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



Gene: adhP Accession Numbers: G6775 (EcoCyc), b1478, ECK1472

Synonyms: yddN

Regulation Summary Diagram: ?

Subunit composition of ethanol dehydrogenase / alcohol dehydrogenase = [AdhP]4
         ethanol dehydrogenase / alcohol dehydrogenase = AdhP

Summary:
AdhP is an ethanol-active medium-chain alcohol dehydrogenase/acetaldehyde reductase. The enzyme is more efficient in the reverse direction of acetaldehyde reduction [Shafqat99]. AdhP activity contributes to the conversion of isobutyraldehyde to isobutanol in an engineered strain [Rodriguez12].

AdhP did not show dehydrogenase activity in a high-throughput screen of purified proteins [Kuznetsova05].

Crystal structures of AdhP has been solved [Karlsson03, Thomas13].

Expression of AdhP is inducible by ethanol [Shafqat99].

Locations: cytosol

Map Position: [1,550,852 <- 1,551,862] (33.43 centisomes)
Length: 1011 bp / 336 aa

Molecular Weight of Polypeptide: 35.38 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0004928 , EchoBASE:EB2506 , EcoGene:EG12622 , EcoliWiki:b1478 , ModBase:P39451 , OU-Microarray:b1478 , PortEco:adhP , PR:PRO_000022057 , Pride:P39451 , Protein Model Portal:P39451 , RefSeq:NP_415995 , RegulonDB:G6775 , SMR:P39451 , String:511145.b1478 , Swiss-Model:P39451 , UniProt:P39451

Relationship Links: InterPro:IN-FAMILY:IPR002085 , InterPro:IN-FAMILY:IPR002328 , InterPro:IN-FAMILY:IPR011032 , InterPro:IN-FAMILY:IPR013149 , InterPro:IN-FAMILY:IPR013154 , InterPro:IN-FAMILY:IPR016040 , Panther:IN-FAMILY:PTHR11695 , PDB:Structure:4GKV , Pfam:IN-FAMILY:PF00107 , Pfam:IN-FAMILY:PF08240 , Prosite:IN-FAMILY:PS00059

In Paralogous Gene Group: 103 (13 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)

GO Terms:

Biological Process: GO:0006974 - cellular response to DNA damage stimulus Inferred from experiment [Khil02]
GO:0045471 - response to ethanol Inferred from experiment [Shafqat99]
GO:0046187 - acetaldehyde catabolic process Inferred from experiment [Shafqat99]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0004022 - alcohol dehydrogenase (NAD) activity Inferred from experiment Inferred by computational analysis [GOA01, Shafqat99]
GO:0008270 - zinc ion binding Inferred from experiment Inferred by computational analysis [GOA01a, Thomas13]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism energy metabolism, carbon anaerobic respiration

Essentiality data for adhP 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:
Created 17-Jul-2013 by Keseler I , SRI International
Last-Curated ? 17-Jul-2013 by Keseler I , SRI International


Enzymatic reaction of: ethanol dehydrogenase

Synonyms: ethanol dehydrogenase/acetaldehyde reductase, alcohol dehydrogenase, propanol-preferring, aldehyde reductase, alcohol:NAD+ oxidoreductase

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. [Shafqat99]

In Pathways: ethanol degradation I , mixed acid fermentation

Inhibitors (Noncompetitive): pyrazole (Ki = 0.2µM) [Shafqat99] , 4-methylpyrazole (Ki = 44µM) [Shafqat99]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
acetaldehyde
30.0
163.0
[Shafqat99]
ethanol
700.0
68.0
[Shafqat99]


Enzymatic reaction of: alcohol dehydrogenase

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.

Alternative Substrates for a primary alcohol: geraniol [Zhou14 ] , octan-1-ol [Shafqat99 ]

Alternative Substrates for an aldehyde: isobutanal [Rodriguez12 ]

In Pathways: ethanol degradation I , mixed acid fermentation

Kinetic Parameters:

Substrate
Km (μM)
Citations
octan-1-ol
1200.0
[Shafqat99]


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 34
[Harayama94, UniProt10a]
Alternate sequence: C → P; UniProt: (in Ref. 4; AA sequence);
Metal-Binding-Site 37
[UniProt10]
UniProt: Zinc 1; catalytic; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 58
[UniProt10]
UniProt: Zinc 1; catalytic; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 89
[UniProt10]
UniProt: Zinc 2; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 90
[Kubo90, UniProt10a]
Alternate sequence: G → R; UniProt: (in Ref. 5; M31532);
Metal-Binding-Site 92
[UniProt10]
UniProt: Zinc 2; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 95
[UniProt10]
UniProt: Zinc 2; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 103
[UniProt10]
UniProt: Zinc 2; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 104
[Kubo90, UniProt10a]
Alternate sequence: R → P; UniProt: (in Ref. 5; M31532);
Sequence-Conflict 108
[Kubo90, UniProt10a]
Alternate sequence: N → K; UniProt: (in Ref. 5; M31532);
Sequence-Conflict 112
[Kubo90, UniProt10a]
Alternate sequence: S → G; UniProt: (in Ref. 5; M31532);
Sequence-Conflict 117 -> 118
[Kubo90, UniProt10a]
Alternate sequence: MA → RV; UniProt: (in Ref. 5; M31532);
Metal-Binding-Site 145
[UniProt10]
UniProt: Zinc 1; catalytic; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

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

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

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, 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."

Harayama94: Harayama S. (1994). Data submission to UniProtKB on 1994-10.

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

Karlsson03: Karlsson A, El-Ahmad M, Johansson K, Shafqat J, Jornvall H, Eklund H, Ramaswamy S (2003). "Tetrameric NAD-dependent alcohol dehydrogenase." Chem Biol Interact 143-144;239-45. PMID: 12604209

Khil02: Khil PP, Camerini-Otero RD (2002). "Over 1000 genes are involved in the DNA damage response of Escherichia coli." Mol Microbiol 44(1);89-105. PMID: 11967071

Kubo90: Kubo KM, Craig NL (1990). "Bacterial transposon Tn7 utilizes two different classes of target sites." J Bacteriol 172(5);2774-8. PMID: 2158980

Kuznetsova05: Kuznetsova E, Proudfoot M, Sanders SA, Reinking J, Savchenko A, Arrowsmith CH, Edwards AM, Yakunin AF (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29(2);263-79. PMID: 15808744

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Rodriguez12: Rodriguez GM, Atsumi S (2012). "Isobutyraldehyde production from Escherichia coli by removing aldehyde reductase activity." Microb Cell Fact 11(1);90. PMID: 22731523

Shafqat99: Shafqat J, Hoog JO, Hjelmqvist L, Oppermann UC, Ibanez C, Jornvall H (1999). "An ethanol-inducible MDR ethanol dehydrogenase/acetaldehyde reductase in Escherichia coli: structural and enzymatic relationships to the eukaryotic protein forms." Eur J Biochem 1999;263(2);305-11. PMID: 10406936

Thomas13: Thomas LM, Harper AR, Miner WA, Ajufo HO, Branscum KM, Kao L, Sims PA (2013). "Structure of Escherichia coli AdhP (ethanol-inducible dehydrogenase) with bound NAD." Acta Crystallogr Sect F Struct Biol Cryst Commun 69(Pt 7);730-2. PMID: 23832197

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

Zhou14: Zhou J, Wang C, Yoon SH, Jang HJ, Choi ES, Kim SW (2014). "Engineering Escherichia coli for selective geraniol production with minimized endogenous dehydrogenation." J Biotechnol 169;42-50. PMID: 24269531


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 Thu Nov 27, 2014, biocyc12.