Review of mutarotase in ‘Metabolic Subculture’ and analytical biochemistry: prelude to 19F NMR studies of its substrate specificity and mechanism
Review of mutarotase in ‘Metabolic Subculture’ and analytical biochemistry: prelude to 19F NMR studies of its substrate specificity and mechanism
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.
Enzyme mechanism, metabolic subculture, mutarotase, nuclear magnetic resonance, red blood cell
112-116
Shishmarev, Dmitry
11bac3f9-42c3-42ba-b3d1-e5fc06365580
Quiquempoix, Lucas G
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Fontenelle, Clement Q
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Linclau, Bruno
19b9cacd-b8e8-4c65-af36-6352cade84ba
Kuchel, Philip W.
62f434b1-d370-4552-85f4-05b76c625945
10 February 2020
Shishmarev, Dmitry
11bac3f9-42c3-42ba-b3d1-e5fc06365580
Quiquempoix, Lucas G
1664af14-ee65-4888-884b-5331983a25ba
Fontenelle, Clement Q
c746c5ea-96bc-46c2-849d-47215ab58c03
Linclau, Bruno
19b9cacd-b8e8-4c65-af36-6352cade84ba
Kuchel, Philip W.
62f434b1-d370-4552-85f4-05b76c625945
Shishmarev, Dmitry, Quiquempoix, Lucas G, Fontenelle, Clement Q, Linclau, Bruno and Kuchel, Philip W.
(2020)
Review of mutarotase in ‘Metabolic Subculture’ and analytical biochemistry: prelude to 19F NMR studies of its substrate specificity and mechanism.
Australian Journal of Chemistry, .
(doi:10.1071/CH19397).
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.
Text
Mutarotase paper 1 FINAL_PWK
- Accepted Manuscript
More information
Accepted/In Press date: 4 December 2019
e-pub ahead of print date: 10 February 2020
Published date: 10 February 2020
Additional Information:
Publisher Copyright:
© 2020 CSIRO.
Keywords:
Enzyme mechanism, metabolic subculture, mutarotase, nuclear magnetic resonance, red blood cell
Identifiers
Local EPrints ID: 436364
URI: http://eprints.soton.ac.uk/id/eprint/436364
ISSN: 0004-9425
PURE UUID: 7c93c05b-4869-4d3b-b3c1-27c3eb592459
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Date deposited: 09 Dec 2019 17:30
Last modified: 17 Mar 2024 02:51
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Contributors
Author:
Dmitry Shishmarev
Author:
Lucas G Quiquempoix
Author:
Clement Q Fontenelle
Author:
Philip W. Kuchel
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