TY - JOUR
T1 - Review of Mutarotase in 'Metabolic Subculture' and Analytical Biochemistry
T2 - Prelude to 19F NMR Studies of its Substrate Specificity and Mechanism
AU - Shishmarev, Dmitry
AU - Quiquempoix, Lucas
AU - Fontenelle, Clément Q.
AU - Linclau, Bruno
AU - Kuchel, Philip W.
N1 - Publisher Copyright:
© 2020 CSIRO.
PY - 2020/3
Y1 - 2020/3
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85183486249&partnerID=8YFLogxK
U2 - 10.1071/CH19397
DO - 10.1071/CH19397
M3 - Article
SN - 0004-9425
VL - 73
SP - 112
EP - 116
JO - Australian Journal of Chemistry
JF - Australian Journal of Chemistry
IS - 3
ER -