Corrigendum: Purification and Characterisation of Malate Dehydrogenase From sp. PCC 6803: Biochemical Barrier of the Oxidative Tricarboxylic Acid Cycle.

[This corrects the article DOI: 10.3389/fpls.2018.

Efficient extraction and preservation of thermotolerant phycocyanins from red alga Cyanidioschyzon merolae.

C-Phycocyanin (PC) is a protein used commercially as a natural blue pigment produced by cyanobacteria, cryptophytes, and rhodophytes. Although it is industrially synthesized from the cyanobacterium Arthrospira platensis, PC requires high levels of energy for its extraction, which involves freezing of cells. However, as a protein, PC is easily denatured at extreme temperatures.

Biochemical characterisation of fumarase C from a unicellular cyanobacterium demonstrating its substrate affinity, altered by an amino acid substitution.

The tricarboxylic acid cycle produces NADH for oxidative phosphorylation and fumarase [EC 4.2.1.

Purification and Characterisation of Malate Dehydrogenase From sp. PCC 6803: Biochemical Barrier of the Oxidative Tricarboxylic Acid Cycle.

Cyanobacteria possess an atypical tricarboxylic acid (TCA) cycle with various bypasses. Previous studies have suggested that a cyclic flow through the TCA cycle is not essential for cyanobacteria under normal growth conditions. The cyanobacterial TCA cycle is, thus, different from that in other bacteria, and the biochemical properties of enzymes in this TCA cycle are less understood.

Substrate Specificity and Allosteric Regulation of a D-Lactate Dehydrogenase from a Unicellular Cyanobacterium are Altered by an Amino Acid Substitution.

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).

Cluster-Level Relationships of Genes Involved in Carbon Metabolism in Synechocystis sp. PCC 6803: Development of a Novel Succinate-Producing Strain.

We quantified the transcript levels of 44 genes related to sugar catabolism in strains with altered primary carbon metabolism and discovered a consistent expression pattern among succinate-producing mutants. To identify factors that determine the expression pattern, we calculated Pearson's correlation coefficients, using the transcript data. Correlation analysis revealed positive and negative correlations among genes encoding sugar catabolic enzymes.

Allosteric Inhibition of Phosphoenolpyruvate Carboxylases is Determined by a Single Amino Acid Residue in Cyanobacteria.

Phosphoenolpyruvate carboxylase (PEPC) is an important enzyme for CO fixation and primary metabolism in photosynthetic organisms including cyanobacteria. The kinetics and allosteric regulation of PEPCs have been studied in many organisms, but the biochemical properties of PEPC in the unicellular, non-nitrogen-fixing cyanobacterium Synechocystis sp. PCC 6803 have not been clarified.

Modification of photosynthetic electron transport and amino acid levels by overexpression of a circadian-related histidine kinase hik8 in Synechocystis sp. PCC 6803.

Cyanobacteria perform oxygenic photosynthesis, and the maintenance of photosynthetic electron transport chains is indispensable to their survival in various environmental conditions. Photosynthetic electron transport in cyanobacteria can be studied through genetic analysis because of the natural competence of cyanobacteria. We here show that a strain overexpressing hik8, a histidine kinase gene related to the circadian clock, exhibits an altered photosynthetic electron transport chain in the unicellular cyanobacterium Synechocystis sp.