Inhibition of Pyruvate Kinase From Thermoanaerobacterium saccharolyticum by IMP Is Independent of the Extra-C Domain

The pyruvate kinase (PYK) isozyme from (TsPYK) has previously been used in metabolic engineering for improved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated...

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Bibliographic Details
Published in:Frontiers in microbiology 2021-02, Vol.12, p.628308-628308
Main Authors: Fenton, Christopher A, Tang, Qingling, Olson, Daniel G, Maloney, Marybeth I, Bose, Jeffrey L, Lynd, Lee R, Fenton, Aron W
Format: Article
Language:English
Subjects:
allosteric regulation
allostery
BASIC BIOLOGICAL SCIENCES
ethanol
metabolic engineering
Microbiology
pyruvate kinase
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Summary:The pyruvate kinase (PYK) isozyme from (TsPYK) has previously been used in metabolic engineering for improved ethanol production. This isozyme belongs to a subclass of PYK isozymes that include an extra C-domain. Like other isozymes that include this extra C-domain, we found that TsPYK is activated by AMP and ribose-5-phosphate (R5P). Our use of sugar-phosphate analogs generated a surprising result in that IMP and GMP are allosteric inhibitors (rather than activators) of TsPYK. We believe this to be the first report of any PYK isozyme being inhibited by IMP and GMP. A truncated protein that lacks the extra C-domain is also inhibited by IMP. A screen of several other bacterial PYK enzymes (include several that have the extra-C domain) indicates that the inhibition by IMP is specific to only a subset of those isozymes.
ISSN:1664-302X
1664-302X
DOI:10.3389/fmicb.2021.628308