Reference to 4.1.2.47; Id = 747168 - BRENDA Enzyme Database

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli BL21 (DE3)	Manihot esculenta
expression in Escherichia coli BL21 (DE3)	Baliospermum montanum

Crystallization (Commentary)

Crystallization (Comment)	Organism
sitting drop vapor diffusion method, two crystal structures of Baliospermum montanum hydroxynitrile lyase, apo1 and apo2, are determined at 2.55 and 1.9 A, respectively. Structural comparison between Baliospermum montanum (apo2) and S-hydroxynitrile lyase from Hevea brasiliensis with (S)-mandelonitrile bound to the active site reveal that hydrophobic residues at the entrance region of Baliospermum montanum hydroxynitrile lyase form hydrophobic interactions with the benzene ring of the substrate. The flexible structures of these hydrophobic residues are confirmed by a 15 ns molecular dynamics simulation. This flexibility regulates the size of the active site cavity, enabling binding of various substrates to Baliospermum montanum. The high affinity of Baliospermum montanum hydroxynitrile lyase toward substrates containing a benzene ring is also confirmed by comparing the kinetics of Baliospermum montanum hydroxynitrile lyase and S-hydroxynitrile lyase from Manihot esculenta	Manihot esculenta
sitting drop vapor diffusion method, two crystal structures of Baliospermum montanum hydroxynitrile lyase, apo1 and apo2, are determined at 2.55 and 1.9 A, respectively. Structural comparison between Baliospermum montanum (apo2) and S-hydroxynitrile lyase from Hevea brasiliensis with (S)-mandelonitrile bound to the active site reveal that hydrophobic residues at the entrance region of Baliospermum montanum hydroxynitrile lyase form hydrophobic interactions with the benzene ring of the substrate. The flexible structures of these hydrophobic residues are confirmed by a 15 ns molecular dynamics simulation. This flexibility regulates the size of the active site cavity, enabling binding of various substrates to Baliospermum montanum. The high affinity of Baliospermum montanum hydroxynitrile lyase toward substrates containing a benzene ring is also confirmed by comparing the kinetics of Baliospermum montanum hydroxynitrile lyase and S-hydroxynitrile lyase from Manihot esculenta	Baliospermum montanum

Crystallization (Comment)

Organism

sitting drop vapor diffusion method, two crystal structures of Baliospermum montanum hydroxynitrile lyase, apo1 and apo2, are determined at 2.55 and 1.9 A, respectively. Structural comparison between Baliospermum montanum (apo2) and S-hydroxynitrile lyase from Hevea brasiliensis with (S)-mandelonitrile bound to the active site reveal that hydrophobic residues at the entrance region of Baliospermum montanum hydroxynitrile lyase form hydrophobic interactions with the benzene ring of the substrate. The flexible structures of these hydrophobic residues are confirmed by a 15 ns molecular dynamics simulation. This flexibility regulates the size of the active site cavity, enabling binding of various substrates to Baliospermum montanum. The high affinity of Baliospermum montanum hydroxynitrile lyase toward substrates containing a benzene ring is also confirmed by comparing the kinetics of Baliospermum montanum hydroxynitrile lyase and S-hydroxynitrile lyase from Manihot esculenta

Manihot esculenta

sitting drop vapor diffusion method, two crystal structures of Baliospermum montanum hydroxynitrile lyase, apo1 and apo2, are determined at 2.55 and 1.9 A, respectively. Structural comparison between Baliospermum montanum (apo2) and S-hydroxynitrile lyase from Hevea brasiliensis with (S)-mandelonitrile bound to the active site reveal that hydrophobic residues at the entrance region of Baliospermum montanum hydroxynitrile lyase form hydrophobic interactions with the benzene ring of the substrate. The flexible structures of these hydrophobic residues are confirmed by a 15 ns molecular dynamics simulation. This flexibility regulates the size of the active site cavity, enabling binding of various substrates to Baliospermum montanum. The high affinity of Baliospermum montanum hydroxynitrile lyase toward substrates containing a benzene ring is also confirmed by comparing the kinetics of Baliospermum montanum hydroxynitrile lyase and S-hydroxynitrile lyase from Manihot esculenta

Baliospermum montanum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.2	-	1-naphthalene carboxaldehyde	pH 4.2, 22°C	Baliospermum montanum
1.4	-	1-naphthalene carboxaldehyde	pH 4.2, 22°C	Manihot esculenta
25.4	-	4-biphenyl carboxaldehyde	pH 4.2, 22°C	Manihot esculenta
34.1	-	2-thiophene carboxaldehyde	pH 4.2, 22°C	Manihot esculenta
47.5	-	2-thiophene carboxaldehyde	pH 4.2, 22°C	Baliospermum montanum

Organism

Organism	UniProt	Comment	Textmining
Baliospermum montanum	D1MX73	-	-
Manihot esculenta	P52705	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Manihot esculenta
-	Baliospermum montanum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
cyanide + 1-naphthalene carboxaldehyde	-	Manihot esculenta	?	-	?
cyanide + 1-naphthalene carboxaldehyde	-	Baliospermum montanum	?	-	?
cyanide + 2-thiophene carboxaldehyde	-	Manihot esculenta	?	-	?
cyanide + 2-thiophene carboxaldehyde	-	Baliospermum montanum	?	-	?
cyanide + 4-biphenyl carboxaldehyde	-	Manihot esculenta	?	-	?
cyanide + 4-biphenyl carboxaldehyde	-	Baliospermum montanum	?	-	?

Synonyms

Synonyms	Comment	Organism
S-HnL	-	Manihot esculenta
S-HnL	-	Baliospermum montanum

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
6	-	1-naphthalene carboxaldehyde	pH 4.2, 22°C	Baliospermum montanum
9.2	-	4-biphenyl carboxaldehyde	pH 4.2, 22°C	Manihot esculenta
23.5	-	1-naphthalene carboxaldehyde	pH 4.2, 22°C	Manihot esculenta
31.5	-	2-thiophene carboxaldehyde	pH 4.2, 22°C	Baliospermum montanum
100	-	2-thiophene carboxaldehyde	pH 4.2, 22°C	Manihot esculenta

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
0.4	-	4-biphenyl carboxaldehyde	pH 4.2, 22°C	Manihot esculenta
0.7	-	2-thiophene carboxaldehyde	pH 4.2, 22°C	Baliospermum montanum
4.2	-	2-thiophene carboxaldehyde	pH 4.2, 22°C	Manihot esculenta
16.8	-	1-naphthalene carboxaldehyde	pH 4.2, 22°C	Manihot esculenta
30	-	1-naphthalene carboxaldehyde	pH 4.2, 22°C	Baliospermum montanum

Literature summary for 4.1.2.47 extracted from

Cloned(Commentary)

Crystallization (Commentary)

KM Value [mM]

Organism

Purification (Commentary)

Substrates and Products (Substrate)

Synonyms

Turnover Number [1/s]

kcat/KM [mM/s]