- Abstract:
-
BACKGROUND: The regulation of milk lactose biosynthesis is highly dependent on the action of a specifier protein, alpha-lactalbumin (LA). Together with a glycosyltransferase, LA forms the enzyme complex lactose synthase. LA promotes the binding of glucose to the complex and facilitates the biosynthesis of lactose. To gain further insight into the molecular basis of LA function in lactose synthase we have determined the structures of three species variants of LA. RESULTS: The crystal structure...
Expand abstract - Publication status:
- Published
- Journal:
- Structure (London, England : 1993)
- Volume:
- 4
- Issue:
- 6
- Pages:
- 691-703
- Publication date:
- 1996-06-05
- DOI:
- EISSN:
-
1878-4186
- ISSN:
-
0969-2126
- URN:
-
uuid:2a760330-ba70-4062-9714-c5b61df9768e
- Source identifiers:
-
317566
- Local pid:
- pubs:317566
- Language:
- English
- Keywords:
- Copyright date:
- 1996
Journal article
Crystal structures of guinea-pig, goat and bovine alpha-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase.
Actions
Authors
Bibliographic Details
Item Description
Terms of use
Metrics
Altmetrics
Dimensions
If you are the owner of this record, you can report an update to it here: Report update to this record