BRENDA - Enzyme Database
show all sequences of 1.1.1.388

The oxidative pentose phosphate pathway in the haloarchaeon Haloferax volcanii involves a novel type of glucose-6-phosphate dehydrogenase - The archaeal Zwischenferment

Pickl, A.; Schönheit, P.; FEBS Lett. 589, 1108-1111 (2015)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
-
Haloferax volcanii
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.18
-
NAD+
pH 7.5, 42°C
Haloferax volcanii
5.4
-
D-glucose 6-phosphate
pH 7.5, 42°C
Haloferax volcanii
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
KCl
highest activity at about 3 M KCl
Haloferax volcanii
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
2 * 34000, SDS-PAGE
Haloferax volcanii
59000
-
gel filtration
Haloferax volcanii
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
D-glucose 6-phosphate + NADP+
Haloferax volcanii
the enzyme is functionally involved in pentose phosphate formation in vivo
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
?
D-glucose 6-phosphate + NADP+
Haloferax volcanii DSM 3757
the enzyme is functionally involved in pentose phosphate formation in vivo
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Haloferax volcanii
D4GS48
-
-
Haloferax volcanii DSM 3757
D4GS48
-
-
Purification (Commentary)
Purification (Commentary)
Organism
-
Haloferax volcanii
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
42
-
pH 7.5, 42°C
Haloferax volcanii
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
D-glucose 6-phosphate + NAD+
the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor
729742
Haloferax volcanii
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose 6-phosphate + NAD+
the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor
729742
Haloferax volcanii DSM 3757
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
the enzyme is functionally involved in pentose phosphate formation in vivo
729742
Haloferax volcanii
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
the enzyme is functionally involved in pentose phosphate formation in vivo
729742
Haloferax volcanii DSM 3757
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
dimer
2 * 34000, SDS-PAGE
Haloferax volcanii
Synonyms
Synonyms
Commentary
Organism
archaeal zwischenferment
-
Haloferax volcanii
azf
-
Haloferax volcanii
Glc6PDH
ambiguous
Haloferax volcanii
HVO_0511
locus name
Haloferax volcanii
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.18
-
NAD+
pH 7.5, 42°C
Haloferax volcanii
5.4
-
D-glucose 6-phosphate
pH 7.5, 42°C
Haloferax volcanii
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Haloferax volcanii
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
the catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor
Haloferax volcanii
Cloned(Commentary) (protein specific)
Commentary
Organism
-
Haloferax volcanii
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
the catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor
Haloferax volcanii
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.18
-
NAD+
pH 7.5, 42°C
Haloferax volcanii
5.4
-
D-glucose 6-phosphate
pH 7.5, 42°C
Haloferax volcanii
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
KCl
highest activity at about 3 M KCl
Haloferax volcanii
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
2 * 34000, SDS-PAGE
Haloferax volcanii
59000
-
gel filtration
Haloferax volcanii
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
D-glucose 6-phosphate + NADP+
Haloferax volcanii
the enzyme is functionally involved in pentose phosphate formation in vivo
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
?
D-glucose 6-phosphate + NADP+
Haloferax volcanii DSM 3757
the enzyme is functionally involved in pentose phosphate formation in vivo
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Haloferax volcanii
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
42
-
pH 7.5, 42°C
Haloferax volcanii
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
D-glucose 6-phosphate + NAD+
the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor
729742
Haloferax volcanii
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose 6-phosphate + NAD+
the enzyme is specific for D-glucose 6-phosphate. D-Glucose is not oxidized at significant rates. The catalytic efficiency of the enzyme for NAD+ (263/s*mM) is about 230-fold higher than for NADP+ (1.13/s*mM), indicating NAD+ to be the physiological electron acceptor
729742
Haloferax volcanii DSM 3757
6-phospho-D-glucono-1,5-lactone + NADH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
the enzyme is functionally involved in pentose phosphate formation in vivo
729742
Haloferax volcanii
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
D-glucose 6-phosphate + NADP+
the enzyme is functionally involved in pentose phosphate formation in vivo
729742
Haloferax volcanii DSM 3757
6-phospho-D-glucono-1,5-lactone + NADPH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
dimer
2 * 34000, SDS-PAGE
Haloferax volcanii
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.18
-
NAD+
pH 7.5, 42°C
Haloferax volcanii
5.4
-
D-glucose 6-phosphate
pH 7.5, 42°C
Haloferax volcanii
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.5
-
-
Haloferax volcanii
General Information
General Information
Commentary
Organism
malfunction
compared to the wild type, the DELTAazf strain does not grow, but growth was fully recovered by in-trans complementation with azf. Growth of the deletion mutant can also be recovered by the addition of uridine to the medium, suggesting that Haloferax volcanii can circumvent the metabolic block for pentose phosphate formation via the oxidative pentose phosphate pathway by converting uridine to ribose-5-phosphate, catalyzed by uridine phosphorylase and phosphopentomutase
Haloferax volcanii
physiological function
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
Haloferax volcanii
General Information (protein specific)
General Information
Commentary
Organism
malfunction
compared to the wild type, the DELTAazf strain does not grow, but growth was fully recovered by in-trans complementation with azf. Growth of the deletion mutant can also be recovered by the addition of uridine to the medium, suggesting that Haloferax volcanii can circumvent the metabolic block for pentose phosphate formation via the oxidative pentose phosphate pathway by converting uridine to ribose-5-phosphate, catalyzed by uridine phosphorylase and phosphopentomutase
Haloferax volcanii
physiological function
the enzyme is essential for the biosynthesis of pentose phosphates from glucose-6-phosphate during growth of Haloferax volcanii on glucose as growth substrate
Haloferax volcanii
Other publictions for EC 1.1.1.388
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
Synonyms
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)
729742
Pickl
The oxidative pentose phosphat ...
Haloferax volcanii, Haloferax volcanii DSM 3757
FEBS Lett.
589
1108-1111
2015
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1
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2
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1
2
2
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7
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1
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-
1
-
4
1
4
-
-
-
2
1
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
2
-
1
2
2
-
-
-
1
-
-
1
-
4
1
-
-
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2
1
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-
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2
2
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