Literature summary for 1.1.1.1 extracted from

Loder, A.J.; Zeldes, B.M.; Garrison, G.D.; Lipscomb, G.L.; Adams, M.W.; Kelly, R.M.
Alcohol selectivity in a synthetic thermophilic n-butanol pathway is driven by biocatalytic and thermostability characteristics of constituent enzymes (2015), Appl. Environ. Microbiol., 81, 7187-7200.

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Application

Application	Comment	Organism
synthesis	synthetic pathway for n-butanol production from acetyl coenzyme at 70°C, using beta-ketothiolase Thl, 3-hydroxybutyryl-CoA dehydrogenase Hbd, and 3-hydroxybutyryl-CoA dehydratase Crt from Caldanaerobacter subterraneus subsp. tengcongensis, trans-2-enoyl-CoA reductase Ter from Spirochaeta thermophila and bifunctional aldehyde dehydrogenase AdhE and and butanol dehydrogenase in vitro. n-Butanol is produced at 70°C, but with different amounts of ethanol as a coproduct, because of the broad substrate specificities of AdhE, Bad, and Bdh. A reaction kinetics model, validated via comparison to in vitro experiments, is used to determine relative enzyme ratios needed to maximize n-butanol production. By using large relative amounts of Thl and Hbd and small amounts of Bad and Bdh, >70% conversion to n-butanol is observed in vitro, but with a 60% decrease in the predicted pathway flux	Thermoanaerobacter sp.

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Thermoanaerobacter sp.

Organism

Organism	UniProt	Comment	Textmining
Thermoanaerobacter sp.	B0K4A2	-	-

Synonyms

Synonyms	Comment	Organism
AdhE	bifunctional enzyme, catalyzes reactions of EC 1.1.1.1 and EC 1.2.1.10	Thermoanaerobacter sp.
Teth514_0627	-	Thermoanaerobacter sp.

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Release 2023.1 (January 2023)