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Information on EC 3.1.3.93 - L-galactose 1-phosphate phosphatase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9M8S8

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.93 L-galactose 1-phosphate phosphatase
IUBMB Comments
The enzyme from plants also has the activity of EC 3.1.3.25, inositol-phosphate phosphatase. The enzymes have very low activity with D-galactose 1-phosphate (cf. EC 3.1.3.94, D-galactose 1-phosphate phosphatase).
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This record set is specific for:
Arabidopsis thaliana
UNIPROT: Q9M8S8
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Word Map
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
l-gal-1-p phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
At3g02870
L-Gal-1-P phosphatase
-
SYSTEMATIC NAME
IUBMB Comments
beta-L-galactose-1-phosphate phosphohydrolase
The enzyme from plants also has the activity of EC 3.1.3.25, inositol-phosphate phosphatase. The enzymes have very low activity with D-galactose 1-phosphate (cf. EC 3.1.3.94, D-galactose 1-phosphate phosphatase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-D-glucose 1-phosphate + H2O
alpha-D-glucose + phosphate
show the reaction diagram
19% of the activity with myo-inositol
-
-
?
beta-L-galactose 1-phosphate + H2O
L-galactose + phosphate
show the reaction diagram
D-galactose 1-phosphate + H2O
D-galactose + phosphate
show the reaction diagram
16.6% of the activity with myo-inositol
-
-
?
D-inositol 3-phosphate + H2O
D-inositol + phosphate
show the reaction diagram
-
-
-
?
glycerol 2-phosphate + H2O
glycerol + phosphate
show the reaction diagram
52% of the activity with myo-inositol
-
-
?
myo-inositol 1-phosphate + H2O
myo-inositol + phosphate
show the reaction diagram
-
-
-
?
additional information
?
-
Fru 1-phosphate, Fru 1,6-bisphosphate, Glc 6-phosphate, D-alpha-glycerophosphate, sorbitol 6-phosphate, and myo-inositol 2-V show little to no hydrolysis in assays
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-inositol 3-phosphate
substrate inhibition above 0.7 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.044 - 0.107
beta-L-galactose 1-phosphate
0.191
D-inositol 3-phosphate
pH 7.5, 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.62
Mg2+
pH 7.0, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.8 - 7
at 2 mM MgCl2 and 0.5 mM L-galactose 1-phosphate
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.01
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
VTC4_ARATH
271
0
29121
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29121
x * 29121, calculated from sequence
33100
x * 39700, SDS-PAGE, x * 33100, calculated
39700
x * 39700, SDS-PAGE, x * 33100, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
P92L
mutant shows decreased ascorbate synthesis. The mutation is predicted to disrupt the positioning of catalytic amino acid residues within the active site. Accordingly, L-Gal-1-phoshate phosphatase activity in the mutant is about 50% of wild-type plants. In addition, mutant plants incorporate significantly more radiolabelfrom [2-3H]Man into L-galactosyl residues suggesting that the mutation increases the availability of GDP-L-Gal for polysaccharide synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Conklin, P.L.; Gatzek, S.; Wheeler, G.L.; Dowdle, J.; Raymond, M.J.; Rolinski, S.; Isupov, M.; Littlechild, J.A.; Smirnoff, N.
Arabidopsis thaliana VTC4 encodes L-galactose-1-P phosphatase, a plant ascorbic acid biosynthetic enzyme
J. Biol. Chem.
281
15662-15670
2006
Arabidopsis thaliana (Q9M8S8), Arabidopsis thaliana
Manually annotated by BRENDA team
Torabinejad, J.; Donahue, J.L.; Gunesekera, B.N.; Allen-Daniels, M.J.; Gillaspy, G.E.
VTC4 is a bifunctional enzyme that affects myoinositol and ascorbate biosynthesis in plants
Plant Physiol.
150
951-961
2009
Arabidopsis thaliana (Q9M8S8)
Manually annotated by BRENDA team
Laing, W.A.; Bulley, S.; Wright, M.; Cooney, J.; Jensen, D.; Barraclough, D.; MacRae, E.
A highly specific L-galactose-1-phosphate phosphatase on the path to ascorbate biosynthesis
Proc. Natl. Acad. Sci. USA
101
16976-16981
2004
Actinidia deliciosa (Q5U789), Arabidopsis thaliana (Q9M8S8), Arabidopsis thaliana Columbia-1 (Q9M8S8)
Manually annotated by BRENDA team