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 hide
4.2.3.134
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RECOMMENDED NAME
GeneOntology No.
5-phosphonooxy-L-lysine phospho-lyase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(5R)-5-phosphonooxy-L-lysine + H2O = (S)-2-amino-6-oxohexanoate + NH3 + phosphate
show the reaction diagram
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-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Lysine degradation
-
-
Metabolic pathways
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-
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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
phosphoallohydroxy-L-lysine + H2O
?
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
0.0036 - 0.0169
(5R)-5-phosphohydroxy-L-lysine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51000
SDS-PAGE
140000
-
gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
expression in Escherichia coli and HK293T cell
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E437V
recombinant protein is very largely insoluble
G240R
recombinant protein is very largely insoluble
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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