Kenneth E. Hammel
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Kenneth E. Hammel has a total of 3 co-authors. Here are the top co-authors by number of shared publications:
Kathryn M. C. Evans
Forest Products Laboratory, U.S. Department of Agriculture, Madison, Wisconsin 53705
1 shared publicationKenneth A. Jensen
Forest Products Laboratory, U.S. Department of Agriculture, Madison, Wisconsin 53705
1 shared publicationT. Kent Kirk
Forest Products Laboratory, U.S. Department of Agriculture, Madison, Wisconsin 53705
1 shared publication
Latest Publications
- 1 February 1994
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 60 (2) , 709-714
Biosynthetic Pathway for Veratryl Alcohol in the Ligninolytic Fungus Phanerochaete chrysosporium
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 14 C-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 14 C. These results support a pathway in which VA biosynthesis proceeds as follows: phenylalanine → cinnamate → benzoate and/or benzaldehyde → VA.
- 1 February 1994
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 60 (2) , 709-714
Biosynthetic Pathway for Veratryl Alcohol in the Ligninolytic Fungus Phanerochaete chrysosporium
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 14 C-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 14 C. These results support a pathway in which VA biosynthesis proceeds as follows: phenylalanine → cinnamate → benzoate and/or benzaldehyde → VA.