Literature summary for 3.1.1.74 extracted from

Miyakawa, T.; Mizushima, H.; Ohtsuka, J.; Oda, M.; Kawai, F.; Tanokura, M.
Structural basis for the Ca2+-enhanced thermostability and activity of PET-degrading cutinase-like enzyme from Saccharomonospora viridis AHK190 (2015), Appl. Microbiol. Biotechnol., 99, 4297-4307 .

Cloned(Commentary)

Cloned (Comment)	Organism
-	Saccharomonospora viridis

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structures of S226P mutant in the Ca2+-bound and free states at 1.75 and 1.45 A resolution, respectively. A Ca2+ ion is coordinated by four residues within loop regions (the Ca2+ site) and two water molecules in a tetragonal bipyramidal array. The binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily	Saccharomonospora viridis

Crystallization (Comment)

Organism

crystal structures of S226P mutant in the Ca2+-bound and free states at 1.75 and 1.45 A resolution, respectively. A Ca2+ ion is coordinated by four residues within loop regions (the Ca2+ site) and two water molecules in a tetragonal bipyramidal array. The binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily

Saccharomonospora viridis

Protein Variants

Protein Variants	Comment	Organism
S226P	mutant shows the highest activities toward tricaproin and tributyrin, the activity is greatly reduced toward tricaprylin	Saccharomonospora viridis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	the binding of Ca2+ induces large conformational changes in three loops, accompanied by the formation of additional interactions. The binding of Ca2+ stabilizes a region that is flexible in the Ca2+-free state but also modifies the substrate-binding groove by stabilizing an open conformation that allows the substrate to bind easily	Saccharomonospora viridis

Organism

Organism	UniProt	Comment	Textmining
Saccharomonospora viridis	W0TJ64	-	-
Saccharomonospora viridis AHK190	W0TJ64	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
tributyrin + H2O	about 85% of the activity with tricaproin, mutant S226P	Saccharomonospora viridis	butyric acid + 1,2-dibutyrylglycerol	-	?
tributyrin + H2O	about 85% of the activity with tricaproin, mutant S226P	Saccharomonospora viridis AHK190	butyric acid + 1,2-dibutyrylglycerol	-	?
tricaproin + H2O	-	Saccharomonospora viridis	?	-	?
tricaproin + H2O	-	Saccharomonospora viridis AHK190	?	-	?

Synonyms

Synonyms	Comment	Organism
Cut190	-	Saccharomonospora viridis

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
59	-	melting temperature, mutant S226P	Saccharomonospora viridis
73	-	melting temperature, mutant S226P, presence of 100 mM Ca2+	Saccharomonospora viridis
75	-	melting temperature, mutant S226P, presence of 300 mM Ca2+	Saccharomonospora viridis