Literature summary for 4.1.2.47 extracted from

Bauer, M.; Griengl, H.; Steiner, W.
Kinetic studies on the enzyme (S)-hydroxynitrile lyase from Hevea brasiliensis using initial rate methods and progress curve analysis (1999), Biotechnol. Bioeng., 62, 20-29.

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Inhibitors

Inhibitors	Comment	Organism	Structure
benzaldehyde	acts as a linear competitive inhibitor against mandelonitrile	Hevea brasiliensis
HCN	shows S-linear I-parabolic mixed-type inhibition	Hevea brasiliensis

Organism

Organism	UniProt	Comment	Textmining
Hevea brasiliensis	P52704	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-mandelonitrile	enzyme kinetics in both directions is studied on a model system with mandelonitrile, benzaldehyde, and HCN using two different methods: initial rate measurements and progress curve analysis. Ordered Uni bi mechanism with the formation of a dead-end complex of enzyme, (S)-mandelonitrile and HCN. HCN is the first product released from the enzyme followed by benzaldehyde while in the synthesis reaction, benzaldehyde is the first substrate bond to the enzyme followed by HCN	Hevea brasiliensis	cyanide + benzaldehyde	-	r

Synonyms

Synonyms	Comment	Organism
(S)-Hydroxynitrile lyase	-	Hevea brasiliensis

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Release 2023.1 (January 2023)