Literature summary for 4.1.2.47 extracted from

Gruber, K.; Gartler, G.; Krammer, B.; Schwab, H.; Kratky, C.
Reaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily: The three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236 (2004), J. Biol. Chem., 279, 20501-20510.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant K236L in Pichia pastoris	Hevea brasiliensis

Crystallization (Commentary)

Crystallization (Comment)	Organism
hanging drop vapor diffusion method, freeze-quench method to prepare crystals of the complex of the enzyme with acetone cyanohydrin, complex of mutant K236L enzyme with acetone, structure of the K236L with acetone cyanohydrin-acetone cyanohydrin shows the substrate in a different orientation from the wild-type complex	Hevea brasiliensis

Protein Variants

Protein Variants	Comment	Organism
C81A	about 20% of wild-type activity	Hevea brasiliensis
C81S	3% of wild-type activity	Hevea brasiliensis
E79A	1% of wild-type activity	Hevea brasiliensis
H235A	no activity	Hevea brasiliensis
K236L	inactive mutant protein, three-dimensional structure is similar to wild-type enzyme	Hevea brasiliensis
K236R	0.15% of wild-type activity	Hevea brasiliensis
P207A	no expression	Hevea brasiliensis
S80A	no activity	Hevea brasiliensis
T11A	2% of wild-type activity	Hevea brasiliensis

Organism

Organism	UniProt	Comment	Textmining
Hevea brasiliensis	P52704	-	-

Purification (Commentary)

Purification (Comment)	Organism
mutant K236L, recombinant	Hevea brasiliensis

Synonyms

Synonyms	Comment	Organism
HbHNL	-	Hevea brasiliensis

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Release 2023.1 (January 2023)