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Literature summary extracted from
- Biochemical characterisation of recombinant Streptomyces pristinaespiralis L-lysine cyclodeaminase (2007), Biochimie, 89, 591-604.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.28 | dithiothreitol | increase in enzyme activity between 2.1 and 2.5fold in the presence of dithiothreitol at 1-3 mM | Streptomyces pristinaespiralis |  |
| 4.3.1.28 | glycerol | enzyme activity increases progressively up to at least 30% (v/v) glycerol. Activity is enhanced 4.6fold at 30% (v/v) glyerol | Streptomyces pristinaespiralis | |
| 4.3.1.28 | additional information | activity is not enhanced in the presence of ammonium sulfate | Streptomyces pristinaespiralis |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.3.1.28 | expressed in Escherichia coli M15[pREP4] cells | Streptomyces pristinaespiralis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.28 | additional information | no inhibition by the substrate L-lysine up to 2.0 M, by the product L-pipecolate at concentrations up to 1.0 M or by NADH up to 1.1 mM | Streptomyces pristinaespiralis |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.3.1.28 | 1.39 | - |
L-lysine | in 100 mM potassium phosphate buffer, pH 8.0 containing 10% (v/v) glycerol, at 37°C | Streptomyces pristinaespiralis | |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.28 | Al3+ | 151% relative activity at 3 mM | Streptomyces pristinaespiralis | |
| 4.3.1.28 | Fe2+ | 1308% relative activity at 3 mM | Streptomyces pristinaespiralis | |
| 4.3.1.28 | Mg2+ | 227% relative activity at 3 mM | Streptomyces pristinaespiralis | |
| 4.3.1.28 | additional information | activity is not enhanced in the presence of Na+, Ca2+, Mn2+, and Zn2+ | Streptomyces pristinaespiralis |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.28 | 37100 | - |
x * 37100, SDS-PAGE | Streptomyces pristinaespiralis |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.3.1.28 | Streptomyces pristinaespiralis | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.3.1.28 | Q-Sepharose column chromatography and ammonium sulfate precipitation | Streptomyces pristinaespiralis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.3.1.28 | 5-hydroxylysine | - |
Streptomyces pristinaespiralis | ? | - |
? | |
| 4.3.1.28 | L-4-thialysine | - |
Streptomyces pristinaespiralis | ? | - |
? | |
| 4.3.1.28 | L-lysine | - |
Streptomyces pristinaespiralis | L-pipecolate + NH3 | - |
? | |
| 4.3.1.28 | L-ornithine | - |
Streptomyces pristinaespiralis | ? | - |
? | |
| 4.3.1.28 | additional information | 4-azalysine, L-2,4-diaminobutyric acid, 1,5-diaminopentane, N3-trifluoroacetyl-L-lysine, N3-Boc-L-lysine and N3-methyl-L-lysine compete against L-lysine turnover without being converted by the enzyme | Streptomyces pristinaespiralis | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 4.3.1.28 | ? | x * 37100, SDS-PAGE | Streptomyces pristinaespiralis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.3.1.28 | LCD | - |
Streptomyces pristinaespiralis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.28 | 61 | - |
- |
Streptomyces pristinaespiralis |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.28 | 40 | 70 | the initial rate of L-lysine cyclodeamination is very low at or below room temperature, but it increases significantly from 23°C to 61°C and drops again suddenly at 66°C, about 50% activity at 50°C | Streptomyces pristinaespiralis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.28 | 4 | 37 | enzyme stability does not change significantly between 4°C and 37°C, while there is clear loss of enzyme stability at temperatures greater than 37°C | Streptomyces pristinaespiralis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.28 | 6.7 | - |
- |
Streptomyces pristinaespiralis |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 4.3.1.28 | 5.4 | 9 | about 50% activity at pH 6.0 and 7.5. The enzyme activity is minimal at pH values below 5.4 and above 9.0 | Streptomyces pristinaespiralis |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.3.1.28 | NAD+ | there is no requirement for an external cofactor for full activity, although sequence data indicate NAD+ as cofactor. NAD+ binds very tightly to the enzyme | Streptomyces pristinaespiralis | |
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