Isolation and Sequence of the Phosphoenolpyruvate Carboxylase Gene of the Marine Cyanobacterium Synechococcus PCC 7002

Smith, Aubrey; Coomes, M W; Smith, Thomas E.

doi:10.3923/jbs.2008.1261.1270

Cited by 7 publications

(1 citation statement)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, PEPCK contributes to photosynthetic carbon fixation as an addition to the C 3 pathway catalyzed by RuBisCO [14]. The same may be said of marine cyanobacteria where -carboxylation reactions involving phosphoenolpyruvate carboxylase (PEPC) and PEPCK are prevalent [15].…”

Section: Introductionmentioning

confidence: 99%

In Silico Characterization and Homology Modeling of a Cyanobacterial Phosphoenolpyruvate Carboxykinase Enzyme

Smith

Caruso

2013

Structural Biology

View full text Add to dashboard Cite

ATP-dependent phosphoenolpyruvate carboxykinase (PEPCK) is a key catabolic enzyme found in various species of bacteria, plants, and yeast. PEPCK may play a role in carbon fixation in aquatic ecosystems consisting of photosynthetic cyanobacteria. RuBisCO-based CO2fixation is prevalent in cyanobacteria through C3intermediates; however, a significant amount of carbon flows into C4acids during cyanobacterial photosynthesis. This indicates that a C4mechanism for inorganic carbon fixation is prevalent in cyanobacteria with PEPCK as an importantβ-carboxylation enzyme. Newly available genomic information has confirmed the existence of putativePEPCKgenes in a number of cyanobacterial species. This project represents the first structural and physicochemical study of cyanobacterial PEPCKs. Biocomputational analyses of cyanobacterial PEPCKs were performed and a homology model ofCyanothecesp. PCC 7424 PEPCK was generated. The modeled enzyme consists of an N-terminal and C-terminal domains with a mixedα/βtopology with the active site located in a deep cleft between the two domains. Active site residues and those involved in metal ion coordination were found to be conserved in the cyanobacterial enzymes. An active site lid which is known to close upon substrate binding was also predicted. Amino acid stretches that are unique to cyanobacterial PEPCKs were also identified.

show abstract

Section: Introductionmentioning

confidence: 99%

In Silico Characterization and Homology Modeling of a Cyanobacterial Phosphoenolpyruvate Carboxykinase Enzyme

Smith

Caruso

2013

Structural Biology

View full text Add to dashboard Cite

show abstract

Analysis and Elucidation of Phosphoenolpyruvate Carboxylase in Cyanobacteria

et al. 2015

View full text Add to dashboard Cite

Phosphoenolpyruvate carboxylase (PEPC) a cytosolic enzyme of higher plants is also found in bacteria and cyanobacteria. Genetic and biochemical investigations have indicated that there are several isoforms of PEPC belonging to C3; C3/C4 and C4 groups but, the evolution of PEPC in cyanobacteria is not yet understood. The present study opens up an opportunity to understand the isoforms and functions of PEPC in cyanobacteria. The variations observed in PEPC among lower and higher orders of cyanobacteria, suggests convergent evolution of PEPC. There is a specific PEPC phosphorylation residue 'serine' at the N-terminus and PEPC determinant residue 'serine' at the C-terminal that facilitates high affinity for substrate binding. These residues were unique to higher orders of cyanobacteria, but, not in lower orders and other prokaryotes. The different PEPC forms of cyanobacteria were investigated for their kinetic properties with phosphoenolpyruvate as the substrate and the findings corroborated well with the in silico findings. In vitro enzymatic study of cyanobacteria belonging to three different orders demonstrated the role of aspartate as an allosteric effector, which inhibited PEPC by interacting with the highly conserved residues in the active site. The differences in mode of inhibition among the different order, thus, give a fair picture about the cyanobacterial PEPCs. The higher orders appear to possess the sequence coordinates and functionally conserved residues similar to isoforms of C4 type higher plants, whereas isoforms of PEPC of the lower orders did not resemble either that of C3 or C4 plants.

show abstract

Study on the Bioconversion of Curcumin to Calebin-A Using Spirulina subsalsa and Its Taxonomic Resolution Using 16S rRNA Analysis

Fathima

Adams

Majeed

et al. 2022

Appl Biochem Biotechnol

View full text Add to dashboard Cite

Isolation and Sequence of the Phosphoenolpyruvate Carboxylase Gene of the Marine Cyanobacterium Synechococcus PCC 7002

Cited by 7 publications

References 20 publications

In Silico Characterization and Homology Modeling of a Cyanobacterial Phosphoenolpyruvate Carboxykinase Enzyme

In Silico Characterization and Homology Modeling of a Cyanobacterial Phosphoenolpyruvate Carboxykinase Enzyme

Analysis and Elucidation of Phosphoenolpyruvate Carboxylase in Cyanobacteria

Study on the Bioconversion of Curcumin to Calebin-A Using Spirulina subsalsa and Its Taxonomic Resolution Using 16S rRNA Analysis

Contact Info

Product

Resources

About