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Literature summary for 4.3.1.28 extracted from

  • Tsotsou, G.E.; Barbirato, F.
    Biochemical characterisation of recombinant Streptomyces pristinaespiralis L-lysine cyclodeaminase (2007), Biochimie, 89, 591-604.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
dithiothreitol increase in enzyme activity between 2.1 and 2.5fold in the presence of dithiothreitol at 1-3 mM Streptomyces pristinaespiralis
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
additional information activity is not enhanced in the presence of ammonium sulfate Streptomyces pristinaespiralis

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli M15[pREP4] cells Streptomyces pristinaespiralis

Inhibitors

Inhibitors Comment Organism Structure
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
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

Metals/Ions Comment Organism Structure
Al3+ 151% relative activity at 3 mM Streptomyces pristinaespiralis
Fe2+ 1308% relative activity at 3 mM Streptomyces pristinaespiralis
Mg2+ 227% relative activity at 3 mM Streptomyces pristinaespiralis
additional information activity is not enhanced in the presence of Na+, Ca2+, Mn2+, and Zn2+ Streptomyces pristinaespiralis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37100
-
x * 37100, SDS-PAGE Streptomyces pristinaespiralis

Organism

Organism UniProt Comment Textmining
Streptomyces pristinaespiralis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Q-Sepharose column chromatography and ammonium sulfate precipitation Streptomyces pristinaespiralis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-hydroxylysine
-
Streptomyces pristinaespiralis ?
-
?
L-4-thialysine
-
Streptomyces pristinaespiralis ?
-
?
L-lysine
-
Streptomyces pristinaespiralis L-pipecolate + NH3
-
?
L-ornithine
-
Streptomyces pristinaespiralis ?
-
?
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

Subunits Comment Organism
? x * 37100, SDS-PAGE Streptomyces pristinaespiralis

Synonyms

Synonyms Comment Organism
LCD
-
Streptomyces pristinaespiralis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
61
-
-
Streptomyces pristinaespiralis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
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]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
-
Streptomyces pristinaespiralis

pH Range

pH Minimum pH Maximum Comment Organism
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

Cofactor Comment Organism Structure
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