Literature summary for 3.1.1.5 extracted from

Lo, Y.C.; Lin, S.C.; Shaw, J.F.; Liaw, Y.C.
Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement (2005), Biochemistry, 44, 1971-1979.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the multifunctional thioesterase I/protease I/lysophospholipase L1 in complex with octanoic acid and of the L109P mutant enzyme in complex with octanoic acid	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
L109P	mutation abolishes switch loop movement	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ADA1	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
TAP	multifunctional lysophospholipasethioesterase I/protease I/lysophospholipase L1	Escherichia coli
thioesterase I/protease I/lysophospholipase L1	multifunctional lysophospholipase	Escherichia coli

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Release 2023.1 (January 2023)