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Information on EC 1.1.1.116 - D-arabinose 1-dehydrogenase (NAD+) and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q04212

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Saccharomyces cerevisiae
UNIPROT: Q04212 not found.
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
d-arabinose dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NAD(+)-specific D-arabinose dehydrogenase
-
arabinose(fucose)dehydrogenase
-
-
-
-
D-arabinose dehydrogenase
-
-
dehydrogenase, D-arabinose
-
-
-
-
NAD-pentose-dehydrogenase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
D-arabinose:NAD+ 1-oxidoreductase
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CAS REGISTRY NUMBER
COMMENTARY hide
37250-47-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
show the reaction diagram
L-fucose + NAD+
?
show the reaction diagram
-
-
-
?
L-galactose + NAD+
?
show the reaction diagram
-
-
-
?
L-xylose + NAD+
?
show the reaction diagram
-
-
-
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
show the reaction diagram
the enzyme, mainly Ara2p not Ara1p, is involved in the biosynthesis of D-erythroascorbic acid, the five-carbon analog of ascorbic acid, from exogeneous D-arabinose
-
-
?
D-arabinose + NAD+
D-arabinono-1,4-lactone + NADH
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
Ara2p is specific for NAD+, while Ara1p utilizes NADP+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
D-arabinose
substrate inhibition of Ara2p at concentrations above 5 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.78
D-arabinose
pH 8.2, 25°C, recombinant His-tagged Ara2p
4.1
NAD+
pH 8.2, 25°C, recombinant His-tagged Ara2p
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00071
NAD+-dependent Ara2p reaction in presence of 200 mM D-arabinose, native cell extract
1.8
purified recombinant His-tagged ARA2p
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9
20% of maximal activity at pH 6.5 and pH 9.0, pH profile
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ARA2; gene YMR041c or ARA2, isozyme Ara2p
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
-
ARA1 can only be detected in yeast peptone dextrose 2-DE gel images, thus higher reductive efficiency and higher cofactor availability are obtained with the alternation of cultivation condition (mainly growth medium)
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
recombinant Ara2p, gel filtration
42400
1 * 42400, recombinant Ara2p, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 42400, recombinant Ara2p, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged Ara2p from Escherichia coli by anion exchange and nickel affinity chromatography to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene YMR041c or ARA2, phylogenetic tree, expression of His6-tagged Ara2p in Escherichia coli
gene ARA1, co-overexpression of the enzyme and the D-arabinono-1,4-lactone oxidase and/or L-galactono-1,4-lactone dehydrogenase in Saccharomyces cerevisiae strains result in overproduction and accumulation of vitamin C in the culture medium, while overexpression of the D-arabinose dehydrogenase alone does not alter the L-ascorbate content, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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production of L-ascorbic acid and secretion into culture medium by overexpression of enzyme and arabinone-1,4-lactone oxidase in Saccharomyces cerevisiae and Zygosaccharomyces bailii
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sauer, M.; Branduardi, P.; Valli, M.; Porro, D.
Production of L-ascorbic acid by metabolically engineered Saccharomyces cerevisiae and Zygosaccharomyces bailii
Appl. Environ. Microbiol.
70
6086-6091
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae GRF18U
Manually annotated by BRENDA team
Amako, K.; Fujita, K.; Shimohata, T.A.; Hasegawa, E.; Kishimoto, R.; Goda, K.
NAD(+)-specific D-arabinose dehydrogenase and its contribution to erythroascorbic acid production in Saccharomyces cerevisiae
FEBS Lett.
580
6428-6434
2006
Saccharomyces cerevisiae (Q04212), Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH250 (Q04212)
Manually annotated by BRENDA team
Lin, J.; Liu, Q.; Su, E.; Wei, D.; Yang, S.
Application of comparative proteome analysis to reveal influence of cultivation conditions on asymmetric bioreduction of beta-keto ester by Saccharomyces cerevisiae
Appl. Microbiol. Biotechnol.
80
831-839
2008
Saccharomyces cerevisiae, Saccharomyces cerevisiae LH1
Manually annotated by BRENDA team