Skip to main content
Applied and Environmental Microbiology logoLink to Applied and Environmental Microbiology
. 1994 Feb;60(2):709–714. doi: 10.1128/aem.60.2.709-714.1994

Biosynthetic Pathway for Veratryl Alcohol in the Ligninolytic Fungus Phanerochaete chrysosporium

Kenneth A Jensen Jr 1, Kathryn M C Evans 1, T Kent Kirk 1, Kenneth E Hammel 1,*
PMCID: PMC201370  PMID: 16349197

Abstract

Veratryl alcohol (VA) is a secondary metabolite of white-rot fungi that produce the ligninolytic enzyme lignin peroxidase. VA stabilizes lignin peroxidase, promotes the ability of this enzyme to oxidize a variety of physiological substrates, and is accordingly thought to play a significant role in fungal ligninolysis. Pulse-labeling and isotope-trapping experiments have now clarified the pathway for VA biosynthesis in the white-rot basidiomycete Phanerochaete chrysosporium. The pulse-labeling data, obtained with 14C-labeled phenylalanine, cinnamic acid, benzoic acid, and benzaldehyde, showed that radiocarbon labeling followed a reproducible sequence: it peaked first in cinnamate, then in benzoate and benzaldehyde, and finally in VA. Phenylalanine, cinnamate, benzoate, and benzaldehyde were all efficient precursors of VA in vivo. The isotope-trapping experiments showed that exogenous, unlabeled benzoate and benzaldehyde were effective traps of phenylalanine-derived 14C. These results support a pathway in which VA biosynthesis proceeds as follows: phenylalanine → cinnamate → benzoate and/or benzaldehyde → VA.

Full text

PDF
709

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Akamatsu Y., Ma D. B., Higuchi T., Shimada M. A novel enzymatic decarboxylation of oxalic acid by the lignin peroxidase system of white-rot fungus Phanerochaete chrysosporium. FEBS Lett. 1990 Aug 20;269(1):261–263. doi: 10.1016/0014-5793(90)81169-o. [DOI] [PubMed] [Google Scholar]
  2. Coulter C., Hamilton J. T., Harper D. B. Evidence for the existence of independent chloromethane- and S-adenosylmethionine-utilizing systems for methylation in Phanerochaete chrysosporium. Appl Environ Microbiol. 1993 May;59(5):1461–1466. doi: 10.1128/aem.59.5.1461-1466.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Coulter C., Kennedy J. T., McRoberts W. C., Harper D. B. Purification and Properties of an S-Adenosylmethionine: 2,4-Disubstituted Phenol O-Methyltransferase from Phanerochaete chrysosporium. Appl Environ Microbiol. 1993 Mar;59(3):706–711. doi: 10.1128/aem.59.3.706-711.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Edwards S. L., Raag R., Wariishi H., Gold M. H., Poulos T. L. Crystal structure of lignin peroxidase. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):750–754. doi: 10.1073/pnas.90.2.750. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Faison B. D., Kirk T. K., Farrell R. L. Role of Veratryl Alcohol in Regulating Ligninase Activity in Phanerochaete chrysosporium. Appl Environ Microbiol. 1986 Aug;52(2):251–254. doi: 10.1128/aem.52.2.251-254.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Gold M. H., Kuwahara M., Chiu A. A., Glenn J. K. Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the white rot basidiomycete, Phanerochaete chrysosporium. Arch Biochem Biophys. 1984 Nov 1;234(2):353–362. doi: 10.1016/0003-9861(84)90280-7. [DOI] [PubMed] [Google Scholar]
  7. Haemmerli S. D., Leisola M. S., Sanglard D., Fiechter A. Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase. J Biol Chem. 1986 May 25;261(15):6900–6903. [PubMed] [Google Scholar]
  8. Hammel K. E., Jensen K. A., Jr, Mozuch M. D., Landucci L. L., Tien M., Pease E. A. Ligninolysis by a purified lignin peroxidase. J Biol Chem. 1993 Jun 15;268(17):12274–12281. [PubMed] [Google Scholar]
  9. Hammel K. E., Jensen K. A., Jr, Mozuch M. D., Landucci L. L., Tien M., Pease E. A. Ligninolysis by a purified lignin peroxidase. J Biol Chem. 1993 Jun 15;268(17):12274–12281. [PubMed] [Google Scholar]
  10. Harper D. B., Buswell J. A., Kennedy J. T., Hamilton J. T. Chloromethane, Methyl Donor in Veratryl Alcohol Biosynthesis in Phanerochaete chrysosporium and Other Lignin-Degrading Fungi. Appl Environ Microbiol. 1990 Nov;56(11):3450–3457. doi: 10.1128/aem.56.11.3450-3457.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Jäger A., Croan S., Kirk T. K. Production of Ligninases and Degradation of Lignin in Agitated Submerged Cultures of Phanerochaete chrysosporium. Appl Environ Microbiol. 1985 Nov;50(5):1274–1278. doi: 10.1128/aem.50.5.1274-1278.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Kirk T. K., Farrell R. L. Enzymatic "combustion": the microbial degradation of lignin. Annu Rev Microbiol. 1987;41:465–505. doi: 10.1146/annurev.mi.41.100187.002341. [DOI] [PubMed] [Google Scholar]
  13. Paszczynski A., Crawford R. L. Degradation of azo compounds by ligninase from Phanerochaete chrysosporium: involvement of veratryl alcohol. Biochem Biophys Res Commun. 1991 Aug 15;178(3):1056–1063. doi: 10.1016/0006-291x(91)90999-n. [DOI] [PubMed] [Google Scholar]
  14. Piontek K., Glumoff T., Winterhalter K. Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution. FEBS Lett. 1993 Jan 4;315(2):119–124. doi: 10.1016/0014-5793(93)81146-q. [DOI] [PubMed] [Google Scholar]
  15. Popp J. L., Kalyanaraman B., Kirk T. K. Lignin peroxidase oxidation of Mn2+ in the presence of veratryl alcohol, malonic or oxalic acid, and oxygen. Biochemistry. 1990 Nov 20;29(46):10475–10480. doi: 10.1021/bi00498a008. [DOI] [PubMed] [Google Scholar]
  16. Périé F. H., Gold M. H. Manganese regulation of manganese peroxidase expression and lignin degradation by the white rot fungus Dichomitus squalens. Appl Environ Microbiol. 1991 Aug;57(8):2240–2245. doi: 10.1128/aem.57.8.2240-2245.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Rüttimann-Johnson C., Salas L., Vicuña R., Kirk T. K. Extracellular Enzyme Production and Synthetic Lignin Mineralization by Ceriporiopsis subvermispora. Appl Environ Microbiol. 1993 Jun;59(6):1792–1797. doi: 10.1128/aem.59.6.1792-1797.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Tien M., Kirk T. K., Bull C., Fee J. A. Steady-state and transient-state kinetic studies on the oxidation of 3,4-dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerocheate chrysosporium Burds. J Biol Chem. 1986 Feb 5;261(4):1687–1693. [PubMed] [Google Scholar]
  19. Wariishi H., Valli K., Gold M. H. In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium. Biochem Biophys Res Commun. 1991 Apr 15;176(1):269–275. doi: 10.1016/0006-291x(91)90919-x. [DOI] [PubMed] [Google Scholar]

Articles from Applied and Environmental Microbiology are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES