Literature summary for 4.1.2.47 extracted from

Hasslacher, M.; Kratky, C.; Griengl, H.; Schwab, H.; Kohlwein, S.D.
Hydroxynitrile lyase from Hevea brasiliensis: molecular characterization and mechanism of enzyme catalysis (1997), Proteins, 27, 438-449.

Search for more literature for 4.1.2.47

Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant and wild-type proteins in Saccharomyces cerevisiae	Hevea brasiliensis

Protein Variants

Protein Variants	Comment	Organism
C81S	no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing. Mutation does not change the charge or size of the amino acid side chain, but nevertheless greatly reduces activity	Hevea brasiliensis
E79A	no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing. Mutation greatly reduces, but does not abolish activity. The negative charge provided by Glu-79 may be required in the active site, but a direct participation of this residue in enzyme catalysis is not suggested	Hevea brasiliensis
H10A	mutation results in a 30000 Da protein with increased electrophoretic mobility on native high percentage (16%) polyacrylamide gels. the mutant enzyme displays almost wild-type specific activity in crude extracts, suggesting that His10 is not crucial for activity. However, activity is almost completely lost during purification, supporting the possibility that the H10A exchange has a destabilizing effect and may prevent formation of an active dimer of the enzyme after purification	Hevea brasiliensis
H235A	inactive mutant enzyme, no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing	Hevea brasiliensis
S80A	no difference can be observed in the electrophoretic mobilities between the wild-type and mutant protein on native polyacrylamide gels and by isoelectric focusing	Hevea brasiliensis

Inhibitors

Inhibitors	Comment	Organism	Structure
HgCl2	-	Hevea brasiliensis
additional information	PMSF, NEM or 4-amidinophenylmethanesulfonylfluoride do not inhibit enzymatic activity	Hevea brasiliensis
p-chloromercurybenzoate	-	Hevea brasiliensis

Organism

Organism	UniProt	Comment	Textmining
Hevea brasiliensis	P52704	-	-

Purification (Commentary)

Purification (Comment)	Organism
mutant enzymes Hnl-E79A, Hnl-S80A, Hnl-C81S, and Hnl-H235A and the wild-type protein are purified to homogeneity, and Hnl-H10A is partially purified, by ion exchange chromatography and native polyacrylamide gel electrophoresis	Hevea brasiliensis

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(S)-mandelonitrile	the enzyme is a member of the alpha/beta hydrolase fold protein family, containing a catalytic triad with C-C cleaving and ligating activity	Hevea brasiliensis	cyanide + benzaldehyde	-	r

Synonyms

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

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Release 2023.1 (January 2023)