|Gene:||ahr||Accession Numbers: EG11436 (EcoCyc), b4269, ECK4262|
Synonyms: yjgB, AdhZ3
Ahr is a member of the zinc-containing medium-chain dehydrogenase/reductase family. The enzyme is a 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].
Unpurified Ahr was previously shown to have acetaldehyde and isobutyraldehyde reductase activity, with a preference for the NADPH co-substrate. This activity contributes to the conversion of isobutyraldehyde to isobutanol in an engineered strain [Rodriguez12]. 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, Ahr, and YahK [Koma12].
Mutants that change the preference of the enzyme for the NADPH cosubstrate towards NADH have been constructed [Pick14].
The yjgB gene of Salmonella enterica serovar Typhimurium is part of the RpoS regulon [IbanezRuiz00].
Ahr: "aldehyde reductase" [Akhtar13]
|Map Position: [4,493,213 <- 4,494,232] (96.84 centisomes)||Length: 1020 bp / 339 aa|
Molecular Weight of Polypeptide: 36.502 kD (from nucleotide sequence)
Unification Links: ASAP:ABE-0013982 , EchoBASE:EB1406 , EcoGene:EG11436 , EcoliWiki:b4269 , ModBase:P27250 , OU-Microarray:b4269 , PortEco:yjgB , Pride:P27250 , Protein Model Portal:P27250 , RefSeq:NP_418690 , RegulonDB:EG11436 , SMR:P27250 , String:511145.b4269 , UniProt:P27250
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 , Pfam:IN-FAMILY:PF00107 , Pfam:IN-FAMILY:PF08240 , Prosite:IN-FAMILY:PS00059
In Paralogous Gene Group: 582 (3 members)
Instance reaction of [an aldehyde + NADP+ + H2O → a carboxylate + NADPH + 2 H+] (188.8.131.52):
Instance reactions of [an alcohol + NADP+ = an aldehyde + NADPH + H+] (184.108.40.206):
|Biological Process:||GO:0006629 - lipid metabolic process
GO:0006631 - fatty acid metabolic process [UniProtGOA11a]
GO:0055114 - oxidation-reduction process [UniProtGOA11a, GOA01]
|Molecular Function:||GO:0008106 - alcohol dehydrogenase (NADP+) activity
[GOA01a, Pick13, Rodriguez12]
GO:0008270 - zinc ion binding [GOA01, Sevcenco11]
GO:0016491 - oxidoreductase activity [UniProtGOA11a, GOA01]
GO:0046872 - metal ion binding [UniProtGOA11a]
|Cellular Component:||GO:0005829 - cytosol [DiazMejia09]|
|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]|
Enzymatic reaction of: aldehyde reductase
EC Number: 220.127.116.11
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.
Kinetic parameters for a range of substrates were measured in [Pick13]. The substrate specificity of the enzyme from E. coli BL21(DE3), which differs in a single amino acid from the K-12 enzyme, was characterized in [Akhtar13]; the enzyme primarily utilizes C4, C6 and C8 aldehydes. The initial rate of alcohol oxidation is two orders of magnitude lower than the initial rate of aldehyde reduction.
T(opt): 37-50 °C [Pick13]
pH(opt): 7-8 [Pick14]
|Sequence-Conflict||331 -> 339|
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 ].
10/20/97 Gene b4269 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11436; confirmed by SwissProt match.
Akhtar13: Akhtar MK, Turner NJ, Jones PR (2013). "Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities." Proc Natl Acad Sci U S A 110(1);87-92. PMID: 23248280
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
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
IbanezRuiz00: Ibanez-Ruiz M, Robbe-Saule V, Hermant D, Labrude S, Norel F (2000). "Identification of RpoS (sigma(S))-regulated genes in Salmonella enterica serovar typhimurium." J Bacteriol 182(20);5749-56. PMID: 11004173
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
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
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
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
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