Escherichia coli K-12 substr. MG1655 Enzyme: acetaldehyde dehydrogenase 2

Gene: mhpF Accession Numbers: M014 (EcoCyc), b0351, ECK0348

Regulation Summary Diagram: ?

Regulation summary diagram for mhpF

mhpF encodes an acetaldehyde dehydrogenase [Ferrandez97]. MhpF is active as a monomer; the rate-limiting step of the reaction appears to be transthioesterification [Fischer13].

MhpF is involved in synthesis of n-butanol in an enigeered reversal of the β-oxidation pathway [Dellomonaco11].

The expression of MhpE is translationally coupled to MhpF, and interaction between the two proteins appears to be required for solubility of MhpE [Lee06].

Citations: [Guadalupe10, Zhang11]

Locations: cytosol

Map Position: [372,145 -> 373,095] (8.02 centisomes, 29°)
Length: 951 bp / 316 aa

Molecular Weight of Polypeptide: 33.442 kD (from nucleotide sequence), 35.3 kD (experimental) [Fischer13 ]

Unification Links: ASAP:ABE-0001207 , DIP:DIP-10210N , EchoBASE:EB3390 , EcoGene:EG13625 , EcoliWiki:b0351 , ModBase:P77580 , OU-Microarray:b0351 , PortEco:mhpF , PR:PRO_000023233 , Protein Model Portal:P77580 , RefSeq:NP_414885 , RegulonDB:M014 , SMR:P77580 , String:511145.b0351 , Swiss-Model:P77580 , UniProt:P77580

Relationship Links: InterPro:IN-FAMILY:IPR000534 , InterPro:IN-FAMILY:IPR003361 , InterPro:IN-FAMILY:IPR015426 , InterPro:IN-FAMILY:IPR016040 , Panther:IN-FAMILY:PTHR21123 , Pfam:IN-FAMILY:PF01118 , Pfam:IN-FAMILY:PF09290 , Smart:IN-FAMILY:SM00859

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

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

Genetic Regulation Schematic: ?

Genetic regulation schematic for mhpF

GO Terms:

Biological Process: GO:0019380 - 3-phenylpropionate catabolic process Inferred by computational analysis [UniProtGOA12]
GO:0019439 - aromatic compound catabolic process Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Lee06]
GO:0008774 - acetaldehyde dehydrogenase (acetylating) activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Fischer13, Ferrandez97, Burlingame83]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11]
GO:0016620 - oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01]
GO:0051287 - NAD binding Inferred by computational analysis [GOA06, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization carbon compounds

Essentiality data for mhpF 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]

Last-Curated ? 08-Jul-2014 by Keseler I , SRI International

Enzymatic reaction of: acetaldehyde dehydrogenase

Synonyms: acetaldehyde dehydrogenase (acetylating), acetaldehyde:NAD+ oxidoreductase (CoA-acetylating)

EC Number:

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 Enzyme Commission system.

This reaction is reversible.

In Pathways: superpathway of L-threonine metabolism , 3-phenylpropanoate and 3-(3-hydroxyphenyl)propanoate degradation , superpathway of purine deoxyribonucleosides degradation , superpathway of pyrimidine deoxyribonucleosides degradation , ethanol degradation I , L-threonine degradation IV , 2-oxopentenoate degradation , 2'-deoxy-α-D-ribose 1-phosphate degradation

Kinetic Parameters:

Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
[Rudolph68, BRENDA14]
[Shone81, BRENDA14]
[Shone81, BRENDA14]
[Rudolph68, BRENDA14]
[Shone81, BRENDA14]
[Rudolph68, BRENDA14]
[Rudolph68, BRENDA14]
[Shone81, BRENDA14]
[Fischer13, BRENDA14]
coenzyme A
[Shone81, BRENDA14]
coenzyme A
[Rudolph68, BRENDA14]
coenzyme A
[Fischer13, BRENDA14]

pH(opt): 7 [BRENDA14, Rudolph68], 8.8 [BRENDA14, Clark80]

Sequence Features

Protein sequence of acetaldehyde dehydrogenase 2 with features indicated

Feature Class Location Citations Comment
Nucleotide-Phosphate-Binding-Region 11 -> 14
UniProt: NAD; Non-Experimental Qualifier: by similarity.
Active-Site 131
UniProt: Acyl-thioester intermediate; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 162 -> 170
UniProt: NAD; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 289
UniProt: NAD; Non-Experimental Qualifier: by similarity.

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b0351 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene M014. 29-April-98 product string changed to acetaldehyde dehydrogenase from 4-hydroxy-2-oxovalerate aldolase. There may still be some confusion due to reciprocal synonyms of mhpE and mhpF. (ptoole)


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

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014."

Burlingame83: Burlingame R, Chapman PJ (1983). "Stereospecificity in meta-fission catabolic pathways." J Bacteriol 155(1);424-6. PMID: 6345511

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

Dellomonaco11: Dellomonaco C, Clomburg JM, Miller EN, Gonzalez R (2011). "Engineered reversal of the β-oxidation cycle for the synthesis of fuels and chemicals." Nature 476(7360);355-9. PMID: 21832992

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

Ferrandez97: Ferrandez A, Garcia JL, Diaz E (1997). "Genetic characterization and expression in heterologous hosts of the 3-(3-hydroxyphenyl)propionate catabolic pathway of Escherichia coli K-12." J Bacteriol 1997;179(8);2573-81. PMID: 9098055

Fischer13: Fischer B, Boutserin S, Mazon H, Collin S, Branlant G, Gruez A, Talfournier F (2013). "Catalytic properties of a bacterial acylating acetaldehyde dehydrogenase: evidence for several active oligomeric states and coenzyme A activation upon binding." Chem Biol Interact 202(1-3);70-7. PMID: 23237860

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.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Guadalupe10: Guadalupe Medina V, Almering MJ, van Maris AJ, Pronk JT (2010). "Elimination of glycerol production in anaerobic cultures of a Saccharomyces cerevisiae strain engineered to use acetic acid as an electron acceptor." Appl Environ Microbiol 76(1);190-5. PMID: 19915031

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

Lee06: Lee SJ, Ko JH, Kang HY, Lee Y (2006). "Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia coli." Biochem Biophys Res Commun 346(3);1009-15. PMID: 16782065

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

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

UniProt12b: UniProt Consortium (2012). "UniProt version 2012-11 released on 2012-11-26 00:00:00." Database.

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

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

Zhang11: Zhang L, Tang Y, Guo ZP, Ding ZY, Shi GY (2011). "Improving the ethanol yield by reducing glycerol formation using cofactor regulation in Saccharomyces cerevisiae." Biotechnol Lett 33(7);1375-80. PMID: 21400237

Other References Related to Gene Regulation

Torres03: Torres B, Porras G, Garcia JL, Diaz E (2003). "Regulation of the mhp cluster responsible for 3-(3-hydroxyphenyl) propionic acid degradation in escherichia coli." J Biol Chem 278(30);27575-85. PMID: 12748194

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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 19.0 on Tue Oct 6, 2015, biocyc13.