Literature summary for 4.1.2.47 extracted from

Asano, Y.; Kawahara, N.
A new S-hydroxynitrile lyase from Baliospermum montanum - its structure, molecular dynamics simulation, and improvement by protein engineering (2016), Ind. Biotechnol., 12, 91-97 .

No PubMed abstract available

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Baliospermum montanum

Crystallization (Commentary)

Crystallization (Comment)	Organism
-	Baliospermum montanum

Protein Variants

Protein Variants	Comment	Organism
H103C/N156G	the double mutant is suitable for (S)-mandelonitrile synthesis, improving its enantioselectivity and specific activity. The specific activity of the H103C/N156G mutant enzyme is improved to 154 U/mg from 52 U/mg as compared with wild type enzyme for (S)-mandelonitrile production, and the enantiomeric excess of (S)-mandelonitrile produced by the double mutant is increased to 93% from 55% compared with wild type enzyme	Baliospermum montanum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
60000	65000	gel filtration	Baliospermum montanum

Organism

Organism	UniProt	Comment	Textmining
Baliospermum montanum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Baliospermum montanum

Source Tissue

Source Tissue	Comment	Organism	Textmining
leaf	-	Baliospermum montanum	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
cyanide + benzaldehyde	-	Baliospermum montanum	(S)-mandelonitrile	-	?

Subunits

Subunits	Comment	Organism
dimer	2 * 29500, SDS-PAGE	Baliospermum montanum

Synonyms

Synonyms	Comment	Organism
S-hydroxynitrile lyase	-	Baliospermum montanum
S-stereoselective HNL	-	Baliospermum montanum

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Release 2023.1 (January 2023)