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
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RECOMMENDED NAME
GeneOntology No.
5-phosphonooxy-L-lysine phospho-lyase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
(5R)-5-phosphonooxy-L-lysine + H2O = (S)-2-amino-6-oxohexanoate + NH3 + phosphate
show the reaction diagram
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PATHWAY
KEGG Link
MetaCyc Link
Lysine degradation
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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).
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5-phosphohydroxy-L-lysine ammoniophospholyase
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AGXT2L
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gene name
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AGXT2L2
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phospho lyase
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ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
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-
?
(5R)-5-phosphohydroxy-L-lysine + H2O
(S)-2-amino-6-oxohexanoate + NH3 + phosphate
show the reaction diagram
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?
phosphoallohydroxy-L-lysine + H2O
?
show the reaction diagram
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?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Borohydride
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inhibits the holoenzyme but no effect on the apoenzyme
additional information
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enzyme is inhibited by excess substrate
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KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0036
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(5R)-5-phosphohydroxy-L-lysine
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pH 7.4, 37°C
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0.0105
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(5R)-5-phosphohydroxy-L-lysine
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pH 7.4, 37°C
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0.0169
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(5R)-5-phosphohydroxy-L-lysine
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pH 7.4, 30°C, Vmax: 256 nmol/min/mg
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pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
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assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
51000
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SDS-PAGE
140000
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gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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