Information on EC 1.1.1.365 - D-galacturonate reductase

Word Map on EC 1.1.1.365
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.365
-
RECOMMENDED NAME
GeneOntology No.
D-galacturonate reductase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-galactonate + NADP+ = D-galacturonate + NADPH + H+
show the reaction diagram
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
-
-
D-galacturonate degradation III
-
-
L-ascorbate biosynthesis V
-
-
Metabolic pathways
-
-
Pentose and glucuronate interconversions
-
-
ascorbate metabolism
-
-
degradation of sugar acids
-
-
SYSTEMATIC NAME
IUBMB Comments
L-galactonate:NADP+ oxidoreductase
The enzyme from plants is involved in ascorbic acid (vitamin C) biosynthesis [1,2]. The enzyme from the fungus Trichoderma reesei (Hypocrea jecorina) is involved in a eukaryotic degradation pathway of D-galacturonate. It is also active with D-glucuronate and glyceraldehyde [3]. Neither enzyme shows any activity with NADH.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
anamorph Trichoderma reesei
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-galactose + NADPH + H+
?
show the reaction diagram
D-galacturonate + NADH + H+
L-galactonate + NAD+
show the reaction diagram
D-galacturonate + NADPH + H+
L-galactonate + NADP+
show the reaction diagram
D-glucose + NADPH + H+
?
show the reaction diagram
D-glucuronate + NADH + H+
?
show the reaction diagram
D-glucuronate + NADPH + H+
?
show the reaction diagram
D-glucuronic acid + NADPH + H+
?
show the reaction diagram
D-xylose + NADPH + H+
?
show the reaction diagram
-
29.9% activity compared to D-glucuronate
-
-
?
DL-glyceraldehyde + NADPH + H+
?
show the reaction diagram
L-arabinose + NADPH + H+
?
show the reaction diagram
-
14.2% activity compared to D-glucuronate
-
-
ir
L-galactonate + NAD+
D-galacturonate + NADH + H+
show the reaction diagram
-
-
-
-
r
L-galactonate + NADP+
D-galacturonate + NADPH + H+
show the reaction diagram
L-galactose + NADPH + H+
?
show the reaction diagram
-
18.8% activity compared to D-glucuronate
-
-
ir
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-galacturonate + NADPH + H+
L-galactonate + NADP+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
135.3% activity at 5 mM
additional information
-
not influenced by Ca2+, Co2+, Mn2+, Ni2+, Zn2+, and Fe2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
-
84% residual activity at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
H2O2
-
the enzyme is activated by 0.1 mM H2O2
additional information
-
not influenced by EDTA, BCS, dithiothreiol, , and p-chloromercuribenzoate, L-GalL, and AsA
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.175 - 7.11
D-galacturonate
0.12 - 4.67
D-glucuronate
11
D-glucuronic acid
-
in 100 mM sodium phosphate (pH 7.0), at 22C
8.48
D-xylose
-
in 50 mM Tris-HCl (pH 7.2), at 25C
6
DL-glyceraldehyde
-
in 100 mM sodium phosphate (pH 7.0), at 22C
4
L-galactonate
-
in 100 mM sodium phosphate (pH 7.0), at 22C
0.326
NADH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22C
0.001
NADP+
-
in 100 mM sodium phosphate (pH 7.0), at 22C
0.03 - 0.0625
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19 - 6.88
D-galacturonate
0.13 - 3.11
D-glucuronate
0.06
D-xylose
Euglena gracilis
-
in 50 mM Tris-HCl (pH 7.2), at 25C
0.08 - 0.16
L-galactonate
4.98
NADH
Aspergillus niger
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22C
7.11
NADPH
Aspergillus niger
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05095 - 39.29
D-galacturonate
1752
0.04135
D-glucuronate
Euglena gracilis
-
in 50 mM Tris-HCl (pH 7.2), at 25C
339
0.00697
D-xylose
Euglena gracilis
-
in 50 mM Tris-HCl (pH 7.2), at 25C
115
15.72
NADH
Aspergillus niger
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22C
8
197.2
NADPH
Aspergillus niger
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22C
5
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00422
-
crude extract, at pH 7.2 and at 25C
0.12
-
with NAD+ and L-galactonate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22C
0.17
-
with NADH and D-glucuronate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22C
0.21
-
with NADP+ and L-galactonate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22C
0.671
-
after 159fold purification, at pH 7.2 and at 25C
3.9
-
with NADPH and D-glucuronate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22C
6.9
-
with NADH and D-galacturonate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22C
8.7
-
with NADPH and D-galacturonate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
-
about 75, 65 and 18.5% of maximum activity at pH 6.5, 8.0 and 9.0, respectively
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
36900
-
x * 36900, isoform GAR1, calculated from amino acid sequence
38000
-
1 * 38000, SDS-PAGE
39000
-
gel filtration
40000
-
x * 40000, SDS-PAGE
44000
-
x * 44000, His6-tagged enzyme, SDS-PAGE
49200
-
x * 49200, isoform GAR2, calculated from amino acid sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
CM-Sepharose column chromatography, ammonium sulfate precipitation, butyl Toyopearl column chromatography, and HiTrap Blue column chromatography
-
Fractogel TSK DEAE-650 column chromatography
-
glutathione agarose column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Arabidopsis thaliana and in Escherichia coli XL1-Blue MRF' cells
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli DH5alpha cells
-
expressed in Saccharomyces cerevisiae strain CEN.PK2-1B
-
expressed in Solanum tuberosum cultivar Taedong Valley
-
expressed in Solanum tuberosum via Agrobacterium tumefaciens-mediated transformation
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
isoform GAR1 is induced about 10fold, while isoform GAR2 is strongly induced in cultures with D-galacturonic acid, pectate, and pectin as carbon source at 3 h after transfer, compared to continuous growth in glucose-containing culture
the enzyme is not regulated by L-galactono-1,4-lactone and ascorbate