Linked Life Data

6817787

Source:http://linkedlifedata.com/resource/pubmed/id/6817787

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
25
pubmed:dateCreated
1983-3-24
pubmed:abstractText
The structural requirements for the donor pyranosyl moiety of UDP-Gal in either galactosyl transfer or "lactose" biosynthesis have been determined. The 4"-deoxy analogue, UDP-4"-deoxyglucose, was synthesized and fully characterized as a donor substrate for galactosyltransferase. The relative rate of deoxyglucosyl transfer to glucose or GlcNAc acceptors was 5.5 +/- 0.6% of that of UDP-Gal as the substrate, with Km values in the same range as that for UDP-Gal or UDP-Glc. Several conclusions may be drawn as to the detailed structural requirements of the UDP-Gal binding site: an axial 4"-hydroxyl group on the pyranosyl moiety is necessary for precise substrate alignment as is also an equatorial 6"-CH2OH moiety. Where one or the other moiety was lacking (UDP-dGlc or UDP-Arab), the maximal rate of glycosyl transfer was ca. 1/20th that of UDP-Gal.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
7
pubmed:volume
21
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6340-3
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Structure-function relationships in lactose synthase. Structural requirements of the uridine 5'-diphosphate galactose binding site.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.