BRENDA - Enzyme Database show
show all sequences of 1.1.99.6

Dehydrogenation of D-lactate by a soluble enzyme from kidney mitochondria

Tubbs, P.K.; Greville, G.D.; Biochim. Biophys. Acta 34, 290-291 (1959)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ferricyanide
-
Oryctolagus cuniculus
methylene blue
-
Oryctolagus cuniculus
additional information
ageing of extracts increases dehydrogenase activity
Oryctolagus cuniculus
O2
no appreciable O2 uptake in absence of electron carrier
Oryctolagus cuniculus
Inhibitors
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
inhibition potentiated by KCN
Oryctolagus cuniculus
Cu2+
strong
Oryctolagus cuniculus
EDTA
-
Oryctolagus cuniculus
Hg2+
strong
Oryctolagus cuniculus
KCN
potentiates inhibition of 1,10-phenanthroline
Oryctolagus cuniculus
p-chloromercuribenzoate
strong
Oryctolagus cuniculus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.4
-
D-lactate
-
Oryctolagus cuniculus
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Oryctolagus cuniculus
5739
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
KCN
raises dehydrogenase activity of freshly prepared kidney extracts
Oryctolagus cuniculus
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-lactate + acceptor
Oryctolagus cuniculus
enzyme acts on a variety of (R)-2-hydroxy acids
pyruvate + reduced acceptor
-
Oryctolagus cuniculus
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Oryctolagus cuniculus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Oryctolagus cuniculus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
kidney
-
Oryctolagus cuniculus
-
liver
-
Oryctolagus cuniculus
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + acceptor
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide
287839
Oryctolagus cuniculus
pyruvate + reduced acceptor
-
287839
Oryctolagus cuniculus
?
(R)-lactate + acceptor
enzyme acts on a variety of (R)-2-hydroxy acids
287839
Oryctolagus cuniculus
pyruvate + reduced acceptor
-
287839
Oryctolagus cuniculus
?
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Oryctolagus cuniculus
30
-
assay at
Oryctolagus cuniculus
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
-
Oryctolagus cuniculus
Cofactor
Cofactor
Commentary
Organism
Structure
2,6-dichlorophenolindophenol
-
Oryctolagus cuniculus
cytochrome c
possible physiological acceptor
Oryctolagus cuniculus
phenazine methosulfate
-
Oryctolagus cuniculus
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ferricyanide
-
Oryctolagus cuniculus
methylene blue
-
Oryctolagus cuniculus
additional information
ageing of extracts increases dehydrogenase activity
Oryctolagus cuniculus
O2
no appreciable O2 uptake in absence of electron carrier
Oryctolagus cuniculus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
2,6-dichlorophenolindophenol
-
Oryctolagus cuniculus
cytochrome c
possible physiological acceptor
Oryctolagus cuniculus
phenazine methosulfate
-
Oryctolagus cuniculus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
1,10-phenanthroline
inhibition potentiated by KCN
Oryctolagus cuniculus
Cu2+
strong
Oryctolagus cuniculus
EDTA
-
Oryctolagus cuniculus
Hg2+
strong
Oryctolagus cuniculus
KCN
potentiates inhibition of 1,10-phenanthroline
Oryctolagus cuniculus
p-chloromercuribenzoate
strong
Oryctolagus cuniculus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
3.4
-
D-lactate
-
Oryctolagus cuniculus
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Oryctolagus cuniculus
5739
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
KCN
raises dehydrogenase activity of freshly prepared kidney extracts
Oryctolagus cuniculus
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
(R)-lactate + acceptor
Oryctolagus cuniculus
enzyme acts on a variety of (R)-2-hydroxy acids
pyruvate + reduced acceptor
-
Oryctolagus cuniculus
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Oryctolagus cuniculus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
kidney
-
Oryctolagus cuniculus
-
liver
-
Oryctolagus cuniculus
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(R)-lactate + acceptor
acceptors: 2,6-dichlorophenolindophenol, phenazine methosulfate, ferricyanide
287839
Oryctolagus cuniculus
pyruvate + reduced acceptor
-
287839
Oryctolagus cuniculus
?
(R)-lactate + acceptor
enzyme acts on a variety of (R)-2-hydroxy acids
287839
Oryctolagus cuniculus
pyruvate + reduced acceptor
-
287839
Oryctolagus cuniculus
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
20
-
assay at
Oryctolagus cuniculus
30
-
assay at
Oryctolagus cuniculus
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.1
-
-
Oryctolagus cuniculus
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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-
-
-
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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
-
-
-
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-
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-
-
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-
1
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
287842
Hekmat
-
Production of pyruvate from (R ...
Proteus vulgaris
Enzyme Microb. Technol.
24
471-479
1999
-
1
-
-
-
-
-
-
-
-
-
-
-
1
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-
1
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1
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1
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-
-
-
-
-
-
-
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
-
-
-
-
-
-
-
-
-