4.1.2.47: (S)-hydroxynitrile lyase

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For detailed information about (S)-hydroxynitrile lyase, go to the full flat file.

Reaction

Synonyms

(R)-LuHNL, (R)-Oxynitrilase, (S)-cyanohydrin producing hydroxynitrile lyase, (S)-Hb-HNL, (S)-HbHNL, (S)-HNL, (S)-Hydroxynitrile lyase, (S)-Me-HNL, (S)-MeHNL, (S)-Oxynitrilase, (S)-selective HNL, (S)-selective hydroxynitrile lyase, Acetone cyanohydrin lyase, ACL, alpha-Hydroxynitrile lyase, EC 4.1.2.37, EC 4.1.2.39, Hb-HNL, HbHNL, HNL, HNL1, Hydroxynitrile lyase, LuHNL, MeHNKL, MeHNL, mut-HNL1, Oxynitrilase, S-HnL, S-hydroxynitrile lyase, S-selective HnL, S-selective hydroxynitrile lyase, S-stereoselective HNL

ECTree

     4 Lyases

         4.1 Carbon-carbon lyases

             4.1.2 Aldehyde-lyases

                4.1.2.47 (S)-hydroxynitrile lyase

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Results	in table
3	Activating Compound
3	AA Sequence
27	Application
33	Cloned(Commentary)
3	Cofactor
16	Crystallization (Commentary)
2	Expression
1	General Information
8	General Stability
50	Inhibitors
77	kcat/KM [mM/s]
2	Ki Value [mM]
135	KM Value [mM]
2	Localization
23	Molecular Weight [Da]
23	Natural Substrates/ Products (Substrates)
4	Organic Solvent Stability
94	Organism
2	Oxidation Stability
3	Pathway
12	PDB ID
23	pH Optimum
4	pH Range
17	pH Stability
2	pI Value
2	Posttranslational Modification
99	Protein Variants
26	Purification (Commentary)
3	Reaction
6	Reaction Type
91	Reference
20	Source Tissue
76	Specific Activity [micromol/min/mg]
1	Storage Stability
368	Substrates and Products (Substrate)
14	Subunits
134	Synonyms
1	Systematic Name
7	Temperature Optimum [°C]
3	Temperature Range [°C]
17	Temperature Stability [°C]
100	Turnover Number [1/s]

pH Stability

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pH Stability on EC 4.1.2.47 - (S)-hydroxynitrile lyase

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pH STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

2.4 - 11

Baliospermum montanum

D1MX73

-

728015

3

Manihot esculenta

P52705

half-life: 47 h

691345

3.5

Hevea brasiliensis

P52704

enzyme is inactivated very fast. Stability decreases with higher buffer concentrations at pH 3.5 in all three buffer systems (phosphate buffer, glutamate buffer, citrate buffer)

705188

4

5 entries

4.5

Hevea brasiliensis

-

below pH 4.5 enzyme is inactivated within a few min

651011

4.8

Hevea brasiliensis

-

still stable at this value

653957

5

2 entries

5 - 10

Hevea brasiliensis

P52704

starts to precipitate below pH 5.0, denatures above pH 10.0

652556

5 - 8

Manihot esculenta

P52705

half-life: above 100 h

691345

5.4

Hevea brasiliensis

-

most stable at

651012

6

Hevea brasiliensis

-

very stable above pH 6.0

650346

6.5

Hevea brasiliensis

P52704

very stable above. At pH 6.5 stability increases with increasing buffer concentration in all three systems (phosphate buffer, glutamate buffer, citrate buffer). The enzyme is most stable in phosphate buffer whereas for glutamate buffer the relative increase of half-life with concentration is more pronounced

705188

4

Hevea brasiliensis

P52704

decativation below pH 4.0, an unfolding of the enzyme followed by aggregation leading to closely packed enzyme particles at low pH values

703489

4

Hevea brasiliensis

-

the enzyme shows a half-life time of ca. 4 h at pH 5.0

704762

4

Manihot esculenta

P52705

half-life time: 2 h, the deactivation of the enzyme at slightly acidic pH is a result of pronounced structural unfolding

704762

4

Manihot esculenta

P52705

half-life: 84 h

691345

4

Manihot esculenta

P52705

the enzyme shows still 40% of its maximal activity at pH 4.0, while its activity is drastically reduced below pH 4.0

704762

5

Hevea brasiliensis

-

half-life in stirred solution is approximately 3.5 h

651011

5

Hevea brasiliensis

-

unstable below. Fivefold increase in half-life under optimal conditions by Venoruton and monohydroxyethylrutoside. 50% increase in half-life by 5-20 ng/ml rutin and 1.5-6 ng/ml by hyperoside

655659