Literature summary for 4.1.2.47 extracted from

Wagner, U.G.; Hasslacher, M.; Griengl, H.; Schwab, H.; Kratky, C.
Mechanism of cyanogenesis: the crystal structure of hydroxynitrile lyase from Hevea brasiliensis (1996), Structure, 4, 811-822.

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the hydroxynitrile lyase at 1.9 A resolution. The structure belongs to the alpha/beta hydrolase superfamily. Its active site is deeply buried inside the protein, and connected to the outside by a narrow tunnel. The catalytic triade consists of residues Ser80, His235 and Asp207. By analogy with other alpha/beta hydrolases, the oxyanion hole is formed by the mainchain-NH of Cys81 and by the side-chains of Cys81 and Thr11	Hevea brasiliensis

Crystallization (Comment)

Organism

crystal structure of the hydroxynitrile lyase at 1.9 A resolution. The structure belongs to the alpha/beta hydrolase superfamily. Its active site is deeply buried inside the protein, and connected to the outside by a narrow tunnel. The catalytic triade consists of residues Ser80, His235 and Asp207. By analogy with other alpha/beta hydrolases, the oxyanion hole is formed by the mainchain-NH of Cys81 and by the side-chains of Cys81 and Thr11

Hevea brasiliensis

Organism

Organism	UniProt	Comment	Textmining
Hevea brasiliensis	P52704	-	-

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Release 2023.1 (January 2023)