Information on EC 1.1.3.37 - D-arabinono-1,4-lactone oxidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY
1.1.3.37
-
RECOMMENDED NAME
GeneOntology No.
D-arabinono-1,4-lactone oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
D-arabinono-1,4-lactone + O2 = dehydro-D-arabinono-1,4-lactone + H2O2
show the reaction diagram
A flavoprotein (FAD). The product had previously been referred to erroneously as D-erythro-ascorbate
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dehydro-D-arabinono-1,4-lactone biosynthesis
-
-
SYSTEMATIC NAME
IUBMB Comments
D-arabinono-1,4-lactone:oxygen oxidoreductase
A flavoprotein (FAD). L-Galactono-1,4-lactone, L-gulono-1,4-lactone and L-xylono-1,4-lactone can also act as substrates but D-glucono-1,5-lactone, L-arabinono-1,4-lactone, D-galactono-1,4-lactone and D-gulono-1,4-lactone cannot [1]. With L-galactono-1,4-lactone as substrate, the product is L-ascorbate [3]. The product dehydro-D-arabinono-1,4-lactone had previously been referred to erroneously as D-erythroascorbate (CAS no.: 5776-48-7; formula: C6H8O6), although it was referred to as a five-carbon compound [1].
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ALO
-
-
-
-
L-galactono-gamma-lactone oxidase
-
-
-
-
Oxidase, D-arabinono-gamma-lactone
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
182372-12-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
AtGulLO2; isozyme AtGulLO2
UniProt
Manually annotated by BRENDA team
AtGulLO3; isozyme AtGulLO3
UniProt
Manually annotated by BRENDA team
AtGulLO5; isozyme AtGulLO5
UniProt
Manually annotated by BRENDA team
ATCC 10231
-
-
Manually annotated by BRENDA team
Leishmania donovani AG83
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
C8CCV9
the enzyme belongs to the family of flavoprotein aldonolactone oxidase/dehydrogenases
evolution
Leishmania donovani AG83
-
the enzyme belongs to the family of flavoprotein aldonolactone oxidase/dehydrogenases
-
metabolism
C8CCV9
the enzyme catalyzes the last step in the biosynthesis of L-ascorbic acid involving the conversion of an aldonolactone substrate to ascorbate (or analogues)
physiological function
C8CCV9
D-arabinono-1,4-lactone oxidase is required for synthesizing ascorbate in Leishmania
physiological function
Leishmania donovani AG83
-
D-arabinono-1,4-lactone oxidase is required for synthesizing ascorbate in Leishmania
-
metabolism
Leishmania donovani AG83
-
the enzyme catalyzes the last step in the biosynthesis of L-ascorbic acid involving the conversion of an aldonolactone substrate to ascorbate (or analogues)
-
additional information
C8CCV9
cysteine residues are required for enzyme activity
additional information
Leishmania donovani AG83
-
cysteine residues are required for enzyme activity
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Arabinono-1,4-lactone + O2
D-erythro-ascorbate + ?
show the reaction diagram
-
-
-
-
D-arabinono-1,4-lactone + O2
?
show the reaction diagram
-
final step in biosynthesis of D-erythroascorbic acid
-
-
-
D-arabinono-1,4-lactone + O2
D-erythro-ascorbate + H2O2
show the reaction diagram
-
the enzyme catalyzes the final step in the biosynthesis of D-erythroascorbic acid
-
-
?
D-arabinono-1,4-lactone + O2
dehydro-D-arabinono-1,4-lactone + H2O2
show the reaction diagram
Leishmania donovani, Leishmania donovani AG83
C8CCV9
-
-
-
?
D-arabinose + NAD+
erythroascorbic acid + NADH + H+
show the reaction diagram
-
-
-
-
?
L-Galactono-1,4-lactone + O2
?
show the reaction diagram
-
87.6% of the activity relative to D-arabinono-1,4-lactone
-
-
-
L-Gulono-1,4-lactone + O2
?
show the reaction diagram
-
24.7% of the activity relative to D-arabinono-1,4-lactone
-
-
-
L-Xylono-1,4-lactone + O2
?
show the reaction diagram
-
84.6% of the activity relative to D-arabinono-1,4-lactone
-
-
-
additional information
?
-
O81030, Q6NQ66, Q9LYD8
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producing L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
-
additional information
?
-
Leishmania donovani, Leishmania donovani AG83
C8CCV9
no activity with L-gulono-1,4-lactone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-arabinono-1,4-lactone + O2
?
show the reaction diagram
-
final step in biosynthesis of D-erythroascorbic acid
-
-
-
D-arabinono-1,4-lactone + O2
D-erythro-ascorbate + H2O2
show the reaction diagram
-
the enzyme catalyzes the final step in the biosynthesis of D-erythroascorbic acid
-
-
?
D-arabinono-1,4-lactone + O2
dehydro-D-arabinono-1,4-lactone + H2O2
show the reaction diagram
Leishmania donovani, Leishmania donovani AG83
C8CCV9
-
-
-
?
additional information
?
-
O81030, Q6NQ66, Q9LYD8
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producing L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
C8CCV9
essentially required
flavin
-
flavoprotein, the flavin may be covalently bound to the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-Galactono-1,4-lactone
-
competitive to D-arabinono-1,4-lactone
D-glucono-1,5-lactone
-
competitive to D-arabinono-1,4-lactone
D-gulono-1,4-lactone
-
competitive to D-arabinono-1,4-lactone
HgCl2
C8CCV9
68% inhibition at 0.05 mM, complete inhibition at 1 mM
iodoacetamide
-
-
iodoacetic acid
-
-
L-Arabinono-1,4-lactone
-
competitive to D-arabinono-1,4-lactone
N-ethylmaleimide
C8CCV9
complete inhibition at 0.05 mM
ZnCl2
C8CCV9
17% inhibition at 0.05 mM, 75% inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0393
D-Arabinono-1,4-lactone
C8CCV9
pH 7.5, 22C
44.1
D-Arabinono-1,4-lactone
-
-
0.78
D-arabinose
-
-
53.7
L-galactono-1,4-lactone
-
-
additional information
additional information
C8CCV9
Michaelis-Menten kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.8
D-Arabinono-1,4-lactone
C8CCV9
pH 7.5, 22C
20.9
D-Arabinono-1,4-lactone
-
-
18.3
L-galactono-1,4-lactone
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
O81030, Q6NQ66, Q9LYD8
assay at; assay at; assay at
7.5
C8CCV9
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
pH 5.0: about 20% of maximal activity, pH 8.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
C8CCV9
assay at room temperature
25
O81030, Q6NQ66, Q9LYD8
assay at; assay at; assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Leishmania donovani AG83
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
84400
-
PAGE in presence of deoxycholate
10663
110000
-
gel filtration
10663
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
C8CCV9
x * 57000, SDS-PAGE
?
Leishmania donovani AG83
-
x * 57000, SDS-PAGE
-
monomer
-
1 * 66700, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5 - 10
-
4C, 48 h, stable
10663
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
above, 1 min, complete loss of activity
10663
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freezing at -20C and thawing results in rapid and irreversible loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C, less than 50% loss of activity after 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant maltose binding protein-tagged LdALO from Escherichia coli strain BL21 (DE3) by amylose affinity chromatography, Factor Xa cleavage of maltose binding protein-tag
C8CCV9
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene AtGulLO2, transgenic expression of the isozyme in Nicotiana tabacum BY-2 cells, the overexpression does not affect the cells. Expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS is not successful; gene AtGulLO3, transgenic expression of the isozyme in Nicotiana tabacum BY-2 cells, the overexpression does not affect the cells. Expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS is not successful; gene AtGulLO5, transgenic expression of the isozyme in Nicotiana tabacum BY-2 cells, the overexpression does not affect the cells. Expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS is not successful
O81030, Q6NQ66, Q9LYD8
gene LdALO, DNA and amino acid sequence determination and analysis, phylogenetic tree, expression of maltose binding protein-tagged LdALO in Escherichia coli strain BL21 (DE3), overexpressioin Leishmania donovani
C8CCV9
expression in Escherichia coli
-
yeasts do not possess an endogenous biochemical pathway for the synthesis of vitamin C. Overexpression of D-arabinose dehydrogenase and D-arabino-1,4-lactone oxidase enhance this ability significantly, production of vitamin C from metabiolically engineered Saccharomyces cerevisaie as well as from Zygosaccharomyces bailii
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
L-gulono-1,4-lactone induces the enzyme, overview
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
C8CCV9
overexpression of LdALO in Leishmannia donovani results in better ability of survival of the parasite within the host in comparison to the vector transfectants
additional information
Leishmania donovani AG83
-
overexpression of LdALO in Leishmannia donovani results in better ability of survival of the parasite within the host in comparison to the vector transfectants
-