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

New: Word Map on EC 1.1.3.37
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
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 expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
1.1.3.37
-
RECOMMENDED NAME
GeneOntology No.
D-arabinono-1,4-lactone oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
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 hide
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].
CAS REGISTRY NUMBER
COMMENTARY hide
182372-12-9
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 10231
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
metabolism
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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 + ?
show the reaction diagram
-
-
-
-
D-arabinono-1,4-lactone + O2
D-erythro-ascorbate + H2O2
show the reaction diagram
D-arabinono-1,4-lactone + O2
dehydro-D-arabinono-1,4-lactone + H2O2
show the reaction diagram
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
?
-
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-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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
essentially required
flavin
-
flavoprotein, the flavin may be covalently bound to the enzyme
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
complete inhibition at 0.05 mM
ZnCl2
17% inhibition at 0.05 mM, 75% inhibition at 1 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0393 - 44.1
D-Arabinono-1,4-lactone
0.78
D-arabinose
-
-
53.7
L-galactono-1,4-lactone
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.8 - 20.9
D-Arabinono-1,4-lactone
18.3
L-galactono-1,4-lactone
Candida albicans
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
assay at; assay at; assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 8
-
pH 5.0: about 20% of maximal activity, pH 8.0: about 40% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
assay at room temperature
25
assay at; assay at; assay at
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
84400
-
PAGE in presence of deoxycholate
110000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 66700, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 10
-
4C, 48 h, stable
10663
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
above, 1 min, complete loss of activity
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
-
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
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
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; L-gulono-1,4-lactone induces the enzyme, overview; L-gulono-1,4-lactone induces the enzyme, overview
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information