Linked Life Data

3170573

Source:http://linkedlifedata.com/resource/pubmed/id/3170573

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1988-11-10
pubmed:abstractText
TDP-D-glucose 4,6-dehydratase was purified from Saccharopolyspora erythraea, the producer of the macrolide antibiotic erythromycin A, by a high resolution chromatographic method that exploited the difference in the behavior of the protein on anionic exchange chromatography in Tris/HCl or phosphate buffers. By this method, the enzyme was purified approximately 900-fold by two anionic exchange steps to more than 90% homogeneity. It was further purified to apparent homogeneity by hydrophobic interaction chromatography. The enzyme is a homodimer of Mr 36,000 subunits, is highly specific for TDP-D-glucose, requires NAD+ as cofactor, and shows a K'm of 34 microM and V'max of 26 mumol h-1 mg-1 of protein for TDP-D-glucose. TDP and TTP strongly inhibit the enzyme at 2 mM. The maximal TDP-D-glucose 4,6-dehydratase activity coincides with the time of erythromycin production, suggesting that this enzyme is involved in antibiotic biosynthesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
14992-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Purification of thymidine-diphospho-D-glucose 4,6-dehydratase from an erythromycin-producing strain of Saccharopolyspora erythraea by high resolution liquid chromatography.
pubmed:affiliation
School of Pharmacy, University of Wisconsin, Madison 53706.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't