L-Lactate dehydrogenase from Cyanidioschyzon merolae shows high catalytic efficiency for pyruvate reduction and is inhibited by ATP.
Cyanidioschyzon merolae
l-Lactate dehydrogenase
Catalytic efficiency
Lactic fermentation
Journal
Plant molecular biology
ISSN: 1573-5028
Titre abrégé: Plant Mol Biol
Pays: Netherlands
ID NLM: 9106343
Informations de publication
Date de publication:
10 Sep 2024
10 Sep 2024
Historique:
received:
05
09
2023
accepted:
21
08
2024
medline:
10
9
2024
pubmed:
10
9
2024
entrez:
10
9
2024
Statut:
epublish
Résumé
L-Lactate is a commodity chemical used in various fields. Microorganisms have produced L-lactate via lactic fermentation using saccharides derived from crops as carbon sources. Recently, L-lactate production using microalgae, whose carbon source is carbon dioxide, has been spotlighted because the prices of the crops have increased. A red alga Cyanidioschyzon merolae produce L-lactate via lactic fermentation under dark anaerobic conditions. The L-lactate titer of C. merolae is higher than those of other microalgae but lower than those of heterotrophic bacteria. Therefore, an increase in the L-lactate titer is required in C. merolae. L-Lactate dehydrogenase (L-LDH) catalyzes the reduction of pyruvate to L-lactate during lactic fermentation. C. merolae possesses five isozymes of L-LDH. The results of previous transcriptome analysis suggested that L-LDHs are the key enzymes in the lactic fermentation of C. merolae. However, their biochemical characteristics, such as catalytic efficiency and tolerance for metabolites, have not been revealed. We compared the amino acid sequences of C. merolae L-LDHs (CmLDHs) and characterized one of the isozymes, CmLDH1. BLAST analysis revealed that the sequence similarities of CmLDH1 and the other isozymes were above 99%. The catalytic efficiency of CmLDH1 under its optimum conditions was higher than those of L-LDHs of other organisms. ATP decreased the affinity and turnover number of CmLDH1 for NADH. These findings contribute to understanding the characteristics of L-LDHs of microalgae and the regulatory mechanisms of lactic fermentation in C. merolae.
Identifiants
pubmed: 39254882
doi: 10.1007/s11103-024-01495-0
pii: 10.1007/s11103-024-01495-0
doi:
Substances chimiques
L-Lactate Dehydrogenase
EC 1.1.1.27
Pyruvic Acid
8558G7RUTR
Adenosine Triphosphate
8L70Q75FXE
Lactic Acid
33X04XA5AT
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
98Subventions
Organisme : Japan Society for the Promotion of Science
ID : 20H02905
Organisme : Advanced Low Carbon Technology Research and Development Program
ID : JPMJAL1306
Informations de copyright
© 2024. The Author(s).
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