity of AdhE described by [Kessler91, Kessler92] has been questioned. [Nnyepi07] were unable to reproduce the AdhE deactivase activity and they noted that small molecule thiols can effect deactivation. The homopolymeric structure of AdhE is unusual in that 20-60 subunits are helically arranged to form rod-like ultrastructures [Kessler92].

Under fermentative conditions AdhE catalyzes the reduction of acetyl-CoA to acetaldehyde and the latter compound to ethanol (see pathway mixed acid fermentation). Aerobically, in the reverse direction, AdhE can catalyze the oxidation of acetaldehyde to acetyl-CoA (see pathways ethanol degradation I and threonine degradation IV). Although E. coli cannot grow aerobically using ethanol as sole carbon and energy source due to the low transcription rate of AdhE and its sensitivity to metal ion-catalyzed oxidation, mutants can be selected that have the ability to grow on ethanol [MembrilloHernan00].

Expression of adhE appears to be regulated at the transcriptional [Chen91, Leonardo96, Mikulskis97] and translational [Aristarkhov96, Kaga02] levels, and possibly at the posttranslational level [HollandStaley00]. Expression of adhE is approximately 10-fold higher during anaerobic growth than during aerobic growth [MembrilloHernan99a]. Its aerobic role is uncertain, but it may protect against oxidative stress [Echave03]. Under aerobic conditions AdhE may be protected against thermal and oxidative inactivation by the heat shock proteins IbpA and IbpB [Matuszewska09].

The AdhE from E. coli B was partially purified and characterized in early work [Rudolph68]. It was later purified to homogeneity from E. coli B and its coenzyme A-linked aldehyde dehydrogenase activity was subjected to detailed kinetic analysis. A bi-uni-uni-uni ping-pong mechanism was proposed [Shone81]. AdhE from Salmonella enterica subsp. enterica serovar Typhimurium showed 70% amino acid sequence identity to that of E. coli. It had a lower Km for alcohol substrates and some differences in substrate specificity as compared to the E. coli enzyme [Dailly00].

In the metabolic engineering field, deletion of adhE is a determinant in the production of compounds such as succinate [Singh11], D-lactate [Zhou11], and polyhydroxyalkanoates [Jian10].

Reviews: [Knappe90, Clark89]

Gene Citations: [Goodlove89, Leonardo93, MembrilloHernan99]

Locations: cytosol, membrane

Map Position: [1,294,669 <- 1,297,344] (27.9 centisomes)
Length: 2676 bp / 891 aa

Molecular Weight of Polypeptide: 96.127 kD (from nucleotide sequence)

pI: 6.72

Unification Links: ASAP:ABE-0004164 , CGSC:1041 , DIP:DIP-35790N , EchoBASE:EB0030 , EcoGene:EG10031 , EcoliWiki:b1241 , Mint:MINT-1288364 , ModBase:P0A9Q7 , OU-Microarray:b1241 , PortEco:adhE , PR:PRO_000022056 , Pride:P0A9Q7 , Protein Model Portal:P0A9Q7 , RefSeq:NP_415757 , RegulonDB:EG10031 , SMR:P0A9Q7 , String:511145.b1241 , UniProt:P0A9Q7

Relationship Links: InterPro:IN-FAMILY:IPR001670 , InterPro:IN-FAMILY:IPR012079 , InterPro:IN-FAMILY:IPR015590 , InterPro:IN-FAMILY:IPR016161 , InterPro:IN-FAMILY:IPR016162 , InterPro:IN-FAMILY:IPR016163 , InterPro:IN-FAMILY:IPR018211 , Pfam:IN-FAMILY:PF00171 , Pfam:IN-FAMILY:PF00465 , Prosite:IN-FAMILY:PS00060 , Prosite:IN-FAMILY:PS00913

In Paralogous Gene Group: 95 (14 members) , 266 (7 members)

Gene-Reaction Schematic: ?

Instance reaction of [a primary alcohol + NAD+ ↔ an aldehyde + NADH + H+] (1.1.1.1):
i1: ethanol + NAD+ ↔ acetaldehyde + NADH + H+ (1.1.1.1)

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006115 - ethanol biosynthetic process Inferred from experiment [Kessler91]
GO:0006066 - alcohol metabolic process Inferred by computational analysis [GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0015976 - carbon utilization Inferred by computational analysis [GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0004022 - alcohol dehydrogenase (NAD) activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Clark80]
GO:0008774 - acetaldehyde dehydrogenase (acetylating) activity Inferred from experiment Inferred by computational analysis [GOA01a, GOA01, Clark80]
GO:0042802 - identical protein binding Inferred from experiment [Acebron09, Lasserre06, Kessler92]
GO:0003824 - catalytic activity Inferred by computational analysis [UniProtGOA11]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016620 - oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Zhang07, LopezCampistrou05, Lasserre06]
GO:0016020 - membrane Inferred from experiment [Lasserre06]

MultiFun Terms: metabolism energy metabolism, carbon fermentation

Essentiality data for adhE knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 21-Nov-2011 by Fulcher C , SRI International


Enzymatic reaction of: pyruvate formate-lyase deactivase (aldehyde-alcohol dehydrogenase)

Synonyms: PFL deactivating enzyme, PFL-deactivase

pyruvate formate-lyase / 2-ketobutyrate formate-lyase <=> pyruvate formate-lyase (inactive)

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.

Reversibility of this reaction is unspecified.

Summary:
This is one of three reactions catalyzed by the multifunctional enzyme encoded by adhE. This activity was reported to catalyze radical quenching in the active form of pyruvate formate-lyase, thereby converting it back into the inactive form [Kessler91, Kessler92]. Deactivation was coupled to NAD+ reduction and required an intact coenzyme A sulfhydryl group [Kessler92]. However, [Nnyepi07] were unable to reproduce this deactivase activity.

It appears unlikely that this deactivase activity operates significantly during anaerobic growth when pyruvate formate-lyase is predominantly in the active radical form. Inhibition by pyruvate or NADH were suggested as possible physiological negative controls [Kessler92].

Cofactors or Prosthetic Groups: Fe2+ [Kessler91], coenzyme A [Kessler91], NAD+ [Kessler91]

Cofactor Binding Comment: Requires Fe+2, NAD and CoA as cofactors. [Knappe90, Kessler91]

Inhibitors (Competitive): NADH [Kessler92] , desulfo-CoA [Kessler92]

Inhibitors (Unknown Mechanism): pyruvate [Kessler92]


Enzymatic reaction of: alcohol dehydrogenase

Synonyms: ADH, alcohol:NAD+ oxidoreductase, aldehyde reductase

EC Number: 1.1.1.1

a primary alcohol + NAD+ <=> an aldehyde + 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.

This reaction is reversible. [Nnyepi07]

EC Number: 1.1.1.1

ethanol + NAD+ <=> acetaldehyde + 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.

This reaction is reversible. [Nnyepi07]

Alternative Substrates for a primary alcohol: n-butanol [Clark89 ] , n-propanol [Clark89 ]

In Pathways: ethanol degradation I , mixed acid fermentation

Summary:
This is one of three reactions catalyzed by the multifunctional enzyme encoded by adhE. The fermentative alcohol dehydrogenase (ADH) activity utilized ethanol, n-propanol and n-butanol, but showed poor activity with pentanol and was ineffective with methanol or branched alcohols (as stated in a review by [Clark89]). Ethanol was used as an assay substrate by [MembrilloHernan00].

Cofactors or Prosthetic Groups: Fe2+ [Kessler91]


Enzymatic reaction of: acetaldehyde dehydrogenase (aldehyde-alcohol dehydrogenase)

Synonyms: acetaldehyde:NAD+ oxidoreductase (CoA-acetylating), ACDH, coenzyme A linked aldehyde dehydrogenase

EC Number: 1.2.1.10

acetaldehyde + coenzyme A + NAD+ <=> acetyl-CoA + 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.

This reaction is reversible. [Shone81]

Alternative Substrates for acetaldehyde: butanal [Rudolph68 ] , propanal [Rudolph68 ]

In Pathways: superpathway of threonine metabolism , superpathway of purine deoxyribonucleosides degradation , superpathway of pyrimidine deoxyribonucleosides degradation , ethanol degradation I , threonine degradation IV , mixed acid fermentation , 2'-deoxy-α-D-ribose 1-phosphate degradation

Summary:
This is one of three reactions catalyzed by the multifunctional enzyme encoded by adhE. The data from [Rudolph68] and [Shone81] are for E. coli B using partially purified AdhE, and purified AdhE, respectively. Non-substrates included chloral, formaldehyde, benzaldehyde, and D,L-glyceraldehyde. The substrate butanal was 30-40% as active as acetaldehyde, and propanal was 60% as active [Rudolph68].

Cofactors or Prosthetic Groups: Fe2+ [Kessler91]

Cofactor Binding Comment: There is evidence that the enzyme contains two distinct NAD+ binding sites, an activator site and a catalytic site. [Shone81]

Activators (Unknown Mechanism): a thiol [Rudolph68, Shone81] , 3-pyridinecarboxaldehyde adenine dinucleotide [Shone81] , NAD+ [Shone81]

Inhibitors (Competitive): benzaldehyde [Shone81, Comment 5] , AMP [Shone81, Comment 6]

Inhibitors (Unknown Mechanism): guaiacol [Gupta00] , AMP [Shone81, Comment 7] , ADP-D-ribose [Shone81, Comment 7]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Yamato94, Kessler91, Goodlove89, UniProt11]
UniProt: Removed.
Chain 2 -> 891
[UniProt09]
UniProt: Aldehyde-alcohol dehydrogenase;
Acetylation-Modification 200
[Yu08]
 
Active-Site 246
[UniProt10]
UniProt: Non-Experimental Qualifier: by similarity;
Acetylation-Modification 358
[Zhang09a, UniProt11]
UniProt: N6-acetyllysine.
Nucleotide-Phosphate-Binding-Region 422 -> 427
[UniProt10]
UniProt: NAD; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b1241 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10031; confirmed by SwissProt match.


References

Acebron09: Acebron SP, Martin I, del Castillo U, Moro F, Muga A (2009). "DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface." FEBS Lett 583(18);2991-6. PMID: 19698713

Aristarkhov96: Aristarkhov A, Mikulskis A, Belasco JG, Lin EC (1996). "Translation of the adhE transcript to produce ethanol dehydrogenase requires RNase III cleavage in Escherichia coli." J Bacteriol 178(14);4327-32. PMID: 8763968

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

Chen91: Chen YM, Lin EC (1991). "Regulation of the adhE gene, which encodes ethanol dehydrogenase in Escherichia coli." J Bacteriol 1991;173(24);8009-13. PMID: 1744060

Clark80: Clark DP, Cronan JE (1980). "Acetaldehyde coenzyme A dehydrogenase of Escherichia coli." J Bacteriol 144(1);179-84. PMID: 6998946

Clark89: Clark DP (1989). "The fermentation pathways of Escherichia coli." FEMS Microbiol Rev 1989;5(3);223-34. PMID: 2698228

Dailly00: Dailly YP, Bunch P, Clark DP (2000). "Comparison of the fermentative alcohol dehydrogenases of Salmonella typhimurium and Escherichia coli." Microbios 103(406);179-96. PMID: 11131810

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

Echave03: Echave P, Tamarit J, Cabiscol E, Ros J (2003). "Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli." J Biol Chem 278(32);30193-8. PMID: 12783863

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

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Goodlove89: Goodlove PE, Cunningham PR, Parker J, Clark DP (1989). "Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli." Gene 85(1);209-14. PMID: 2695398

Gupta00: Gupta S, Mat-Jan F, Latifi M, Clark DP (2000). "Acetaldehyde dehydrogenase activity of the AdhE protein of Escherichia coli is inhibited by intermediates in ubiquinone synthesis." FEMS Microbiol Lett 182(1);51-5. PMID: 10612730

HollandStaley00: Holland-Staley CA, Lee K, Clark DP, Cunningham PR (2000). "Aerobic activity of Escherichia coli alcohol dehydrogenase is determined by a single amino acid." J Bacteriol 182(21);6049-54. PMID: 11029424

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

Jian10: Jian J, Zhang SQ, Shi ZY, Wang W, Chen GQ, Wu Q (2010). "Production of polyhydroxyalkanoates by Escherichia coli mutants with defected mixed acid fermentation pathways." Appl Microbiol Biotechnol 87(6);2247-56. PMID: 20535465

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

Kaga02: Kaga N, Umitsuki G, Clark DP, Nagai K, Wachi M (2002). "Extensive overproduction of the AdhE protein by rng mutations depends on mutations in the cra gene or in the Cra-box of the adhE promoter." Biochem Biophys Res Commun 295(1);92-7. PMID: 12083772

Kessler91: Kessler D, Leibrecht I, Knappe J (1991). "Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE." FEBS Lett 1991;281(1-2);59-63. PMID: 2015910

Kessler92: Kessler D, Herth W, Knappe J (1992). "Ultrastructure and pyruvate formate-lyase radical quenching property of the multienzymic AdhE protein of Escherichia coli." J Biol Chem 1992;267(25);18073-9. PMID: 1325457

Knappe90: Knappe J, Sawers G (1990). "A radical-chemical route to acetyl-CoA: the anaerobically induced pyruvate formate-lyase system of Escherichia coli." FEMS Microbiol Rev 1990;6(4);383-98. PMID: 2248795

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

Leonardo93: Leonardo MR, Cunningham PR, Clark DP (1993). "Anaerobic regulation of the adhE gene, encoding the fermentative alcohol dehydrogenase of Escherichia coli." J Bacteriol 1993;175(3);870-8. PMID: 8423158

Leonardo96: Leonardo MR, Dailly Y, Clark DP (1996). "Role of NAD in regulating the adhE gene of Escherichia coli." J Bacteriol 178(20);6013-8. PMID: 8830700

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

Lorowitz82: Lorowitz W, Clark D (1982). "Escherichia coli mutants with a temperature-sensitive alcohol dehydrogenase." J Bacteriol 152(2);935-8. PMID: 6752127

Matuszewska09: Matuszewska E, Kwiatkowska J, Ratajczak E, Kuczynska-Wisnik D, Laskowska E (2009). "Role of Escherichia coli heat shock proteins IbpA and IbpB in protection of alcohol dehydrogenase AdhE against heat inactivation in the presence of oxygen." Acta Biochim Pol 56(1);55-61. PMID: 19238259

MembrilloHernan00: Membrillo-Hernandez J, Echave P, Cabiscol E, Tamarit J, Ros J, Lin EC (2000). "Evolution of the adhE gene product of Escherichia coli from a functional reductase to a dehydrogenase. Genetic and biochemical studies of the mutant proteins." J Biol Chem 275(43);33869-75. PMID: 10922373

MembrilloHernan99: Membrillo-Hernandez J, Kwon O, De Wulf P, Finkel SE, Lin EC (1999). "Regulation of adhE (encoding ethanol oxidoreductase) by the Fis protein in Escherichia coli." J Bacteriol 181(23);7390-3. PMID: 10572146

MembrilloHernan99a: Membrillo-Hernandez J, Lin EC (1999). "Regulation of expression of the adhE gene, encoding ethanol oxidoreductase in Escherichia coli: transcription from a downstream promoter and regulation by fnr and RpoS." J Bacteriol 181(24);7571-9. PMID: 10601216

Mikulskis97: Mikulskis A, Aristarkhov A, Lin EC (1997). "Regulation of expression of the ethanol dehydrogenase gene (adhE) in Escherichia coli by catabolite repressor activator protein Cra." J Bacteriol 1997;179(22);7129-34. PMID: 9371462

Nnyepi07: Nnyepi MR, Peng Y, Broderick JB (2007). "Inactivation of E. coli pyruvate formate-lyase: role of AdhE and small molecules." Arch Biochem Biophys 459(1);1-9. PMID: 17280641

Rudolph68: Rudolph FB, Purich DL, Fromm HJ (1968). "Coenzyme A-linked aldehyde dehydrogenase from Escherichia coli. I. Partial purification, properties, and kinetic studies of the enzyme." J Biol Chem 1968;243(21);5539-45. PMID: 4301680

Shone81: Shone CC, Fromm HJ (1981). "Steady-state and pre-steady-state kinetics of coenzyme A linked aldehyde dehydrogenase from Escherichia coli." Biochemistry 1981;20(26);7494-501. PMID: 7034777

Singh11: Singh A, Cher Soh K, Hatzimanikatis V, Gill RT (2011). "Manipulating redox and ATP balancing for improved production of succinate in E. coli." Metab Eng 13(1);76-81. PMID: 21040799

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

UniProt10: 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."

Yamato94: Yamato M, Takahashi Y, Tomotake H, Ota F, Hirota K, Yamaguchi K (1994). "Monoclonal antibodies to spirosin of Yersinia enterocolitica and analysis of the localization of spirosome by use of them." Microbiol Immunol 38(3);177-82. PMID: 7521508

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

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111

Zhang09a: 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

Zhou11: Zhou L, Zuo ZR, Chen XZ, Niu DD, Tian KM, Prior BA, Shen W, Shi GY, Singh S, Wang ZX (2011). "Evaluation of genetic manipulation strategies on D-lactate production by Escherichia coli." Curr Microbiol 62(3);981-9. PMID: 21086129

Other References Related to Gene Regulation

Lintner08: Lintner RE, Mishra PK, Srivastava P, Martinez-Vaz BM, Khodursky AB, Blumenthal RM (2008). "Limited functional conservation of a global regulator among related bacterial genera: Lrp in Escherichia, Proteus and Vibrio." BMC Microbiol 8;60. PMID: 18405378

Saier96: Saier MH, Ramseier TM (1996). "The catabolite repressor/activator (Cra) protein of enteric bacteria." J Bacteriol 1996;178(12);3411-7. PMID: 8655535

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


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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