Linked Life Data

3122838

Source:http://linkedlifedata.com/resource/pubmed/id/3122838

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1988-3-21
pubmed:abstractText
A bromoperoxidase was isolated from the chlortetracycline-producing actinomycete, Streptomyces aureofaciens. This enzyme catalysed bromination and iodination, but surprisingly did not catalyse chlorination. The enzyme had an acidic pH optimum (pH 4.3) and the isoelectric point was 3.5. The Km for bromide was 20 mM and the Km for H2O2 was as high as 8 mM. The bromoperoxidase did not contain haem, since it was not inhibited by azide or cyanide. Excess bromide or chloride had no effect on its brominating activity; however, fluoride strongly inhibited the bromoperoxidase (Ki = 20 microM). On the basis of gel electrophoresis in the absence and presence of sodium dodecyl sulphate, the molecular mass of the enzyme was 65 kDa and it consisted of two subunits of 32 kDa each. The bromoperoxidase was remarkably thermostable.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
952
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
255-60
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Purification and some characteristics of a non-haem bromoperoxidase from Streptomyces aureofaciens.
pubmed:affiliation
Laboratory of Biochemistry, University of Amsterdam, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't