Purification and properties of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium
Details
Serval ID
serval:BIB_0734BEE9F44A
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Purification and properties of an aryl-alcohol dehydrogenase from the white-rot fungus Phanerochaete chrysosporium
Journal
European Journal of Biochemistry
ISSN
0014-2956 (Print)
Publication state
Published
Issued date
01/1991
Volume
195
Number
2
Pages
369-75
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jan 30
Research Support, Non-U.S. Gov't --- Old month value: Jan 30
Abstract
An intracellular aryl-alcohol dehydrogenase (previously referred to as aryl-aldehyde reductase) was purified from the white-rot fungus Phanerochaete chrysosporium. The enzyme reduced veratraldehyde to veratryl alcohol using NADPH as a cofactor. Other aromatic benzaldehydes were also reduced, but not aromatic ketones. Methoxy-substituted rings were better substrates than hydroxylated ones. The enzyme was also able to reduce a dimeric aldehyde (4-benzyloxy-3-methoxybenzaldehyde). The highest reduction rate was measured when 3,5-dimethoxybenzaldehyde was used as a substrate. On SDS/PAGE the purified enzyme showed one major band with a molecular mass of 47 kDa, whereas gel filtration suggested a molecular mass of 280 kDa. Polyclonal antibodies raised against the gel purified 47-kDa protein were able to immunoprecipitate the aryl-alcohol dehydrogenase indicating that its activity possibly resides entirely in this protein fragment. The pI of the enzyme was 5.2 and it was most active at pH 6.1. The aryl-alcohol dehydrogenase was partially inhibited by typical oxidoreductase inhibitors.
Keywords
Alcohol Oxidoreductases/*chemistry/isolation & purification
Aldehydes/metabolism
Benzyl Alcohols/metabolism
Electrophoresis, Polyacrylamide Gel
Enzyme Stability
Fungi/drug effects/*enzymology
Hydrogen-Ion Concentration
Lignin/metabolism
Molecular Weight
NADP/metabolism
Protein Synthesis Inhibitors/pharmacology
Substrate Specificity
Pubmed
Web of science
Open Access
Yes
Create date
25/01/2008 14:40
Last modification date
20/08/2019 12:29