Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-2-20
pubmed:abstractText
Vanillyl-alcohol oxidase (EC 1.1.3.7) from Penicillium simplicissimum was modified with p-mercuribenzoate. One cysteine residue reacts rapidly without loss of enzyme activity. Three sulfhydryl groups then react in an 'all or none process' involving enzyme inactivation and dissociation of the octamer into dimers. The inactivation reaction is slowed down in the presence of the competitive inhibitor isoeugenol and fully reversible by treatment of the modified enzyme with dithiothreitol. Vanillyl-alcohol oxidase is more rapidly inactivated at low enzyme concentrations and protected from mercuration by antichaotropic salts. It is proposed that subunit dissociation accounts for the observed sensitivity of vanillyl-alcohol oxidase crystals towards mercury compounds.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
402
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
33-5
pubmed:dateRevised
2010-10-13
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Mercuration of vanillyl-alcohol oxidase from Penicillium simplicissimum generates inactive dimers.
pubmed:affiliation
Department of Biochemistry, Agricultural University, Wageningen, The Netherlands.
pubmed:publicationType
Journal Article