Information on EC 4.2.3.134 - 5-phosphonooxy-L-lysine phospho-lyase

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The expected taxonomic range for this enzyme is: Euarchontoglires

EC NUMBER
COMMENTARY
4.2.3.134
-
RECOMMENDED NAME
GeneOntology No.
5-phosphonooxy-L-lysine phospho-lyase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(5R)-5-phosphonooxy-L-lysine + H2O = (S)-2-amino-6-oxohexanoate + NH3 + phosphate
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Lysine degradation
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
(5R)-5-phosphonooxy-L-lysine phosphate-lyase (deaminating; (S)-2-amino-6-oxohexanoate-forming)
A pyridoxal-phosphate protein. Has no activity with phosphoethanolamine (cf. EC 4.2.3.2, ethanolamine-phosphate phospho-lyase).
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5-phosphohydroxy-L-lysine ammoniophospholyase
-
-
-
-
AGXT2L
-
-
gene name
-
phospho lyase
-
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(5R)-5-phosphohydroxy-L-lysine + H2O
(S)-2-amino-6-oxohexanoate + NH3 + phosphate
show the reaction diagram
-
-
-
?
(5R)-5-phosphohydroxy-L-lysine + H2O
(S)-2-amino-6-oxohexanoate + NH3 + phosphate
show the reaction diagram
-
-
?
phosphoallohydroxy-L-lysine + H2O
?
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Borohydride
-
inhibits the holoenzyme but no effect on the apoenzyme
additional information
enzyme is inhibited by excess substrate
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0036
(5R)-5-phosphohydroxy-L-lysine
-
pH 7.4, 37°C
-
0.0105
(5R)-5-phosphohydroxy-L-lysine
-
pH 7.4, 37°C
-
0.0169
(5R)-5-phosphohydroxy-L-lysine
pH 7.4, 30°C, Vmax: 256 nmol/min/mg
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
SDS-PAGE
720057
140000
-
gel filtration
719774
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and HK293T cell
expressed in Escherichia coli as a His-tagged fusion protein
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E437V
recombinant protein is very largely insoluble
G240R
recombinant protein is very largely insoluble
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
phosphohydroxylysinuria results from mutations in the AGXT2L2 gene, encoding phosphohydroxylysine phospholyase, and the resulting lack of activty o the enzyme. Mutants Gly240Arg and Glu437Val isolated from a patient are largely insoluble. The diversity of the clinical symptoms described in three patients with phosphohydroxylysinuria indicates that this is most likely not a neurometabolic disease