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 ACCESSION NO.
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 ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
PATHWAY
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 ACCESSION NO.
COMMENTARY
LITERATURE
ALO
-
-
-
-
ALO
O81030, Q6NQ66, Q9LYD8
-
ALO
Leishmania donovani AG83
C8CCV9
-
-
arabino-1,4-lactone oxidase
C8CCV9
-
arabino-1,4-lactone oxidase
Leishmania donovani AG83
C8CCV9
-
-
arabinonolactone oxidase
C8CCV9
-
arabinonolactone oxidase
Leishmania donovani AG83
C8CCV9
-
-
L-galactono-gamma-lactone oxidase
-
-
-
-
NAD+ - specific D-arabinose dehydrogenase
-
-
Oxidase, D-arabinono-gamma-lactone
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
182372-12-9
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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 ACCESSION NO.
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 ACCESSION NO.
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
C8CCV9, -
-
-
-
?
D-arabinono-1,4-lactone + O2
dehydro-D-arabinono-1,4-lactone + H2O2
show the reaction diagram
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
?
-
C8CCV9, -
no activity with L-gulono-1,4-lactone
-
-
-
additional information
?
-
Leishmania donovani AG83
C8CCV9
no activity with L-gulono-1,4-lactone
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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
C8CCV9, -
-
-
-
?
D-arabinono-1,4-lactone + O2
dehydro-D-arabinono-1,4-lactone + H2O2
show the reaction diagram
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
C8CCV9, -
essentially required
flavin
-
flavoprotein, the flavin may be covalently bound to the enzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
18.8
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
O81030, Q6NQ66, Q9LYD8
assay at; assay at; assay at
7.5
-
C8CCV9, -
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
8
-
pH 5.0: about 20% of maximal activity, pH 8.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22
-
C8CCV9, -
assay at room temperature
25
-
O81030, Q6NQ66, Q9LYD8
assay at; assay at; assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Leishmania donovani AG83
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
84400
-
-
PAGE in presence of deoxycholate
110000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
C8CCV9, -
x * 57000, SDS-PAGE
?
Leishmania donovani AG83
-
x * 57000, SDS-PAGE
-
monomer
-
1 * 66700, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
10
-
4C, 48 h, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50
-
-
above, 1 min, complete loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
repeated freezing at -20C and thawing results in rapid and irreversible loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, less than 50% loss of activity after 2 months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
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 ACCESSION NO.
LITERATURE
L-gulono-1,4-lactone induces the enzyme, overview; L-gulono-1,4-lactone induces the enzyme, overview; L-gulono-1,4-lactone induces the enzyme, overview
O81030, Q6NQ66, Q9LYD8
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
-