Linked Life Data

9090109

Source:http://linkedlifedata.com/resource/pubmed/id/9090109

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-5-5
pubmed:abstractText
2,4-Dichlorophenol hydroxylase (DCP-hydroxylase) is a key enzyme in the pathway for degradation of 2,4-dichlorophenoxyacetic acid (2,4-D) in many bacteria. In Alcaligenes eutrophus JMP134, DCP-hydroxylase was reported to consist of two dissimilar types of subunit of 66 and 45 kDa, a structure which is different from that in other bacteria. Using a different procedure involving affinity purification and ion-exchange chromatography, we have purified active enzyme from JMP134 and show that it has a native molecular mass of approximately 245 kDa and consists of a single type of subunit of 66 kDa, similar to all other flavoprotein monooxygenase enzymes. A 45-kDa polypeptide, found in partially purified enzyme preparations, was not required for enzyme activity but had some serologic and N-terminal amino acid sequence similarity to the 66-kDa enzyme subunit.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0008-4166
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
202-5
pubmed:dateRevised
2002-11-1
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
The 2,4-dichlorophenol hydroxylase of Alcaligenes eutrophus JMP134 is a homotetramer.
pubmed:affiliation
Department of Microbiology, University of Sydney, N.S.W., Australia.
pubmed:publicationType
Journal Article