Biology:Long-chain-alcohol oxidase

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long-chain-alcohol oxidase
Identifiers
EC number1.1.3.20
CAS number129430-50-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

Long-chain alcohol oxidase is one of two enzyme classes that oxidize long-chain or fatty alcohols to aldehydes. It has been found in certain Candida yeast, where it participates in omega oxidation of fatty acids to produce acyl-CoA for energy or industrial use, as well as in other fungi, plants, and bacteria.[1]

Mechanism

Long-chain alcohol oxidase catalyzes the chemical reaction
long-chain alcohol + O2 [math]\displaystyle{ \rightleftharpoons }[/math] 2 long-chain aldehyde + 2 H2O2
Thus, the two substrates of this enzyme are long-chain/fatty alcohol and O2, whereas its two products are long-chain/fatty aldehyde and hydrogen peroxide.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with oxygen as acceptor. The systematic name of this enzyme class is long-chain-alcohol:oxygen oxidoreductase. Other names in common use include long-chain fatty alcohol oxidase, fatty alcohol oxidase, fatty alcohol:oxygen oxidoreductase, and long-chain fatty acid oxidase.[2]

Structure

The enzyme is an octamer of ~46kD subunits[3] (except in C. tropicalis, in which it is a dimer of subunits ~70kD).[4] It is a Cytochrome c oxidase containing a covalently-bound heme group using the Cys-X-X-Cys-His motif. It also contains flavin to assist in oxidation-reduction. The enzyme is bound to the endoplasmic reticulum membrane.[5]

Long-chain fatty alcohol oxidases vary between species in their specificity; some species have multiple different alcohol oxidases. They generally have a broad range of substrates, ranging from short chain alcohols starting at 4 carbons to the longest long-chain alcohols at 22 carbons. Some can also oxidize select diols, secondary alcohols, hydroxy fatty acids, and even long-chain aldehydes.[4] However, each enzyme is optimized to function for specific alcohol, often between 10 and 16 carbons. In at least one species, the enzyme was stereoselective for the R(-) entantiomer.[6]

The long-chain alkane/omega-oxidation pathway, from alkane to carboxylic acid.

Function

This enzyme can be induced in many Candida yeast strains[5] by growing them on long-chain alkanes as the major food source.[4] Long-chain fatty alcohol oxidases participate in omega-oxidation of long chain alkanes or fatty acids. The alkane is first oxidized to an alcohol by an enzyme of the Cytochrome P450 family using NADPH. This alcohol is oxidized by long-chain fatty alcohol oxidase in yeast.[5]

(This is different from the pathway found in mammalian tissues, which employs long-chain fatty alcohol dehydrogenase or fatty alcohol:NAD+ oxidoreductase and requires NAD+.[7] Yeast have low levels of fatty alcohol dehydrogenase.[4])

The long-chain alcohol is then oxidized by long-chain fatty aldehyde dehydrogenase to a carboxylic acid, also producing NADH from NAD+. Fatty acids can be oxidized again to make dicarboxylic species that join with coenzyme A and enter the beta oxidation pathway in the peroxisome.[5]

Long-chain alcohol oxidase is also used in germinating seedlings of jojoba (Simmondsia chinensis) to degrade esterified long-chain fatty alcohols stored as wax.[8]

Species

This enzyme has been found in the following organisms:[2]

Yeast

Candida cloacae
Candida tropicalis
Starmerella bombicola
Yarrowia lipolytica

Other Fungi

Aspergillus terreus
Mucor circinelloides

Plants

Arabidopsis thaliana (thale cress)
Lotus japonicus
Simmondsia chinensis (jojoba)
Tanacetum vulgare (common tansy)

Archaea

Uncultured marine euryarchaeota[9]

Industrial use

This enzyme is required for production of dicarboxylic acids by industrial Candida yeast, which have nonfunctional beta oxidation pathways. They can thus produce relatively pure saturated and unsaturated dicarboxylic acids in high yield, which is not possible using chemical synthesis. The dicarboxylic acids are used to produce fragrances, polyamides, polyesters, adhesives, and antibiotics.[10]

References

  1. ↑ "A consensus sequence for long-chain fatty-acid alcohol oxidases from Candida identifies a family of genes involved in lipid omega-oxidation in yeast with homologues in plants and bacteria". The Journal of Biological Chemistry 275 (6): 4445–52. February 2000. doi:10.1074/jbc.275.6.4445. PMID 10660617. 
  2. ↑ 2.0 2.1 Brenda Enzymes Database[full citation needed]
  3. ↑ "Intracellular distribution of fatty alcohol oxidase activity in Mucor circinelloides YR-1 isolated from petroleum contaminated soils". Antonie van Leeuwenhoek 96 (4): 527–35. November 2009. doi:10.1007/s10482-009-9368-x. PMID 19642009. 
  4. ↑ 4.0 4.1 4.2 4.3 "Purification and some properties of alcohol oxidase from alkane-grown Candida tropicalis". The Biochemical Journal 282 ( Pt 2) (2): 325–31. March 1992. doi:10.1042/bj2820325. PMID 1546949. 
  5. ↑ 5.0 5.1 5.2 5.3 "Candida yeast long chain fatty alcohol oxidase is a c-type haemoprotein and plays an important role in long chain fatty acid metabolism". Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids 1735 (3): 192–203. August 2005. doi:10.1016/j.bbalip.2005.06.006. PMID 16046182. 
  6. ↑ Mauersberger, Stephan; Drechsler, Hannelore; Oehme, Günther; Müller, Hans-Georg (1992). "Substrate specificity and stereoselectivity of fatty alcohol oxidase from the yeast Candida maltosa". Applied Microbiology and Biotechnology 37. doi:10.1007/BF00174205. 
  7. ↑ "Characterization of fatty alcohol:NAD+ oxidoreductase from rat liver". The Journal of Biological Chemistry 254 (8): 2892–6. April 1979. doi:10.1016/S0021-9258(17)30157-6. PMID 34610. 
  8. ↑ "Oxidation of fatty alcohol in the cotyledons of jojoba seedlings". Archives of Biochemistry and Biophysics 194 (2): 422–30. May 1979. doi:10.1016/0003-9861(79)90636-2. PMID 36040. 
  9. ↑ "Discovery of two novel oxidases using a high-throughput activity screen". ChemBioChem 23 (2): e202100510. 2021. doi:10.1002/cbic.202100510. PMID 34709726. 
  10. ↑ "[Non-steroid inhibitors of the adrenal cortex]". La Clinica Terapeutica 20: 667–79. June 1961. PMID 13689840. 



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