Cultural advice

The Australian National University acknowledges, celebrates and pays our respects to the Ngunnawal and Ngambri people of the Canberra region and to all First Nations Australians on whose traditional lands we meet and work, and whose cultures are among the oldest continuing cultures in human history.

Aboriginal and Torres Strait Islander peoples are advised that ANU Library collections may include images, names, voices, and other representations of deceased persons.

Material in the collection may contain terms, language or views that reflect the period in which the item was created and may be considered inappropriate today.

Review of Mutarotase in 'Metabolic Subculture' and Analytical Biochemistry: Prelude to 19F NMR Studies of its Substrate Specificity and Mechanism

Loading...
Thumbnail Image

Date

Authors

Shishmarev, Dmitry
Quiquempoix, Lucas
Fontenelle, Clement Q
Linclau, Bruno
Kuchel, Philip William

Journal Title

Journal ISSN

Volume Title

Publisher

CSIRO Publishing

Abstract

This is the first paper in a sequential pair devoted to the enzyme mutarotase (aldose 1-epimerase; EC 5.1.3.3). Here, the broader context of the physiological role of mutarotase, among those enzymes considered to be part of ‘metabolic structure’, is reviewed. We also summarise the current knowledge about the molecular mechanism and substrate specificity of the enzyme, which is considered in the context of the binding of fluorinated glucose analogues to the enzyme’s active site. This was done as a prelude to our experimental studies of the anomerisation of fluorinated sugars by mutarotase that are described in the following paper.

Description

Keywords

Citation

Source

Australian Journal of Chemistry

Book Title

Entity type

Access Statement

License Rights

Restricted until

2099-12-31
abcd