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show all sequences of 1.1.1.B35

Identification of the missing links in prokaryotic pentose oxidation pathways: evidence for enzyme recruitment

Brouns, S.J.; Walther, J.; Snijders, A.P.; van de Werken, H.J.; Willemen, H.L.; Worm, P.; de Vos, M.G.; Andersson, A.; Lundgren, M.; Mazon, H.F.; van den Heuvel, R.H.; Nilsson, P.; Salmon, L.; de Vos, W.M.; Wright, P.C.; Bernander, R.; van der Oost, J.; J. Biol. Chem. 281, 27378-27388 (2006)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Saccharolobus solfataricus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
NADP+
pH 7.5, 80C
Saccharolobus solfataricus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
contains two zinc ions per monomer
Saccharolobus solfataricus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37291
-
4 * 37291, calculated from sequence
Saccharolobus solfataricus
149700
-
mass spectrometry
Saccharolobus solfataricus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-arabinose + NADP+
Saccharolobus solfataricus
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
D-arabinono-1,4-lactone + NADPH + H+
-
-
?
D-arabinose + NADP+
Saccharolobus solfataricus P2
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
D-arabinono-1,4-lactone + NADPH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharolobus solfataricus
Q97YM2
-
-
Saccharolobus solfataricus P2
Q97YM2
-
-
Purification (Commentary)
Commentary
Organism
-
Saccharolobus solfataricus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + NADP+
-
719837
Saccharolobus solfataricus
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-arabinose + NADP+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
719837
Saccharolobus solfataricus
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-arabinose + NADP+
-
719837
Saccharolobus solfataricus P2
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-arabinose + NADP+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
719837
Saccharolobus solfataricus P2
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-ribose + NADP+
-
719837
Saccharolobus solfataricus
D-ribonolactone + NADPH
-
-
-
?
D-ribose + NADP+
-
719837
Saccharolobus solfataricus P2
D-ribonolactone + NADPH
-
-
-
?
L-fucose + NADP+
most active with L-fucose as substrate
719837
Saccharolobus solfataricus
L-fuconolactone + NADPH
-
-
-
?
L-fucose + NADP+
most active with L-fucose as substrate
719837
Saccharolobus solfataricus P2
L-fuconolactone + NADPH
-
-
-
?
L-galactose + NADP+
-
719837
Saccharolobus solfataricus
L-galactonolactone + NADPH
-
-
-
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 37291, calculated from sequence
Saccharolobus solfataricus
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
80
-
assay at
Saccharolobus solfataricus
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
74
100
more than 50% of maximal activity
Saccharolobus solfataricus
Temperature Stability [C]
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
85
-
half-life: 42 min
Saccharolobus solfataricus
90
-
half-life: 26 min
Saccharolobus solfataricus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
17.7
-
D-ribose
pH 7.5, 80C
Saccharolobus solfataricus
17.7
-
L-galactose
pH 7.5, 80C
Saccharolobus solfataricus
23.8
-
D-arabinose
pH 7.5, 80C
Saccharolobus solfataricus
26.8
-
L-fucose
pH 7.5, 80C
Saccharolobus solfataricus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Saccharolobus solfataricus
8.2
-
-
Saccharolobus solfataricus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7.3
9.3
more than 50% of maximal activity
Saccharolobus solfataricus
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
the Km-value for NAD+ is 30fold higher compared to the Km-value for NADP+
Saccharolobus solfataricus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Saccharolobus solfataricus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
the Km-value for NAD+ is 30fold higher compared to the Km-value for NADP+
Saccharolobus solfataricus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.04
-
NADP+
pH 7.5, 80C
Saccharolobus solfataricus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
contains two zinc ions per monomer
Saccharolobus solfataricus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
37291
-
4 * 37291, calculated from sequence
Saccharolobus solfataricus
149700
-
mass spectrometry
Saccharolobus solfataricus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-arabinose + NADP+
Saccharolobus solfataricus
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
D-arabinono-1,4-lactone + NADPH + H+
-
-
?
D-arabinose + NADP+
Saccharolobus solfataricus P2
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
D-arabinono-1,4-lactone + NADPH + H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharolobus solfataricus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-arabinose + NADP+
-
719837
Saccharolobus solfataricus
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-arabinose + NADP+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
719837
Saccharolobus solfataricus
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-arabinose + NADP+
-
719837
Saccharolobus solfataricus P2
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-arabinose + NADP+
the enzyme is involved in the conversion of D-arabinose into the tricarboxylic acid cycle intermediate 2-oxoglutarate via the pentose oxidation pathway
719837
Saccharolobus solfataricus P2
D-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
D-ribose + NADP+
-
719837
Saccharolobus solfataricus
D-ribonolactone + NADPH
-
-
-
?
D-ribose + NADP+
-
719837
Saccharolobus solfataricus P2
D-ribonolactone + NADPH
-
-
-
?
L-fucose + NADP+
most active with L-fucose as substrate
719837
Saccharolobus solfataricus
L-fuconolactone + NADPH
-
-
-
?
L-fucose + NADP+
most active with L-fucose as substrate
719837
Saccharolobus solfataricus P2
L-fuconolactone + NADPH
-
-
-
?
L-galactose + NADP+
-
719837
Saccharolobus solfataricus
L-galactonolactone + NADPH
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 37291, calculated from sequence
Saccharolobus solfataricus
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
80
-
assay at
Saccharolobus solfataricus
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
74
100
more than 50% of maximal activity
Saccharolobus solfataricus
Temperature Stability [C] (protein specific)
Temperature Stability Minimum [C]
Temperature Stability Maximum [C]
Commentary
Organism
85
-
half-life: 42 min
Saccharolobus solfataricus
90
-
half-life: 26 min
Saccharolobus solfataricus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
17.7
-
D-ribose
pH 7.5, 80C
Saccharolobus solfataricus
17.7
-
L-galactose
pH 7.5, 80C
Saccharolobus solfataricus
23.8
-
D-arabinose
pH 7.5, 80C
Saccharolobus solfataricus
26.8
-
L-fucose
pH 7.5, 80C
Saccharolobus solfataricus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Saccharolobus solfataricus
8.2
-
-
Saccharolobus solfataricus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7.3
9.3
more than 50% of maximal activity
Saccharolobus solfataricus
Other publictions for EC 1.1.1.B35
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)
741519
Hu
Structures of Saccharomyces c ...
Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
69
1190-1195
2013
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
710944
Gonzalez
Role of Saccharomyces cerevisi ...
Saccharomyces cerevisiae
Appl. Environ. Microbiol.
76
670-679
2010
-
-
1
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
681445
Brouns
Crystal structure and biochemi ...
Saccharolobus solfataricus, Saccharolobus solfataricus P2
J. Mol. Biol.
371
1249-1260
2007
-
-
-
1
-
-
-
4
-
1
-
-
-
3
-
-
1
-
-
-
-
-
10
1
2
1
2
-
2
1
-
2
-
-
-
-
-
-
2
1
-
-
-
-
-
4
-
1
-
-
-
-
-
1
-
-
-
-
10
1
2
1
2
-
2
1
-
-
-
-
-
-
4
4
719837
Brouns
Identification of the missing ...
Saccharolobus solfataricus, Saccharolobus solfataricus P2
J. Biol. Chem.
281
27378-27388
2006
-
-
1
-
-
-
-
1
-
1
2
2
-
3
-
-
1
-
-
-
-
-
9
1
1
1
2
4
2
1
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
1
-
1
2
2
-
-
-
1
-
-
-
-
9
1
1
1
2
4
2
1
-
-
-
-
-
-
-
-
285774
Kim
D-Arabinose dehydrogenase and ...
Saccharomyces cerevisiae
Biochim. Biophys. Acta
1429
29-39
1998
-
-
-
-
-
-
-
4
1
-
3
1
-
1
-
-
1
-
-
-
1
-
10
2
1
-
-
-
1
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
4
1
-
3
1
-
-
-
1
-
-
1
-
10
2
1
-
-
-
1
-
-
-
-
-
-
-
-
-