ArticleScientific reports2017
Substrate Specificity and Allosteric Regulation of a D-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Enhanced fumarate production using high-density cultivation of Synechocystis sp. PCC 6803.Microbial cell factories · 2026Article
- Pyruvate kinase 2 from Synechocystis sp. PCC 6803 increased substrate affinity via glucose-6-phosphate and ribose-5-phosphate for phosphoenolpyruvate consumption.Plant molecular biology · 2024Article
- Regulation of organic acid and hydrogen production by NADH/NADFrontiers in microbiology · 2023Article
- Structure, Function, and Thermodynamics of Lactate Dehydrogenases from Humans and the Malaria ParasiteBiochemistry · 2021Article
- Article
- Biochemical characterisation of fumarase C from a unicellular cyanobacterium demonstrating its substrate affinity, altered by an amino acid substitution.Scientific reports · 2019Article
- Citrate synthase from Synechocystis is a distinct class of bacterial citrate synthase.Scientific reports · 2019Article
- Purification and Characterisation of Malate Dehydrogenase FromFrontiers in plant science · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactate/lactic acid is an important chemical compound for the manufacturing of bioplastics. The unicellular cyanobacterium Synechocystis sp. PCC 6803 can produce lactate from carbon dioxide and possesses D-lactate dehydrogenase (Ddh). Here, we performed a biochemical analysis of the Ddh from this cyanobacterium (SyDdh) using recombinant proteins. SyDdh was classified into a cyanobacterial clade similar to those from Gram-negative bacteria, although it was distinct from them. SyDdh can use both pyruvate and oxaloacetate as a substrate and is activated by fructose-1,6-bisphosphate and repressed by divalent cations. An amino acid substitution based on multiple sequence alignment data revealed that the glutamine at position 14 and serine at position 234 are important for the allosteric regulation by Mg
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