BRENDA - Enzyme Database show
show all sequences of 1.1.1.116

Production of L-ascorbic acid by metabolically engineered Saccharomyces cerevisiae and Zygosaccharomyces bailii

Sauer, M.; Branduardi, P.; Valli, M.; Porro, D.; Appl. Environ. Microbiol. 70, 6086-6091 (2004)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
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
Saccharomyces cerevisiae
Cloned(Commentary)
Commentary
Organism
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
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-arabinose + NAD+
Saccharomyces cerevisiae
-
D-arabinono-1,4-lactone + NADH
-
-
?
D-arabinose + NAD+
Saccharomyces cerevisiae GRF18U
-
D-arabinono-1,4-lactone + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
recombinant enzyme overexpressed in Saccharomyces cerevisiae and Zygosaccharomyces bailii; strain GRF18U, gene ARA1
-
Saccharomyces cerevisiae GRF18U
-
strain GRF18U, gene ARA1
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
additional information
-
-
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + NAD+
-
654283
Saccharomyces cerevisiae
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-arabinose + NAD+
-
654283
Saccharomyces cerevisiae GRF18U
D-arabinono-1,4-lactone + NADH
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Saccharomyces cerevisiae
Application (protein specific)
Application
Commentary
Organism
synthesis
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
Saccharomyces cerevisiae
Cloned(Commentary) (protein specific)
Commentary
Organism
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
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-arabinose + NAD+
Saccharomyces cerevisiae
-
D-arabinono-1,4-lactone + NADH
-
-
?
D-arabinose + NAD+
Saccharomyces cerevisiae GRF18U
-
D-arabinono-1,4-lactone + NADH
-
-
?
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
additional information
-
-
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + NAD+
-
654283
Saccharomyces cerevisiae
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-arabinose + NAD+
-
654283
Saccharomyces cerevisiae GRF18U
D-arabinono-1,4-lactone + NADH
-
-
-
?
Other publictions for EC 1.1.1.116
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [░C]
Temperature Range [░C]
Temperature Stability [░C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [░C] (protein specific)
Temperature Range [░C] (protein specific)
Temperature Stability [░C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
695806
Lin
Application of comparative pro ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae LH1
Appl. Microbiol. Biotechnol.
80
831-839
2008
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2
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1
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1
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668641
Amako
NAD(+)-specific D-arabinose de ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae YPH250
FEBS Lett.
580
6428-6434
2006
-
-
1
-
1
-
1
2
-
-
2
2
-
4
-
-
1
-
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-
2
-
11
1
1
-
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1
1
-
1
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-
1
1
-
1
-
-
1
-
2
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2
2
-
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1
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2
-
11
1
1
-
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-
1
1
-
-
-
-
-
-
-
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668709
Baroja-Mazo
Characterisation and biosynthe ...
Phycomyces blakesleeanus
Fungal Genet. Biol.
42
390-402
2005
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1
3
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3
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1
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3
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1
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1
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4
1
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654283
Sauer
Production of L-ascorbic acid ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae GRF18U
Appl. Environ. Microbiol.
70
6086-6091
2004
-
1
1
-
-
-
-
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-
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-
2
-
8
-
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-
1
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2
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1
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1
1
1
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2
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1
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2
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285774
Kim
D-Arabinose dehydrogenase and ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1429
29-39
1998
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4
1
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3
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2
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1
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1
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6
1
1
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1
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1
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4
1
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1
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6
1
1
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1
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10663
Kim
D-Arabinose dehydrogenase and ...
Candida albicans
Biochim. Biophys. Acta
1297
1-8
1996
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9
4
1
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2
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2
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1
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1
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5
1
1
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1
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1
1
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1
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9
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4
1
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2
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1
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1
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5
1
1
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1
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1
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285771
Carrasco
Genetic and biochemical charac ...
Neurospora crassa
J. Bacteriol.
145
164-170
1981
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2
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2
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2
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1
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1
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1
1
1
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1
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1
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1
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1
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2
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2
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1
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1
1
1
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1
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1
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285772
Yamanaka
-
Specific microassay of D-arabi ...
Pseudomonas sp.
Agric. Biol. Chem.
39
2227-2234
1975
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2
4
-
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1
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1
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4
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1
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1
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1
2
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2
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2
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4
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1
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4
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1
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1
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1
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285770
Carper
Arabinose (fucose) dehydrogena ...
Sus scrofa
Biochim. Biophys. Acta
358
49-56
1974
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3
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5
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1
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1
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285768
Pincheira G.; Leon G.; Ureta
Aldosugar dehydrogenases from ...
Neurospora crassa
FEBS Lett.
30
111-114
1973
-
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2
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2
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1
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1
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8
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8
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285769
Maijub
Arabinose (fucose) dehydrogena ...
Sus scrofa
Biochim. Biophys. Acta
315
37-42
1973
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1
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3
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1
1
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1
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1
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1
2
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3
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1
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1
1
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1
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3
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1
1
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1
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1
2
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3
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1
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1
1
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285767
Schiwara
Differenzierung verschiedener ...
Sus scrofa
Hoppe-Seyler's Z. Physiol. Chem.
349
1575-1581
1968
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4
5
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1
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1
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7
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1
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1
1
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2
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2
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4
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7
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1
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1
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