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show all sequences of 1.1.99.6

The Archaeoglobus fulgidus D-lactate dehydrogenase is a Zn2+ flavoprotein

Reed, D.W.; Hartzell, P.L.; J. Bacteriol. 181, 7580-7587 (1999)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate
stimulates
Archaeoglobus fulgidus
n-dodecyl beta-D-maltoside
stimulates
Archaeoglobus fulgidus
phenazine methosulfate
stimulates
Archaeoglobus fulgidus
Triton X-100
stimulates
Archaeoglobus fulgidus
Cloned(Commentary)
Commentary
Organism
expression as part of a fusion protein with maltose-binding protein in Escherichia coli
Archaeoglobus fulgidus
Inhibitors
Inhibitors
Commentary
Organism
Structure
oxalate
1 mM, addition of Tris buffered oxalate to a reaction mixture inhibits activity
Archaeoglobus fulgidus
Tris
slight inhibition above 30 mM
Archaeoglobus fulgidus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.15
-
(R)-lactate
pH 8.5, 60°C
Archaeoglobus fulgidus
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
the enzyme contains 1 mol of Zn2+ per mol of protein
Archaeoglobus fulgidus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Archaeoglobus fulgidus
O29853
-
-
Purification (Commentary)
Commentary
Organism
-
Archaeoglobus fulgidus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
no activity with L-lactate
722504
Archaeoglobus fulgidus
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
(R)-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
-
722504
Archaeoglobus fulgidus
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
-
-
-
?
additional information
methylene blue, dimethylnaphthoquinone, NAD+, and horse heart cytochrome c do not serve as electron acceptors for the purified enzyme
722504
Archaeoglobus fulgidus
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
assay at
Archaeoglobus fulgidus
90
-
-
Archaeoglobus fulgidus
Temperature Range [°C]
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
95
25°C: 8% of maximal activity, 95°C: about 75% of maximal activity
Archaeoglobus fulgidus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
83
-
half-life: 105 min
Archaeoglobus fulgidus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
in a 25 mM Tris buffer at 60°C
Archaeoglobus fulgidus
pH Range
pH Minimum
pH Maximum
Commentary
Organism
7
9.5
pH 7.0: about 30% of maximal activit, pH 9.5: about 55% of maximal activity
Archaeoglobus fulgidus
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
flavoprotein. FAD binds to apoprotein with a 1:1 stoichiometry and is essential for activity. Although the cofactor is tightly associated with the enzyme, it is not covalently attached
Archaeoglobus fulgidus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate
stimulates
Archaeoglobus fulgidus
n-dodecyl beta-D-maltoside
stimulates
Archaeoglobus fulgidus
phenazine methosulfate
stimulates
Archaeoglobus fulgidus
Triton X-100
stimulates
Archaeoglobus fulgidus
Cloned(Commentary) (protein specific)
Commentary
Organism
expression as part of a fusion protein with maltose-binding protein in Escherichia coli
Archaeoglobus fulgidus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
flavoprotein. FAD binds to apoprotein with a 1:1 stoichiometry and is essential for activity. Although the cofactor is tightly associated with the enzyme, it is not covalently attached
Archaeoglobus fulgidus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
oxalate
1 mM, addition of Tris buffered oxalate to a reaction mixture inhibits activity
Archaeoglobus fulgidus
Tris
slight inhibition above 30 mM
Archaeoglobus fulgidus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.15
-
(R)-lactate
pH 8.5, 60°C
Archaeoglobus fulgidus
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
the enzyme contains 1 mol of Zn2+ per mol of protein
Archaeoglobus fulgidus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Archaeoglobus fulgidus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + oxidized 2,6-dichlorophenolindophenol
no activity with L-lactate
722504
Archaeoglobus fulgidus
pyruvate + reduced 2,6-dichlorophenolindophenol
-
-
-
?
(R)-lactate + oxidized 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
-
722504
Archaeoglobus fulgidus
pyruvate + reduced 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyl tetrazolium
-
-
-
?
additional information
methylene blue, dimethylnaphthoquinone, NAD+, and horse heart cytochrome c do not serve as electron acceptors for the purified enzyme
722504
Archaeoglobus fulgidus
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
60
-
assay at
Archaeoglobus fulgidus
90
-
-
Archaeoglobus fulgidus
Temperature Range [°C] (protein specific)
Temperature Minimum [°C]
Temperature Maximum [°C]
Commentary
Organism
25
95
25°C: 8% of maximal activity, 95°C: about 75% of maximal activity
Archaeoglobus fulgidus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
83
-
half-life: 105 min
Archaeoglobus fulgidus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8
-
in a 25 mM Tris buffer at 60°C
Archaeoglobus fulgidus
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
7
9.5
pH 7.0: about 30% of maximal activit, pH 9.5: about 55% of maximal activity
Archaeoglobus fulgidus
Other publictions for EC 1.1.99.6
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)
721200
Shibahara
Crystallization and preliminar ...
Aeropyrum pernix, Aeropyrum pernix DSM 11879
Acta Crystallogr. Sect. F
67
1425-1427
2011
-
-
1
1
-
-
-
-
-
-
-
-
-
4
-
-
1
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-
-
-
-
-
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-
-
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1
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1
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1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
693285
Satomura
A novel flavin adenine dinucle ...
Sulfurisphaera tokodaii, Sulfurisphaera tokodaii 7
J. Biosci. Bioeng.
106
16-21
2008
-
-
1
-
-
-
5
3
-
-
3
-
-
8
-
-
1
-
-
-
-
-
10
1
2
-
2
-
1
1
1
1
-
-
-
-
-
1
1
-
-
-
-
5
-
3
-
-
3
-
-
-
-
1
-
-
-
-
10
1
2
-
2
-
1
1
1
-
-
-
-
-
-
-
721463
Pagala
Cellular localization of D-lac ...
Archaeoglobus fulgidus
Archaea
1
95-104
2002
-
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287843
Huang
Cloning and characterization o ...
Homo sapiens
Biochem. Biophys. Res. Commun.
268
298-301
2000
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287842
Hekmat
-
Production of pyruvate from (R ...
Proteus vulgaris
Enzyme Microb. Technol.
24
471-479
1999
-
1
-
-
-
-
-
-
-
-
-
-
-
1
-
-
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-
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1
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1
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-
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-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
722504
Reed
The Archaeoglobus fulgidus D-l ...
Archaeoglobus fulgidus
J. Bacteriol.
181
7580-7587
1999
4
-
1
-
-
-
2
1
-
1
-
-
-
3
-
-
1
-
-
-
-
-
3
-
2
1
1
-
1
1
-
1
-
-
-
4
-
1
1
-
-
-
-
2
-
1
-
1
-
-
-
-
-
1
-
-
-
-
3
-
2
1
1
-
1
1
-
-
-
-
-
-
-
-
287841
Trautwein
The (2R)-hydroxycarboxylate-vi ...
Proteus vulgaris
Eur. J. Biochem.
222
1025-1032
1994
-
-
-
-
-
-
1
-
-
1
2
-
-
1
1
-
1
-
-
-
2
-
5
1
-
-
-
-
-
-
-
3
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
1
2
-
-
1
-
1
-
-
2
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287840
Cammack
D-2-hydroxy acid dehydrogenase ...
Oryctolagus cuniculus
Methods Enzymol.
41
323-329
1975
4
-
-
-
-
1
7
2
1
-
1
2
-
2
-
-
1
-
-
1
1
2
14
-
1
-
-
-
2
-
1
5
-
-
-
4
-
-
5
-
-
1
-
7
-
2
1
-
1
2
-
-
-
1
-
1
1
2
14
-
1
-
-
-
2
-
1
-
-
-
-
-
-
-
287839
Tubbs
Dehydrogenation of D-lactate b ...
Oryctolagus cuniculus
Biochim. Biophys. Acta
34
290-291
1959
4
-
-
-
-
-
6
1
1
1
-
1
-
1
-
-
1
-
-
2
-
-
2
-
2
-
-
-
1
-
-
3
-
-
-
4
-
-
3
-
-
-
-
6
-
1
1
1
-
1
-
-
-
1
-
2
-
-
2
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-