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Information on EC 1.1.1.365 - D-galacturonate reductase
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EC Tree
1.1.1.365 D-galacturonate reductaseIUBMB Comments
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 . Neither enzyme shows any activity with NADH.
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Word Map
- 1.1.1.365
-
l-ascorbic
- pectin
- ascorbate
- asa
- galurs
- dehydratase
- niger
-
hypocrea
-
ripening
- strawberry
- jecorina
-
ripe
- l-galactono-1,4-lactone
- l-galactose
-
trichoderma
-
solanum
- reesei
- l-gulono-1,4-lactone
-
pectin-rich
- gdp-d-mannose
-
d-glucuronic
- dehydroascorbate
- synthesis
- nutrition
The enzyme appears in viruses and cellular organisms
Synonyms
d-galacturonate reductase, d-galacturonic acid reductase, fagalur, galacturonate reductase, nadph-dependent d-galacturonate reductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AKR2
AnGar1
Cd-GAR
D-galacturonate reductase
D-galacturonic acid reductase
D-galacturonic acid reductases
FaGalUR
gaaA
GalA reductase
galacturonate reductase
GalUR
gar1
GAR2
NADPH-dependent D-galacturonate reductase
GalUR
-
-
-
-
gar1
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-galactonate + NADP+ = aldehydo-D-galacturonate + NADPH + H+
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-arabinose + NADPH + H+
?
-
14.2% activity compared to D-glucuronate
-
-
ir
L-galactose + NADPH + H+
?
-
18.8% activity compared to D-glucuronate
-
-
ir
D-galactose + NADPH + H+
?
-
14.9% activity compared to D-glucuronate
-
-
ir
D-galactose + NADPH + H+
?
-
14.9% activity compared to D-glucuronate
-
-
ir
D-galacturonate + NADH + H+
L-galactonate + NAD+
-
17.7% activity compared to NADPH
-
-
ir
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
HV538330
-
-
-
r
D-glucose + NADPH + H+
?
-
14.6% activity compared to D-glucuronate
-
-
ir
D-glucuronate + NADPH + H+
?
-
82.4% activity compared to D-glucuronate
-
-
?
D-glucuronate + NADPH + H+
?
-
82.4% activity compared to D-glucuronate
-
-
?
DL-glyceraldehyde + NADPH + H+
?
-
14.2% activity compared to D-glucuronate
-
-
ir
additional information
?
-
-
the enzyme does not catalyze the reverse reaction with L-galactonate and NADP+ and does not utilize 4-nitrobenzaldehyde or menadione
-
-
?
additional information
?
-
-
the enzyme does not catalyze the reverse reaction with L-galactonate and NADP+ and does not utilize 4-nitrobenzaldehyde or menadione
-
-
?
additional information
?
-
HV538330
optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview
-
-
?
additional information
?
-
-
optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview
-
-
?
additional information
?
-
HV538330
optimization of conversion of D-galacturonic acid to L-galactonic acid by recombinant enzyme in Saccharomyces cerevisiae, overview
-
-
?
additional information
?
-
-
the enzyme catalyzes the reduction of the C-1 carbon of D-glucuronate and C-4 epimer D-galacturonate to their corresponding aldonic acids. It is active on both glucuronic acid and galacturonic acid, with similar substrate specificities using the preferred cosubstrate NADPH. Substrate acceptance extends to lactone congeners, and D-glucurono-3,6-lactone is converted to L-gulono-1,4-lactone
-
-
-
additional information
?
-
-
no activity with NADH and D-glucose, D-fructose, D-xylose, D-galactose, L-arabinose, or D-mannose. No backward reaction with L-gulonic acid, glycerol, D-arabitol, L-arabitol, xylitol, galactitol, or ribitol
-
-
?
additional information
?
-
-
no activity with NADH and D-glucose, D-fructose, D-xylose, D-galactose, L-arabinose, or D-mannose. No backward reaction with L-gulonic acid, glycerol, D-arabitol, L-arabitol, xylitol, galactitol, or ribitol
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
r
D-galacturonate + NADPH + H+
L-galactonate + NADP+
-
-
-
?
D-galacturonate + NADPH + H+
L-galactonate + NADP+
HV538330
-
-
-
r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme accepts NADPH as well as NADH as cofactor. But its catalytic efficiency for GalA reduction is approximately 50fold higher with NADPH than with NADH
-
additional information
the enzyme accepts NADPH as well as NADH as cofactor. But its catalytic efficiency for GalA reduction is approximately 50fold higher with NADPH than with NADH
-
additional information
the enzyme accepts NADPH as well as NADH as cofactor. But its catalytic efficiency for GalA reduction is approximately 50fold higher with NADPH than with NADH
-
additional information
-
the wild-type enzyme Gar1 accepts NADPH but not NADH as cofactor
-
additional information
the wild-type enzyme Gar1 accepts NADPH but not NADH as cofactor
-
additional information
the wild-type enzyme Gar1 accepts NADPH but not NADH as cofactor
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
not influenced by Ca2+, Co2+, Mn2+, Ni2+, Zn2+, and Fe2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADP+
mutant enzyme R267L shows a considerable sensitivity at the lower (0.16 mM) but not at the higher (0.8 mM) NADH concentration
additional information
-
substrate inhibition by aldonic acids. The products L-galactonate and L-galactono-1,4-lactone are observed to mitigate substrate inhibition by galacturonate, with the lactone having a greater effect than the acid
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
not influenced by EDTA, BCS, dithiothreiol, , and p-chloromercuribenzoate, L-GalL, and AsA
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.326
NADH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.175
D-galacturonate
-
with NADPH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
7.11
D-galacturonate
-
with NADH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.036
NADPH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4.98
NADH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
7.11
NADPH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
5.45
D-galacturonate
-
with NADH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
6.88
D-galacturonate
-
with NADPH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.13
D-glucuronate
-
with NADH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
3.11
D-glucuronate
-
with NADPH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.08
L-galactonate
-
with NAD+ as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.16
L-galactonate
-
with NADP+ as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.72
NADH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
197.2
NADPH
-
with D-galacturonate as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.767
D-galacturonate
-
with NADH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
39.29
D-galacturonate
-
with NADPH as cosubstrate, in 10 mM sodium phosphate, at pH 7.2 and 22°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.12
-
with NAD+ and L-galactonate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.17
-
with NADH and D-glucuronate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22°C
0.21
-
with NADP+ and L-galactonate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22°C
3.9
-
with NADPH and D-glucuronate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22°C
6.9
-
with NADH and D-galacturonate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22°C
8.7
-
with NADPH and D-galacturonate as substrates, in 10 mM sodium phosphate, at pH 7.2 and 22°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE