期刊
EMBO JOURNAL
卷 39, 期 18, 页码 -出版社
WILEY
DOI: 10.15252/embj.2019104081
关键词
carbon fixation; carboxylation rate; enhanced photosynthesis; metagenomic survey; ribulose-1,5-bisphosphate carboxylase/oxygenase
资金
- European Research Council [NOVCARBFIX 646827]
- Israel Science Foundation [740/16]
- Singapore National Research Foundation [NRF2017-NRF-ISF002-2667]
- Beck-Canadian Center for Alternative Energy Research
- Ullmann Family Foundation
- Helmsley Charitable Trust
- Larson Charitable Foundation
- Wolfson Family Charitable Trust
CO2 is converted into biomass almost solely by the enzyme rubisco. The poor carboxylation properties of plant rubiscos have led to efforts that made it the most kinetically characterized enzyme, yet these studies focused on < 5% of its natural diversity. Here, we searched for fast-carboxylating variants by systematically mining genomic and metagenomic data. Approximately 33,000 unique rubisco sequences were identified and clustered into approximate to 1,000 similarity groups. We then synthesized, purified, and biochemically tested the carboxylation rates of 143 representatives, spanning all clusters of form-II and form-II/III rubiscos. Most variants (> 100) were active in vitro, with the fastest having a turnover number of 22 +/- 1 s(-1)-sixfold faster than the median plant rubisco and nearly twofold faster than the fastest measured rubisco to date. Unlike rubiscos from plants and cyanobacteria, the fastest variants discovered here are homodimers and exhibit a much simpler folding and activation kinetics. Our pipeline can be utilized to explore the kinetic space of other enzymes of interest, allowing us to get a better view of the biosynthetic potential of the biosphere.
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