Information on EC 4.3.1.28 - L-lysine cyclodeaminase

New: Word Map on EC 4.3.1.28
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Streptomyces

EC NUMBER
COMMENTARY hide
4.3.1.28
-
RECOMMENDED NAME
GeneOntology No.
L-lysine cyclodeaminase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-lysine = L-pipecolate + NH3
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
L-lysine ammonia-lyase (cyclizing; ammonia-forming)
Requires bound NAD+. The enzyme produces the non-proteinogenic amino acid L-pipecolate, which is incorporated into multiple secondary metabolite products, including rapamycin, tobulysin, virginiamycin and pristinamycin.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5-hydroxylysine
?
show the reaction diagram
-
-
-
-
?
L-4-thialysine
?
show the reaction diagram
-
-
-
-
?
L-lysine
L-pipecolate + NH3
show the reaction diagram
L-ornithine
?
show the reaction diagram
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
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Al3+
-
151% relative activity at 3 mM
Fe2+
-
1308% relative activity at 3 mM
Mg2+
-
227% relative activity at 3 mM
additional information
-
activity is not enhanced in the presence of Na+, Ca2+, Mn2+, and Zn2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(R)-(-)-nipecotic acid
-
-
-
(S)-(+)-nipecotic acid
-
-
-
thiazolidine-2-carboxylic acid
-
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
-
increase in enzyme activity between 2.1 and 2.5fold in the presence of dithiothreitol at 1-3 mM
glycerol
-
enzyme activity increases progressively up to at least 30% (v/v) glycerol. Activity is enhanced 4.6fold at 30% (v/v) glyerol
additional information
-
activity is not enhanced in the presence of ammonium sulfate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.046 - 1.39
L-lysine
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.61
L-lysine
Streptomyces hygroscopicus
-
0.1 mM NAD+, in 100 mM HEPES (pH 8.0), at 30C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13
L-lysine
Streptomyces hygroscopicus
-
0.1 mM NAD+, in 100 mM HEPES (pH 8.0), at 30C
134
0.14
L-ornithine
Streptomyces hygroscopicus
-
0.1 mM NAD+, in 100 mM HEPES (pH 8.0), at 30C
192
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.8
(R)-(-)-nipecotic acid
Streptomyces hygroscopicus
-
in 100 mM HEPES (pH 8.0), at 30C
-
0.68
(S)-(+)-nipecotic acid
Streptomyces hygroscopicus
-
in 100 mM HEPES (pH 8.0), at 30C
-
0.096
thiazolidine-2-carboxylic acid
Streptomyces hygroscopicus
-
in 100 mM HEPES (pH 8.0), at 30C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 70
-
the initial rate of L-lysine cyclodeamination is very low at or below room temperature, but it increases significantly from 23C to 61C and drops again suddenly at 66C, about 50% activity at 50C
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 37
-
enzyme stability does not change significantly between 4C and 37C, while there is clear loss of enzyme stability at temperatures greater than 37C
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
Q-Sepharose column chromatography and ammonium sulfate precipitation
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli DH10B cells
-
expressed in Escherichia coli M15[pREP4] cells
-