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Escherichia coli K-12 substr. MG1655 Enzyme: aldehyde reductase, NADPH-dependent



Gene: yahK Accession Numbers: G6190 (EcoCyc), b0325, ECK0323

Synonyms: AdhZ2

Regulation Summary Diagram: ?

Summary:
YahK is a member of the zinc-containing medium-chain dehydrogenase/reductase family. The enzyme is a major source of NADPH-dependent aldehyde reductase activity in the cell. Catalytic activity of the purified enzyme was measured with a variety of aldehyde substrates [Pick13].

In a metabolically engineered strain, phenylacetaldehyde and 4-hydroxyphenylacetaldehyde are reduced to 2-phenylethanol and 2-(4-hydroxyphenyl)ethanol by the endogenous aldehyde reductases YqhD, YjgB, and YahK [Koma12]. In a different engineered strain (S)-lactaldehyde and (R)-lactaldehyde were reduced to the corresponding forms of propane-1,2-diol [Niu14]. Conversely, a broad survey of aldehyde reductases showed that YahK was one of several endogenous aldehyde reductases that contribute to the degradation of desired aldehyde end products of metabolic engineering [Rodriguez14].

Mutants that change the preference of the enzyme for the NADPH cosubstrate towards NADH have been constructed [Pick14].

An acetate-tolerant mutant of E. coli DH5α, DA19, grows faster and produces less acetate on chemically defined medium than its parent; expression of yahK is downregulated in DA19 compared to DH5α [Zhang11c].

yahK is involved in biofilm formation by a reduced-genome E. coli strain, but not wild-type [May11].

Map Position: [342,108 -> 343,157] (7.37 centisomes)
Length: 1050 bp / 349 aa

Molecular Weight of Polypeptide: 37.978 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0001113 , DIP:DIP-11263N , EchoBASE:EB3364 , EcoGene:EG13595 , EcoliWiki:b0325 , ModBase:P75691 , OU-Microarray:b0325 , PortEco:yahK , Pride:P75691 , Protein Model Portal:P75691 , RefSeq:NP_414859 , RegulonDB:G6190 , SMR:P75691 , String:511145.b0325 , UniProt:P75691

Relationship Links: InterPro:IN-FAMILY:IPR002085 , InterPro:IN-FAMILY:IPR002328 , InterPro:IN-FAMILY:IPR006140 , InterPro:IN-FAMILY:IPR011032 , InterPro:IN-FAMILY:IPR013149 , InterPro:IN-FAMILY:IPR013154 , InterPro:IN-FAMILY:IPR016040 , Panther:IN-FAMILY:PTHR11695 , PDB:Structure:1UUF , 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 [an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+] (1.2.1.4):
i3: acetaldehyde + NADP+ + H2O → acetate + NADPH + 2 H+ (1.2.1.4)

Instance reactions of [an alcohol + NADP+ = an aldehyde + NADPH + H+] (1.1.1.2):
i1: (S)-propane-1,2-diol + NADP+ = (S)-lactaldehyde + NADPH + H+ (1.1.1.-)

i2: (R)-propane-1,2-diol + NADP+ = (R)-lactaldehyde + NADPH + H+ (1.1.1.-)

GO Terms:

Biological Process: GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0008106 - alcohol dehydrogenase (NADP+) activity Inferred from experiment Inferred by computational analysis [GOA01a, Pick13]
GO:0008270 - zinc ion binding Inferred by computational analysis [GOA01]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]

Gene Class: UNCLASSIFIED

Essentiality data for yahK 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]

Credits:
Last-Curated ? 05-Sep-2014 by Keseler I , SRI International


Enzymatic reaction of: aldehyde reductase

EC Number: 1.1.1.2

an alcohol + NADP+ <=> an aldehyde + NADPH + 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.

Alternative Substrates for an alcohol: geraniol [Zhou14 ]

Alternative Substrates for an aldehyde: acetaldehyde [Rodriguez14 ] , hexanal [Rodriguez14 ] , octanal [Rodriguez14 ] , decanal [Rodriguez14 ] , furfural [Pick13 ] , butanal [Pick13 ]

Summary:
Kinetic parameters for a range of substrates were measured in [Pick13].

Kinetic Parameters:

Substrate
Km (μM)
Citations
NADP+
12.0
[Pick13]
butanal
2100.0
[Pick13]
furfural
135.0
[Pick13]
NADPH
11.0
[Pick13]


Enzymatic reaction of: isobutyraldehyde reductase (aldehyde reductase, NADPH-dependent)

EC Number: 1.1.1.-

isobutanol + NADP+ <=> isobutanal + NADPH + 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.

Reversibility of this reaction is unspecified.


Enzymatic reaction of: (S)-lactaldehyde dehydrogenase (aldehyde reductase, NADPH-dependent)

EC Number: 1.1.1.-

(S)-propane-1,2-diol + NADP+ <=> (S)-lactaldehyde + NADPH + 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.

Reversibility of this reaction is unspecified.

Credits:
Imported from MetaCyc 08-Aug-2014 by Caspi R , SRI International


Enzymatic reaction of: (R)-lactaldehyde dehydrogenase (aldehyde reductase, NADPH-dependent)

EC Number: 1.1.1.-

(R)-propane-1,2-diol + NADP+ <=> (R)-lactaldehyde + NADPH + 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.

Reversibility of this reaction is unspecified.

Credits:
Imported from MetaCyc 08-Aug-2014 by Caspi R , SRI International


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 40
[UniProt10a]
UniProt: Zinc 1; catalytic;
Metal-Binding-Site 62
[UniProt10a]
UniProt: Zinc 1; catalytic;
Metal-Binding-Site 93
[UniProt10a]
UniProt: Zinc 2;
Metal-Binding-Site 96
[UniProt10a]
UniProt: Zinc 2;
Metal-Binding-Site 99
[UniProt10a]
UniProt: Zinc 2;
Metal-Binding-Site 107
[UniProt10a]
UniProt: Zinc 2;
Sequence-Conflict 116
[Chung97, UniProt10a]
Alternate sequence: S → L; UniProt: (in Ref. 1; AAB18051);
Sequence-Conflict 145
[Chung97, UniProt10a]
Alternate sequence: H → Y; UniProt: (in Ref. 1; AAB18051);
Metal-Binding-Site 158
[UniProt10a]
UniProt: Zinc 1; catalytic;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
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

Cameron86: Cameron, D.C., Cooney, C.L. (1986). "A novel fermentation: the production of (R)-1,2-propanediol and acetol by Clostridium thermosaccharolyticum." Nature Bio/Technology 4:651-654.

Chung97: Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. (1997). "Sequence of minutes 4-25 of Escherichia coli." Data submission to EMBL/GenBank/DDBJ databases on 1997-01.

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.

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

Koma12: Koma D, Yamanaka H, Moriyoshi K, Ohmoto T, Sakai K (2012). "Production of aromatic compounds by metabolically engineered Escherichia coli with an expanded shikimate pathway." Appl Environ Microbiol 78(17);6203-16. PMID: 22752168

May11: May T, Okabe S (2011). "Enterobactin is required for biofilm development in reduced-genome Escherichia coli." Environ Microbiol 13(12);3149-62. PMID: 21980953

Niu14: Niu W, Guo J (2014). "Stereospecific Microbial Conversion of Lactic Acid into 1,2-Propanediol." ACS Synth Biol. PMID: 25007409

Pick13: Pick A, Ruhmann B, Schmid J, Sieber V (2013). "Novel CAD-like enzymes from Escherichia coli K-12 as additional tools in chemical production." Appl Microbiol Biotechnol 97(13);5815-24. PMID: 23093176

Pick14: Pick A, Ott W, Howe T, Schmid J, Sieber V (2014). "Improving the NADH-cofactor specificity of the highly active AdhZ3 and AdhZ2 from Escherichia coli K-12." J Biotechnol. PMID: 24992211

Rodriguez14: Rodriguez GM, Atsumi S (2014). "Toward aldehyde and alkane production by removing aldehyde reductase activity in Escherichia coli." Metab Eng 25;227-37. PMID: 25108218

Shelley07: Shelley S (2007). "A renewable route to propylene glycol." Chemical Engineering Progress 103(8):6-9.

Suzuki68: Suzuki, T., Onishi, H. (1968). "Aerobic dissimilation of l-rhamnose and the production of l-rhamnonic acid and 1,2-propanediol by yeasts." Agr. Biol. Chem. 32:888-893.

TranDin85: Tran-Din K, Gottschalk G (1985). "Formation of d(-)-1,2-propanediol and d(-)-lactate from glucose by Clostridium sphenoides under phosphate limitation." Archives of Microbiology 142(1);87-92.

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

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

Weimer84: Weimer PJ (1984). "Fermentation of 6-Deoxyhexoses by Bacillus macerans." Appl Environ Microbiol 47(2);263-7. PMID: 16346466

Zhang11c: Zhang X, Zhang Y, Li Z, Xia Y, Ye Q (2011). "Continuous culture and proteomic analysis of Escherichia coli DH5α and its acetate-tolerant mutant DA19 under conditions of nitrogen source limitation." Bioprocess Biosyst Eng 34(2);179-87. PMID: 20700606

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 Dec 18, 2014, BIOCYC14B.