Literature summary for 4.2.1.118 extracted from

Harrington, L.B.; Jha, R.K.; Kern, T.L.; Schmidt, E.N.; Canales, G.M.; Finney, K.B.; Koppisch, A.T.; Strauss, C.E.; Fox, D.T.
Rapid thermostabilization of Bacillus thuringiensis serovar Konkukian 97-27 dehydroshikimate dehydratase through a structure-based enzyme design and whole cell activity assay (2017), ACS Synth. Biol., 6, 120-129 .

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Cloned(Commentary)

Cloned (Comment)	Organism
in vivo overexpression of enzyme mutant Mut1 in Escherichiaxa0coli results in a about 60fold increase in functional enzyme when compared to the wild-type enzyme under the identical expression conditions, and 80-120% increase in DHB accumulation in the media	Bacillus thuringiensis

Protein Variants

Protein Variants	Comment	Organism
additional information	gene asbF is unstable at 37°C, structure-based design to identify stabilizing mutations and creation a combinatorial library based upon predicted mutations at specific locations on the enzyme surface. A diversified asbF library (with about 2000 variants) is expressed in Escherichiaxa0coli harboring a GFP reporter system linked to the product of AsbF activity (3,4-dihydroxybenzoate, DHB)	Bacillus thuringiensis
T61N/H135Y/H257P	random mutagenesis, triple AsbF mutant Mut1, half-life of Mut1 at 37°C is over 10fold higher compared to wild-type AsbF. The second-order rate constants for both wild-type AsbF and Mut1 are approximately equal, thus demonstrating protein thermostability does not come at the expense of enzyme thermophilicity	Bacillus thuringiensis

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
3-dehydro-shikimate	Bacillus thuringiensis	-	protocatechuate + H2O	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus thuringiensis	A0A1B1L4G3	serovar Konkukian 97-27	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
3-dehydro-shikimate	-	Bacillus thuringiensis	protocatechuate + H2O	-	?

Synonyms

Synonyms	Comment	Organism
AsbF	-	Bacillus thuringiensis
BT246_21860	-	Bacillus thuringiensis
dehydroshikimate dehydratase	-	Bacillus thuringiensis
DHSase	-	Bacillus thuringiensis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
37	-	recombinant wild-type enzyme AsbF, t1/2 is 169 min	Bacillus thuringiensis

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Release 2023.1 (January 2023)