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Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis

Marcinkeviciene, J.; Blanchard, J.S.; Arch. Biochem. Biophys. 340, 168-176 (1997)

Data extracted from this reference:

Inhibitors
EC Number
Inhibitors
Commentary
Organism
Structure
1.8.1.4
arsenite
reversible inactivation of lipoamide-reducing reaction, no decrease in diaphorase activity
Mycolicibacterium smegmatis
1.8.1.4
NAD+
substrate inhibition. The rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
Mycolicibacterium smegmatis
1.8.1.4
NADH
substrate inhibition. The rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
Mycolicibacterium smegmatis
KM Value [mM]
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.8.1.4
0.01
-
1,4-benzoquinone
-
Mycolicibacterium smegmatis
1.8.1.4
0.05
-
1,4-Naphthoquinone
-
Mycolicibacterium smegmatis
1.8.1.4
1.3
-
Lipoamide
-
Mycolicibacterium smegmatis
1.8.1.4
2.9
-
lipoate
-
Mycolicibacterium smegmatis
1.8.1.4
4.7
-
dihydrolipoate
-
Mycolicibacterium smegmatis
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.8.1.4
49342
-
x * 49342, electrospray mass spectrometry
Mycolicibacterium smegmatis
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
1.8.1.4
Mycolicibacterium smegmatis
-
-
-
1.8.1.4
Pisum sativum
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
1.8.1.4
-
Mycolicibacterium smegmatis
Reaction
EC Number
Reaction
Commentary
Organism
1.8.1.4
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+
ping-pong mechanism
Mycolicibacterium smegmatis
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
1.8.1.4
2.43
-
-
Mycolicibacterium smegmatis
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.1.4
1,4-benzoquinone + NADH
-
394007
Mycolicibacterium smegmatis
1,4-benzoquinol + NAD+
-
-
-
?
1.8.1.4
dihydrolipoamide + NAD+
-
394007
Mycolicibacterium smegmatis
lipoamide + NADH
-
-
-
?
1.8.1.4
dihydrolipoamide + NAD+
-
394007
Pisum sativum
lipoamide + NADH
-
-
-
?
1.8.1.4
naphthoquinone + NADH
-
394007
Mycolicibacterium smegmatis
1,4-naphthoquinol + NAD+
-
-
-
?
Subunits
EC Number
Subunits
Commentary
Organism
1.8.1.4
?
x * 49342, electrospray mass spectrometry
Mycolicibacterium smegmatis
1.8.1.4
?
-
Pisum sativum
1.8.1.4
More
the enzyme oligomerizes to a high-molecular weight species, above 300000 Da, under nondenaturing conditions
Mycolicibacterium smegmatis
1.8.1.4
More
-
Pisum sativum
Cofactor
EC Number
Cofactor
Commentary
Organism
Structure
1.8.1.4
NAD+
the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
Mycolicibacterium smegmatis
1.8.1.4
NAD+
-
Pisum sativum
1.8.1.4
NADH
the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
Mycolicibacterium smegmatis
Cofactor (protein specific)
EC Number
Cofactor
Commentary
Organism
Structure
1.8.1.4
NAD+
the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
Mycolicibacterium smegmatis
1.8.1.4
NAD+
-
Pisum sativum
1.8.1.4
NADH
the rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
Mycolicibacterium smegmatis
Inhibitors (protein specific)
EC Number
Inhibitors
Commentary
Organism
Structure
1.8.1.4
arsenite
reversible inactivation of lipoamide-reducing reaction, no decrease in diaphorase activity
Mycolicibacterium smegmatis
1.8.1.4
NAD+
substrate inhibition. The rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
Mycolicibacterium smegmatis
1.8.1.4
NADH
substrate inhibition. The rate of lipoamide reduction is dependent upon the NAD+/NADH ratio, the reaction is activated at low ratios and inhibited at high ratios
Mycolicibacterium smegmatis
KM Value [mM] (protein specific)
EC Number
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
1.8.1.4
0.01
-
1,4-benzoquinone
-
Mycolicibacterium smegmatis
1.8.1.4
0.05
-
1,4-Naphthoquinone
-
Mycolicibacterium smegmatis
1.8.1.4
1.3
-
Lipoamide
-
Mycolicibacterium smegmatis
1.8.1.4
2.9
-
lipoate
-
Mycolicibacterium smegmatis
1.8.1.4
4.7
-
dihydrolipoate
-
Mycolicibacterium smegmatis
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
1.8.1.4
49342
-
x * 49342, electrospray mass spectrometry
Mycolicibacterium smegmatis
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
1.8.1.4
-
Mycolicibacterium smegmatis
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [Ámol/min/mg]
Specific Activity Maximum [Ámol/min/mg]
Commentary
Organism
1.8.1.4
2.43
-
-
Mycolicibacterium smegmatis
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1.8.1.4
1,4-benzoquinone + NADH
-
394007
Mycolicibacterium smegmatis
1,4-benzoquinol + NAD+
-
-
-
?
1.8.1.4
dihydrolipoamide + NAD+
-
394007
Mycolicibacterium smegmatis
lipoamide + NADH
-
-
-
?
1.8.1.4
dihydrolipoamide + NAD+
-
394007
Pisum sativum
lipoamide + NADH
-
-
-
?
1.8.1.4
naphthoquinone + NADH
-
394007
Mycolicibacterium smegmatis
1,4-naphthoquinol + NAD+
-
-
-
?
Subunits (protein specific)
EC Number
Subunits
Commentary
Organism
1.8.1.4
?
x * 49342, electrospray mass spectrometry
Mycolicibacterium smegmatis
1.8.1.4
?
-
Pisum sativum
1.8.1.4
More
the enzyme oligomerizes to a high-molecular weight species, above 300000 Da, under nondenaturing conditions
Mycolicibacterium smegmatis
1.8.1.4
More
-
Pisum sativum