BRENDA - Enzyme Database show
show all sequences of 1.2.1.59

Glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaebacterium Pyrococcus woesei: characterization of the enzyme, cloning and sequencing of the gene, and expression in Escherichia coli

Zwickl, P.; Fabry, S.; Bogedain, C.; Haas, A.; Hensel, R.; J. Bacteriol. 172, 4329-4338 (1990)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
expression at high levels in Escherichia coli, the primary structure exhibits a strikingly high proportion of aromatic amino acids
Pyrococcus woesei
General Stability
General Stability
Organism
several salts stabilize against thermal inactivation, K+-citrate is most effective
Pyrococcus woesei
Inhibitors
Inhibitors
Commentary
Organism
Structure
additional information
insensitive to pentalenolactone
Pyrococcus woesei
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADP+
-
Pyrococcus woesei
1
-
NAD+
-
Pyrococcus woesei
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
phosphate
dependent on; Km: 0.04 mM
Pyrococcus woesei
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pyrococcus woesei
-
-
-
Purification (Commentary)
Commentary
Organism
-
Pyrococcus woesei
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Pyrococcus woesei
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
-
11537
Pyrococcus woesei
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
D-glyceraldehyde-3-phosphate + phosphate + NADP+
-
11537
Pyrococcus woesei
1,3-diphosphoglycerate + NADPH
-
-
-
-
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
half-life: 44 min
Pyrococcus woesei
Cloned(Commentary) (protein specific)
Commentary
Organism
expression at high levels in Escherichia coli, the primary structure exhibits a strikingly high proportion of aromatic amino acids
Pyrococcus woesei
General Stability (protein specific)
General Stability
Organism
several salts stabilize against thermal inactivation, K+-citrate is most effective
Pyrococcus woesei
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
additional information
insensitive to pentalenolactone
Pyrococcus woesei
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.01
-
NADP+
-
Pyrococcus woesei
1
-
NAD+
-
Pyrococcus woesei
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
phosphate
dependent on; Km: 0.04 mM
Pyrococcus woesei
Purification (Commentary) (protein specific)
Commentary
Organism
-
Pyrococcus woesei
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
additional information
-
-
Pyrococcus woesei
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-glyceraldehyde-3-phosphate + phosphate + NAD(P)+
-
11537
Pyrococcus woesei
1,3-diphosphoglycerate + NAD(P)H
-
-
-
-
D-glyceraldehyde-3-phosphate + phosphate + NADP+
-
11537
Pyrococcus woesei
1,3-diphosphoglycerate + NADPH
-
-
-
-
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
100
-
half-life: 44 min
Pyrococcus woesei
Other publictions for EC 1.2.1.59
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)
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725013
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Comparative analysis of two gl ...
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FEBS Lett.
586
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1
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1
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7
7
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6
-
5
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1
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10
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1
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1
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2
7
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1
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1
2
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7
7
7
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6
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1
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10
-
1
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1
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723857
Tourigny
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Campylobacter jejuni, Campylobacter jejuni NCTC 11168
Acta Crystallogr. Sect. F
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1
1
1
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4
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15
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1
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4
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725853
Kim
Alteration of reducing powers ...
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Lett. Appl. Microbiol.
52
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1
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5
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1
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2
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726605
Malay
Structure of glyceraldehyde-3- ...
Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661
Acta Crystallogr. Sect. F
65
1227-1233
2009
-
-
1
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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1
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656414
Marri
Co-ordinated gene expression o ...
Arabidopsis thaliana
J. Exp. Bot.
56
73-80
2005
-
-
-
-
-
-
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1
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3
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1
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1
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-
11538
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Functional complementation of ...
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J. Bacteriol.
179
4513-4522
1997
-
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1
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4
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2
1
-
17
-
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1
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28
2
1
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1
1
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1
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4
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2
1
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1
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28
2
1
-
-
-
1
1
-
-
-
-
-
-
-
-
11542
Serrano
-
Identification of two differen ...
Cyanophora paradoxa
Arch. Microbiol.
162
14-19
1994
-
-
-
-
-
-
-
-
2
-
2
-
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1
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1
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1
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744178
Schäfer
-
Gluconeogenesis from pyruvate ...
Pyrococcus furiosus
Arch. Microbiol.
159
354-363
1993
-
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-
-
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-
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4
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1
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4
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2
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1
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2
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4
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4
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2
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1
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1
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1
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-
11537
Zwickl
Glyceraldehyde-3-phosphate deh ...
Pyrococcus woesei
J. Bacteriol.
172
4329-4338
1990
-
-
1
-
-
1
1
2
-
1
-
-
-
7
-
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1
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1
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2
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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
-
1
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1
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1
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2
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-
-
1
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-
-
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-
11539
Fabry
Purification and characterizat ...
Methanothermus fervidus
Eur. J. Biochem.
165
147-155
1987
-
-
-
1
-
2
1
4
-
1
2
-
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1
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1
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1
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2
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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4
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1
2
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1
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1
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2
1
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1
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1
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11541
Papen
-
Properties of the glyceraldehy ...
Anabaena cylindrica, Anabaena sp., Anabaena sp. 7119, Trichormus variabilis
FEMS Microbiol. Lett.
36
201-206
1986
9
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9
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9
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9
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11540
Krusteva
-
Allosteric regulation of NAD(N ...
Auxenochlorella pyrenoidosa
FEBS Lett.
171
137-140
1984
6
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1
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