BRENDA - Enzyme Database show
show all sequences of 1.1.1.179

Identification in the mould Hypocrea jecorina of a gene encoding an NADP(+):D-xylose dehydrogenase

Berghaell, S.; Hilditch, S.; Penttilae, M.; Richard, P.; FEMS Microbiol. Lett. 277, 249-253 (2007)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene xyd1, DNA and amino acid sequence determination and analysis, functional expression of the His-tagged enzyme in Saccharomyces cerevisiae
Trichoderma reesei
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics, recombinant enzyme
Trichoderma reesei
5.7
-
D-glucose
pH 8.0, 30C, recombinant enzyme
Trichoderma reesei
24
-
NADP+
pH 8.1, 30C, recombinant enzyme
Trichoderma reesei
43
-
D-xylose
pH 8.1, 30C, recombinant enzyme
Trichoderma reesei
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Trichoderma reesei
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42720
-
x * 42720, sequence calculation
Trichoderma reesei
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-xylose + NADP+
Trichoderma reesei
best substrate
D-xylono-1,5-lactone + NADPH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Trichoderma reesei
A8BT09
i.e. Trichoderma reesei, strain VTT-D-80133, gene xyd1
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
Trichoderma reesei
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
substrate specificity
Trichoderma reesei
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galactose + NADP+
-
686797
Trichoderma reesei
D-galactono-1,5-lactone + NADPH
-
-
-
?
D-glucose + NADP+
-
686797
Trichoderma reesei
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-ribose + NADP+
low activity
686797
Trichoderma reesei
? + NADPH
-
-
-
?
D-xylose + NADP+
best substrate
686797
Trichoderma reesei
D-xylono-1,5-lactone + NADPH + H+
-
-
-
?
L-arabinose + NADP+
-
686797
Trichoderma reesei
L-arabinono-1,4-lactone + NADPH
-
-
-
?
additional information
no or poor activity with D-arabinose, D-mannose, L-rhamnose, D-lyxose, D-fructose, D-glyceraldehyde, and DL-glyceraldehyde
686797
Trichoderma reesei
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 42720, sequence calculation
Trichoderma reesei
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Trichoderma reesei
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.7
-
D-glucose
pH 8.0, 30C, recombinant enzyme
Trichoderma reesei
21.8
-
D-xylose
pH 8.1, 30C, recombinant enzyme
Trichoderma reesei
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
assay at
Trichoderma reesei
Cofactor
Cofactor
Commentary
Organism
Structure
NADP+
dependent on, specific for
Trichoderma reesei
Cloned(Commentary) (protein specific)
Commentary
Organism
gene xyd1, DNA and amino acid sequence determination and analysis, functional expression of the His-tagged enzyme in Saccharomyces cerevisiae
Trichoderma reesei
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADP+
dependent on, specific for
Trichoderma reesei
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetics, recombinant enzyme
Trichoderma reesei
5.7
-
D-glucose
pH 8.0, 30C, recombinant enzyme
Trichoderma reesei
24
-
NADP+
pH 8.1, 30C, recombinant enzyme
Trichoderma reesei
43
-
D-xylose
pH 8.1, 30C, recombinant enzyme
Trichoderma reesei
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Trichoderma reesei
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
42720
-
x * 42720, sequence calculation
Trichoderma reesei
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
D-xylose + NADP+
Trichoderma reesei
best substrate
D-xylono-1,5-lactone + NADPH + H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Saccharomyces cerevisiae by nickel affinity chromatography
Trichoderma reesei
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
additional information
-
substrate specificity
Trichoderma reesei
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-galactose + NADP+
-
686797
Trichoderma reesei
D-galactono-1,5-lactone + NADPH
-
-
-
?
D-glucose + NADP+
-
686797
Trichoderma reesei
D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-ribose + NADP+
low activity
686797
Trichoderma reesei
? + NADPH
-
-
-
?
D-xylose + NADP+
best substrate
686797
Trichoderma reesei
D-xylono-1,5-lactone + NADPH + H+
-
-
-
?
L-arabinose + NADP+
-
686797
Trichoderma reesei
L-arabinono-1,4-lactone + NADPH
-
-
-
?
additional information
no or poor activity with D-arabinose, D-mannose, L-rhamnose, D-lyxose, D-fructose, D-glyceraldehyde, and DL-glyceraldehyde
686797
Trichoderma reesei
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 42720, sequence calculation
Trichoderma reesei
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
30
-
assay at
Trichoderma reesei
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
5.7
-
D-glucose
pH 8.0, 30C, recombinant enzyme
Trichoderma reesei
21.8
-
D-xylose
pH 8.1, 30C, recombinant enzyme
Trichoderma reesei
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
assay at
Trichoderma reesei
Other publictions for EC 1.1.1.179
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)
723749
Mihasan
Evidence of a plasmid-encoded ...
Paenarthrobacter nicotinovorans
Res. Microbiol.
164
22-30
2013
-
-
1
-
-
-
-
3
-
1
1
-
-
1
-
-
-
-
-
-
-
-
3
1
-
-
-
3
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
3
-
1
1
-
-
-
-
-
-
-
-
-
3
1
-
-
-
3
-
-
-
-
-
-
-
-
3
3
724150
Ahmed
-
Oxidation and reduction of D-x ...
Ogataea angusta
Aust. J. Basic Appl. Sci.
5
95-100
2011
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
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-
2
-
-
-
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-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
725867
Nygard
Bioconversion of d-xylose to d ...
Trichoderma reesei
Metab. Eng.
13
383-391
2011
-
1
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
1
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
698940
Johnsen
D-xylose degradation pathway i ...
Haloferax volcanii, Haloferax volcanii DS2, Haloferax volcanii GR501
J. Biol. Chem.
284
27290-27303
2009
1
-
1
-
1
-
-
6
-
-
3
2
-
4
-
-
1
-
-
1
3
-
12
1
-
-
-
-
-
-
-
2
-
-
-
1
-
2
2
-
1
-
-
-
-
6
-
-
3
2
-
-
-
1
-
1
3
-
12
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
684150
Carbone
Structure of monkey dimeric di ...
Macaca fascicularis
Acta Crystallogr. Sect. D
64
532-542
2008
-
-
1
1
15
-
2
13
-
-
-
2
-
2
-
-
1
-
-
-
-
-
2
1
-
-
-
8
1
-
-
1
-
-
-
-
-
1
1
1
15
-
-
2
-
13
-
-
-
2
-
-
-
1
-
-
-
-
2
1
-
-
-
8
1
-
-
-
-
-
-
-
-
-
686797
Berghaell
Identification in the mould Hy ...
Trichoderma reesei
FEMS Microbiol. Lett.
277
249-253
2007
-
-
1
-
-
-
-
4
-
1
1
1
-
1
-
-
1
-
-
-
1
-
6
1
1
-
-
2
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
4
-
1
1
1
-
-
-
1
-
-
1
-
6
1
1
-
-
2
1
-
-
-
-
-
-
-
-
-
655884
Johnsen
Novel xylose dehydrogenase in ...
Haloarcula marismortui
J. Bacteriol.
186
6198-6207
2004
-
-
1
-
-
-
-
3
-
3
2
1
-
1
-
-
1
-
-
1
1
-
5
1
2
1
-
3
1
1
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
3
-
3
2
1
-
-
-
1
-
1
1
-
5
1
2
1
-
3
1
1
-
-
-
-
-
-
3
3
286128
Aoki
Identity of dimeric dihydrodio ...
Canis lupus familiaris, Homo sapiens, Macaca fuscata, Oryctolagus cuniculus, Sus scrofa
Chem. Biol. Interact.
130-132
775-784
2001
4
-
-
-
2
-
1
4
-
-
-
5
-
10
-
-
4
1
-
8
2
-
18
-
-
-
-
-
8
-
-
7
-
-
-
4
-
-
7
-
2
-
-
1
-
4
-
-
-
5
-
-
-
4
-
8
2
-
18
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
286127
Asada
Roles of His-79 and Tyr-180 of ...
Macaca fuscata
Biochem. Biophys. Res. Commun.
278
333-337
2000
1
-
1
-
2
-
1
9
-
-
2
-
-
1
-
-
1
-
-
1
3
-
3
1
-
-
-
-
-
-
-
1
-
-
-
1
-
1
1
-
2
-
-
1
-
9
-
-
2
-
-
-
-
1
-
1
3
-
3
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286126
Zepeda
NADP(+)-dependent D-xylose deh ...
Sus scrofa
Biochem. J.
266
637-644
1990
-
-
-
-
-
-
2
9
-
-
2
-
-
1
-
-
1
1
-
1
1
-
7
1
1
-
-
7
1
-
-
2
-
-
-
-
-
-
2
-
-
-
-
2
-
9
-
-
2
-
-
-
-
1
-
1
1
-
7
1
1
-
-
7
1
-
-
-
-
-
-
-
-
-
286124
Wissler
-
D-Xylose:NADP+ oxidoreductase ...
Bos taurus, Canis lupus familiaris, Sus scrofa
Hoppe-Seyler's Z. Physiol. Chem.
358
1300-1301
1977
-
-
-
-
-
-
-
-
-
-
3
-
-
3
-
-
-
-
-
7
-
-
24
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
7
-
-
24
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
286125
Suzuki
Oxidation and reduction of D-x ...
Starmera quercuum
Appl. Microbiol.
25
850-852
1973
-
-
-
-
-
-
-
-
-
-
-
-
-
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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