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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
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, amongst 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 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
0004-9425
112-116
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
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, 112-116. (doi:10.1071/CH19397).

Record type: Article

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, amongst 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 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.

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Mutarotase paper 1 FINAL_PWK - Accepted Manuscript
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More information

Accepted/In Press date: 4 December 2019
e-pub ahead of print date: 10 February 2020
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
ORCID for Clement Q Fontenelle: ORCID iD orcid.org/0000-0002-1630-3407
ORCID for Bruno Linclau: ORCID iD orcid.org/0000-0001-8762-0170

Catalogue record

Date deposited: 09 Dec 2019 17:30
Last modified: 26 Nov 2021 02:43

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Contributors

Author: Dmitry Shishmarev
Author: Lucas G Quiquempoix
Author: Clement Q Fontenelle ORCID iD
Author: Bruno Linclau ORCID iD
Author: Philip W. Kuchel

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