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Information on EC 4.2.3.134 - 5-phosphonooxy-L-lysine phospho-lyase and Organism(s) Homo sapiens

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.3 Acting on phosphates
                4.2.3.134 5-phosphonooxy-L-lysine phospho-lyase
IUBMB Comments
A pyridoxal-phosphate protein. Has no activity with phosphoethanolamine (cf. EC 4.2.3.2, ethanolamine-phosphate phospho-lyase).
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Homo sapiens
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
agxt2l2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5-phosphohydroxy-L-lysine ammoniophospholyase
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AGXT2L
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PATHWAY SOURCE
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).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
AT2L2_HUMAN
450
0
49711
Swiss-Prot
Mitochondrion (Reliability: 5)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E437V
recombinant protein is very largely insoluble
G240R
recombinant protein is very largely insoluble
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli and HK293T cell
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
phosphohydroxylysinuria results from mutations in the AGXT2L2 gene, encoding phosphohydroxylysine phospholyase, and the resulting lack of activity 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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Veiga-da-Cunha, M.; Verhoeven-Duif, N.M.; de Koning, T.J.; Duran, M.; Dorland, B.; Van Schaftingen, E.
Mutations in the AGXT2L2 gene cause phosphohydroxylysinuria
J. Inherit. Metab. Dis.
36
961-966
2013
Homo sapiens (Q8IUZ5), Homo sapiens
Manually annotated by BRENDA team