BRENDA - Enzyme Database show
show all sequences of 1.1.1.116

Specific microassay of D-arabinose and L-fucose with D-arabinose (L-fucose) dehydrogenase

Yamanaka, K.; Agric. Biol. Chem. 39, 2227-2234 (1975)
No PubMed abstract available

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
D-glucose
excess concentration
Pseudomonas sp.
L-Xylose
excess concentration
Pseudomonas sp.
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.048
-
NADP+
-
Pseudomonas sp.
0.087
-
NAD+
-
Pseudomonas sp.
0.18
-
L-fucose
-
Pseudomonas sp.
0.5
-
D-arabinose
-
Pseudomonas sp.
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas sp.
-
-
-
Purification (Commentary)
Commentary
Organism
-
Pseudomonas sp.
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + NAD+
-
285772
Pseudomonas sp.
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-xylose + NAD+
no substrate for bacterial enzyme
285772
Pseudomonas sp.
D-xylono-1,4-lactone + NADH
-
-
-
?
L-fucose + NAD+
-
285772
Pseudomonas sp.
L-fuconolactone + NADH
-
-
-
-
additional information
no substrates for the bacterial enzyme are D-lyxose, D-fucose, L-rhamnose, 2-deoxy-D-glucose, D-fructose, sucrose, xylitol, L-arabitol, D-arabitol, ribitol, D-sorbitol, D-mannitol, D-galactose, D-mannose
285772
Pseudomonas sp.
?
-
-
-
-
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Pseudomonas sp.
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.6
-
Tris/HCl buffer
Pseudomonas sp.
pH Stability
pH Stability
pH Stability Maximum
Commentary
Organism
7
8
-
Pseudomonas sp.
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas sp.
NADP+
66% as effective as NAD+; as effective as NAD+
Pseudomonas sp.
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
-
Pseudomonas sp.
NADP+
66% as effective as NAD+; as effective as NAD+
Pseudomonas sp.
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-glucose
excess concentration
Pseudomonas sp.
L-Xylose
excess concentration
Pseudomonas sp.
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.048
-
NADP+
-
Pseudomonas sp.
0.087
-
NAD+
-
Pseudomonas sp.
0.18
-
L-fucose
-
Pseudomonas sp.
0.5
-
D-arabinose
-
Pseudomonas sp.
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pseudomonas sp.
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + NAD+
-
285772
Pseudomonas sp.
D-arabinono-1,4-lactone + NADH
-
-
-
?
D-xylose + NAD+
no substrate for bacterial enzyme
285772
Pseudomonas sp.
D-xylono-1,4-lactone + NADH
-
-
-
?
L-fucose + NAD+
-
285772
Pseudomonas sp.
L-fuconolactone + NADH
-
-
-
-
additional information
no substrates for the bacterial enzyme are D-lyxose, D-fucose, L-rhamnose, 2-deoxy-D-glucose, D-fructose, sucrose, xylitol, L-arabitol, D-arabitol, ribitol, D-sorbitol, D-mannitol, D-galactose, D-mannose
285772
Pseudomonas sp.
?
-
-
-
-
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Pseudomonas sp.
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.6
-
Tris/HCl buffer
Pseudomonas sp.
pH Stability (protein specific)
pH Stability
pH Stability Maximum
Commentary
Organism
7
8
-
Pseudomonas sp.
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
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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
-
-
-
2
-
11
1
1
-
-
-
1
1
-
1
-
-
-
-
-
1
1
-
1
-
-
1
-
2
-
-
2
2
-
-
-
1
-
-
2
-
11
1
1
-
-
-
1
1
-
-
-
-
-
-
-
-
668709
Baroja-Mazo
Characterisation and biosynthe ...
Phycomyces blakesleeanus
Fungal Genet. Biol.
42
390-402
2005
-
-
-
-
-
-
-
-
-
-
1
3
-
3
-
-
1
-
-
1
-
-
4
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
3
-
-
-
1
-
1
-
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
654283
Sauer
Production of L-ascorbic acid ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae GRF18U
Appl. Environ. Microbiol.
70
6086-6091
2004
-
1
1
-
-
-
-
-
-
-
-
2
-
8
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285774
Kim
D-Arabinose dehydrogenase and ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1429
29-39
1998
-
-
-
-
-
-
-
4
1
-
3
-
-
2
-
-
1
-
-
-
1
-
6
1
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
4
1
-
3
-
-
-
-
1
-
-
1
-
6
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
10663
Kim
D-Arabinose dehydrogenase and ...
Candida albicans
Biochim. Biophys. Acta
1297
1-8
1996
-
-
-
-
-
-
9
4
1
-
2
-
-
2
-
-
1
-
-
-
1
-
5
1
1
-
-
-
1
-
1
1
-
-
-
-
-
-
1
-
-
-
-
9
-
4
1
-
2
-
-
-
-
1
-
-
1
-
5
1
1
-
-
-
1
-
1
-
-
-
-
-
-
-
285771
Carrasco
Genetic and biochemical charac ...
Neurospora crassa
J. Bacteriol.
145
164-170
1981
-
-
-
-
-
-
-
2
-
-
2
-
-
2
-
-
1
-
-
-
1
-
1
1
1
-
1
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
2
-
-
2
-
-
-
-
1
-
-
1
-
1
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
285772
Yamanaka
-
Specific microassay of D-arabi ...
Pseudomonas sp.
Agric. Biol. Chem.
39
2227-2234
1975
-
-
-
-
-
-
2
4
-
-
-
-
-
1
-
-
1
-
-
-
-
-
4
-
1
-
-
-
1
-
1
2
-
-
-
-
-
-
2
-
-
-
-
2
-
4
-
-
-
-
-
-
-
1
-
-
-
-
4
-
1
-
-
-
1
-
1
-
-
-
-
-
-
-
285770
Carper
Arabinose (fucose) dehydrogena ...
Sus scrofa
Biochim. Biophys. Acta
358
49-56
1974
-
-
-
-
-
-
3
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
5
-
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
1
-
-
5
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
285768
Pincheira G.; Leon G.; Ureta
Aldosugar dehydrogenases from ...
Neurospora crassa
FEBS Lett.
30
111-114
1973
-
-
-
-
-
2
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
8
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
2
-
-
-
2
-
-
-
-
-
-
-
1
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
285769
Maijub
Arabinose (fucose) dehydrogena ...
Sus scrofa
Biochim. Biophys. Acta
315
37-42
1973
-
-
-
-
-
1
-
3
-
-
1
1
-
1
-
-
1
-
-
1
2
-
3
-
1
-
-
-
1
1
-
1
-
-
-
-
-
-
1
-
-
1
-
-
-
3
-
-
1
1
-
-
-
1
-
1
2
-
3
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-
285767
Schiwara
Differenzierung verschiedener ...
Sus scrofa
Hoppe-Seyler's Z. Physiol. Chem.
349
1575-1581
1968
-
-
-
-
-
-
4
5
-
-
-
-
-
1
-
-
1
-
-
1
-
-
7
-
1
-
-
-
1
1
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
5
-
-
-
-
-
-
-
1
-
1
-
-
7
-
1
-
-
-
1
1
-
-
-
-
-
-
-
-