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Identification
YMDB IDYMDB00570
Nameisoamylol
SpeciesSaccharomyces cerevisiae
StrainBrewer's yeast
Description3-Methylbutanol (isoamyl alcohol, isopentanol) is one of several isomers of amyl alcohol. It is the major higher chain alcohol in alcoholic beverages and is present in cider, mead, beer, wine, and spirits to varying degrees, being obtained by the fermentation of starches. It is responsible for malt-like aromas. This alcohol tends to decrease in content during wine aging.
Structure
Thumb
Synonyms
  • 1-Butanol, 3-methyl-
  • 1-Hydroxy-3-methylbutane
  • 2-Methyl-4-butanol
  • 3-Methyl-1-Butanol
  • 3-Methyl-butan-(1)-ol
  • 3-methyl-Butanol
  • 3-Methylbutan-1-ol
  • 3-methylbutanoI
  • 3-Methylbutanol
  • 3-Metil-butanolo
  • Alcool amilico
  • Alcool isoamylique
  • Amylowy alkohol
  • Butan-1-ol, 3-methyl
  • Butanol, 3-methyl-
  • Fermentation amyl alcohol
  • Fusel oil
  • Fuseloel
  • Huile de fusel
  • I-amyl alcohol
  • Iso-amyl alcohol
  • Iso-amylalkohol
  • Isoamyl alcohol
  • Isoamyl alkohol
  • Isoamylalcohol
  • isoamylol
  • Isobutyl carbinol
  • Isobutylcarbinol
  • Isopentan-1-ol
  • Isopentanol
  • Isopentyl alcohol
  • Isopentylalkohol
  • Methyl-3-butan-1-ol
  • primary isoamyl alcohol
  • Isoamyl alcohol (3-methyl butanol)
  • Isoamyl alcohol (natural)
  • Isopentyl alcohol, barium salt
  • Isopentyl alcohol, magnesium salt
  • Isopentyl alcohol, sodium salt
  • Isopentyl alcohol, lead (2+) salt
  • Isopentyl alcohol, potassium salt
  • Isopentyl alcohol, strontium salt
  • Isopentyl alcohol, 1-(14)C-labeled
CAS number123-51-3
WeightAverage: 88.1482
Monoisotopic: 88.088815006
InChI KeyPHTQWCKDNZKARW-UHFFFAOYSA-N
InChIInChI=1S/C5H12O/c1-5(2)3-4-6/h5-6H,3-4H2,1-2H3
IUPAC Name3-methylbutan-1-ol
Traditional IUPAC Nameisoamyl alcohol
Chemical FormulaC5H12O
SMILESCC(C)CCO
Chemical Taxonomy
DescriptionThis compound belongs to the class of organic compounds known as primary alcohols. These are compounds comprising the primary alcohol functional group, with the general structure RCOH (R=alkyl, aryl).
KingdomOrganic compounds
Super ClassOrganic oxygen compounds
ClassOrganooxygen compounds
Sub ClassAlcohols and polyols
Direct ParentPrimary alcohols
Alternative Parents
Substituents
  • Hydrocarbon derivative
  • Primary alcohol
  • Aliphatic acyclic compound
Molecular FrameworkAliphatic acyclic compounds
External Descriptors
Physical Properties
StateLiquid
Charge0
Melting point-117.2 °C
Experimental Properties
PropertyValueReference
Water Solubility26.7 mg/mL at 25 oC [RIDDICK,JA et al. (1986)]PhysProp
LogP1.16 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility38 g/LALOGPS
logP1.33ALOGPS
logP1.09ChemAxon
logS-0.37ALOGPS
pKa (Strongest Acidic)17.17ChemAxon
pKa (Strongest Basic)-1.9ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count1ChemAxon
Hydrogen Donor Count1ChemAxon
Polar Surface Area20.23 ŲChemAxon
Rotatable Bond Count2ChemAxon
Refractivity26.68 m³·mol⁻¹ChemAxon
Polarizability11.03 ųChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations
  • extracellular
  • mitochondrion
  • cytoplasm
Organoleptic Properties
Flavour/OdourSource
AlcoholicFDB008131
BananaFDB008131
BurntFDB008131
FruityFDB008131
FuselFDB008131
MaltFDB008131
OilFDB008131
WhiskeyFDB008131
SMPDB Pathways
Leucine DegradationPW002490 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG PathwaysNot Available
SMPDB Reactions
3-methylbutanal + NADH + hydronNAD + isoamylol
KEGG Reactions
Acetyl-CoA + isoamylolisoamyl acetate + Coenzyme A
NADH + 3-methylbutanal + hydronNAD + isoamylol
3-methylbutanal + NADPH + hydronNADP + isoamylol
isoamyl acetate + waterAcetic acid + isoamylol + hydron
Concentrations
Intracellular ConcentrationsNot Available
Extracellular ConcentrationsNot Available
Spectra
Spectra
References
References:
  • Scheer, M., Grote, A., Chang, A., Schomburg, I., Munaretto, C., Rother, M., Sohngen, C., Stelzer, M., Thiele, J., Schomburg, D. (2011). "BRENDA, the enzyme information system in 2011." Nucleic Acids Res 39:D670-D676.21062828
  • Herrgard, M. J., Swainston, N., Dobson, P., Dunn, W. B., Arga, K. Y., Arvas, M., Bluthgen, N., Borger, S., Costenoble, R., Heinemann, M., Hucka, M., Le Novere, N., Li, P., Liebermeister, W., Mo, M. L., Oliveira, A. P., Petranovic, D., Pettifer, S., Simeonidis, E., Smallbone, K., Spasic, I., Weichart, D., Brent, R., Broomhead, D. S., Westerhoff, H. V., Kirdar, B., Penttila, M., Klipp, E., Palsson, B. O., Sauer, U., Oliver, S. G., Mendes, P., Nielsen, J., Kell, D. B. (2008). "A consensus yeast metabolic network reconstruction obtained from a community approach to systems biology." Nat Biotechnol 26:1155-1160.18846089
  • Dickinson, J. R., Lanterman, M. M., Danner, D. J., Pearson, B. M., Sanz, P., Harrison, S. J., Hewlins, M. J. (1997). "A 13C nuclear magnetic resonance investigation of the metabolism of leucine to isoamyl alcohol in Saccharomyces cerevisiae." J Biol Chem 272:26871-26878.9341119
  • Gallardo-Chacon, J. J., Vichi, S., Lopez-Tamames, E., Buxaderas, S. (2010). "Changes in the Sorption of Diverse Volatiles by Saccharomyces cerevisiae Lees during Sparkling Wine Aging." J Agric Food Chem :.21073195
  • Patel, S., Shibamoto, T. (2002). "Effect of different strains of Saccharomyces cerevisiae on production of volatiles in Napa Gamay wine and Petite Sirah wine." J Agric Food Chem 50:5649-5653.12236692
  • Leskovac, V., Trivic, S., Pericin, D. (2002). "The three zinc-containing alcohol dehydrogenases from baker's yeast, Saccharomyces cerevisiae." FEMS Yeast Res 2:481-494.12702265
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
  • Fukuda, K., Kiyokawa, Y., Yanagiuchi, T., Wakai, Y., Kitamoto, K., Inoue, Y., Kimura, A. (2000). "Purification and characterization of isoamyl acetate-hydrolyzing esterase encoded by the IAH1 gene of Saccharomyces cerevisiae from a recombinant Escherichia coli." Appl Microbiol Biotechnol 53:596-600.10855721
  • Verstrepen, K. J., Van Laere, S. D., Vanderhaegen, B. M., Derdelinckx, G., Dufour, J. P., Pretorius, I. S., Winderickx, J., Thevelein, J. M., Delvaux, F. R. (2003). "Expression levels of the yeast alcohol acetyltransferase genes ATF1, Lg-ATF1, and ATF2 control the formation of a broad range of volatile esters." Appl Environ Microbiol 69:5228-5237.12957907
  • Larroy, C., Pares, X., Biosca, J. A. (2002). "Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family." Eur J Biochem 269:5738-5745.12423374
  • Dickinson, J. R., Salgado, L. E., Hewlins, M. J. (2003). "The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae." J Biol Chem 278:8028-8034.12499363
  • Larroy, C., Fernandez, M. R., Gonzalez, E., Pares, X., Biosca, J. A. (2002). "Characterization of the Saccharomyces cerevisiae YMR318C (ADH6) gene product as a broad specificity NADPH-dependent alcohol dehydrogenase: relevance in aldehyde reduction." Biochem J 361:163-172.11742541
Synthesis Reference:Not Available
External Links:
ResourceLink
CHEBI ID15837
HMDB IDHMDB06007
Pubchem Compound ID9536
Kegg IDC07328
ChemSpider ID29000
FOODB IDFDB008131
WikipediaIsoamyl_alcohol
BioCyc IDCPD-7032

Enzymes

General function:
Involved in zinc ion binding
Specific function:
An alcohol + NAD(+) = an aldehyde or ketone + NADH
Gene Name:
ADH3
Uniprot ID:
P07246
Molecular weight:
40369.19922
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in zinc ion binding
Specific function:
Oxidizes long-chain alcohols and, in the presence of glutathione, is able to oxidize formaldehyde. Is responsible for yeast resistance to formaldehyde
Gene Name:
SFA1
Uniprot ID:
P32771
Molecular weight:
41041.69922
Reactions
S-(hydroxymethyl)glutathione + NAD(P)(+) → S-formylglutathione + NAD(P)H.
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in zinc ion binding
Specific function:
This isozyme preferentially catalyzes the conversion of primary unbranched alcohols to their corresponding aldehydes. Also also shows activity toward secondary alcohols
Gene Name:
ADH1
Uniprot ID:
P00330
Molecular weight:
36849.0
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in oxidoreductase activity
Specific function:
Reduces acetaldehyde to ethanol during glucose fermentation. Specific for ethanol. Shows drastically reduced activity towards primary alcohols from 4 carbon atoms upward. Isomers of aliphatic alcohol, as well as secondary alcohols and glycerol are not used at all
Gene Name:
ADH4
Uniprot ID:
P10127
Molecular weight:
41141.69922
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in zinc ion binding
Specific function:
An alcohol + NAD(+) = an aldehyde or ketone + NADH
Gene Name:
ADH5
Uniprot ID:
P38113
Molecular weight:
37647.89844
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in zinc ion binding
Specific function:
This isozyme preferentially catalyzes the conversion of ethanol to acetaldehyde. Acts on a variety of primary unbranched aliphatic alcohols
Gene Name:
ADH2
Uniprot ID:
P00331
Molecular weight:
36731.60156
Reactions
An alcohol + NAD(+) → an aldehyde or ketone + NADH.
General function:
Involved in carboxylesterase activity
Specific function:
Displays enzymatic activity both for medium-chain fatty acid (MCFA) ethyl ester synthesis and hydrolysis (esterase activity). MCFA are toxic for yeast and this enzyme could thus be involved in their detoxification by esterification
Gene Name:
EHT1
Uniprot ID:
P38295
Molecular weight:
51254.80078
Reactions
Acetyl-CoA + an alcohol → CoA + an acetyl ester.
General function:
Involved in alcohol O-acetyltransferase activity
Specific function:
Catalyzes the esterification of isoamyl alcohol and various other alcohols by acetyl-CoA
Gene Name:
ATF1
Uniprot ID:
P40353
Molecular weight:
61035.5
Reactions
Acetyl-CoA + an alcohol → CoA + an acetyl ester.
General function:
Involved in carboxylesterase activity
Specific function:
Displays enzymatic activity both for medium-chain fatty acid (MCFA) ethyl ester synthesis and hydrolysis (esterase activity). MCFA are toxic for yeast and this enzyme could thus be involved in their detoxification by esterification
Gene Name:
EEB1
Uniprot ID:
Q02891
Molecular weight:
51723.19922
Reactions
Acetyl-CoA + an alcohol → CoA + an acetyl ester.
General function:
Involved in alcohol O-acetyltransferase activity
Specific function:
Acetyl-CoA + an alcohol = CoA + an acetyl ester
Gene Name:
ATF2
Uniprot ID:
P53296
Molecular weight:
61897.5
Reactions
Acetyl-CoA + an alcohol → CoA + an acetyl ester.
General function:
Involved in catalytic activity
Specific function:
Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG) to (R)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation
Gene Name:
GRE2
Uniprot ID:
Q12068
Molecular weight:
38169.19922
Reactions
Lactaldehyde + NADP(+) → methylglyoxal + NADPH.
3-methylbutanol + NAD(P)+ → 3-methylbutanal + NAD(P)H + H+
General function:
Involved in zinc ion binding
Specific function:
NADP-dependent alcohol dehydrogenase with a broad substrate specificity
Gene Name:
ADH7
Uniprot ID:
P25377
Molecular weight:
39348.19922
Reactions
An alcohol + NADP(+) → an aldehyde + NADPH.
General function:
Involved in enzyme regulator activity
Specific function:
Required for calcium regulation. May regulate calcium accumulation by a non-vacuole organelle. Also regulates the activity of CSH1 and SUR1 during mannosyl phosphorylinositol ceramide synthesis
Gene Name:
CSG2
Uniprot ID:
P35206
Molecular weight:
45441.60156
Reactions
General function:
Involved in zinc ion binding
Specific function:
NADP-dependent alcohol dehydrogenase with a broad substrate specificity
Gene Name:
ADH6
Uniprot ID:
Q04894
Molecular weight:
39617.30078
Reactions
An alcohol + NADP(+) → an aldehyde + NADPH.
General function:
Involved in hydrolase activity
Specific function:
Plays a crucial role in the hydrolysis of isoamyl acetate in sake mash
Gene Name:
IAH1
Uniprot ID:
P41734
Molecular weight:
27346.0
Reactions