Literature summary for 4.2.3.134 extracted from

Veiga-da-Cunha, M.; Hadi, F.; Balligand, T.; Stroobant, V.; Van Schaftingen, E.
Molecular identification of hydroxylysine kinase and of ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and phosphoethanolamine (2012), J. Biol. Chem., 287, 7246-7255.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli as a His-tagged fusion protein	Mus musculus

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	enzyme is inhibited by excess substrate	Mus musculus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0169	-	(5R)-5-phosphohydroxy-L-lysine	pH 7.4, 30°C, Vmax: 256 nmol/min/mg	Mus musculus

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cytosol	-	Mus musculus	5829	-

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
51000	-	SDS-PAGE	Mus musculus

Organism

Organism	UniProt	Comment	Textmining
Mus musculus	Q8R1K1	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
kidney	cDNA	Mus musculus	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
(5R)-5-phosphohydroxy-L-lysine + H2O	-	Mus musculus	(S)-2-amino-6-oxohexanoate + NH3 + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
AGXT2L2	-	Mus musculus

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
30	-	assay at	Mus musculus

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.4	-	assay at	Mus musculus

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	-	Mus musculus

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Release 2023.1 (January 2023)