2007
DOI: 10.1007/s11120-007-9240-7
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Ribulose-1,5-bisphosphate carboxylase/oxygenase from thermophilic cyanobacterium Thermosynechococcus elongatus

Abstract: Ribulose-1,5-bisphosphate carboxylase/oxygenase (rubisco) can be divided into two branches: the "red-like type" of marine algae and the "green-like type" of cyanobacteria, green algae, and higher plants. We found that the "green-like type" rubisco from the thermophilic cyanobacterium Thermosynechococcus elongatus has an almost 2-fold higher specificity factor compared with rubiscos of mesophilic cyanobacteria, reaching the values of higher plants, and simultaneously revealing an improvement in enzyme thermosta… Show more

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Cited by 23 publications
(23 citation statements)
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“…for parameters used here (based on best approximations in comparison to known data) agrees well with measured values of inverse specificity [11,26,27].…”
Section: Viability and Light-limited Rangessupporting
confidence: 75%
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“…for parameters used here (based on best approximations in comparison to known data) agrees well with measured values of inverse specificity [11,26,27].…”
Section: Viability and Light-limited Rangessupporting
confidence: 75%
“…Effectively, η is a branching function of O 2 and IC that determines how much photosynthetic product goes to synthesis of new biomaterial and how much to synthesis of soluble, excretable, organic carbon. Phototrophs may have a degree of control over the value of η either directly through the structure of RuBisCO itself [26,27] or through indirect machinery such as carbon capture mechanisms, so we treat γ 1 as a tunable parameter and study effects of its variation.…”
Section: Photorespirationmentioning
confidence: 99%
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“…Interestingly, RuBisCo purified from the cyanobacterium Phrochlorococcus marinus MIT9313 showed an activity of 0.41 μmol min −1 mg protein −1 [49] and RuBisCO from the cyanobacterium Thermosynechococcus elongatus expressed and purified in Escherichia coli a specific activity of 1.83 μmol min −1 mg protein −1 [50] compared to the PEPc activity of 8.84 μmol min −1 mg protein −1 observed in the cyanobacterium C. peniocystis [47]. PEPc is the primary CO 2 -fixing enzyme in C 4 and CAM plants [48] and [51].…”
Section: Phosphoenolpyruvate Carboxylase (Pepc)mentioning
confidence: 99%