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Literature summary for 1.8.1.4 extracted from

  • Marcinkeviciene, J.; Blanchard, J.S.
    Catalytic properties of lipoamide dehydrogenase from Mycobacterium smegmatis (1997), Arch. Biochem. Biophys., 340, 168-176.
    View publication on PubMed
Search for more literature for 1.8.1.4

Inhibitors

Inhibitors Comment Organism Structure
arsenite reversible inactivation of lipoamide-reducing reaction, no decrease in diaphorase activity Mycolicibacterium smegmatis
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
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]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 1,4-benzoquinone
-
 Mycolicibacterium smegmatis
0.05
-
 1,4-Naphthoquinone
-
 Mycolicibacterium smegmatis
1.3
-
 Lipoamide
-
 Mycolicibacterium smegmatis
2.9
-
 lipoate
-
 Mycolicibacterium smegmatis
4.7
-
 dihydrolipoate
-
 Mycolicibacterium smegmatis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49342
-
 x * 49342, electrospray mass spectrometry Mycolicibacterium smegmatis

Organism

Organism UniProt Comment Textmining
Mycolicibacterium smegmatis
-
-
-
Pisum sativum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycolicibacterium smegmatis

Reaction

Reaction Comment Organism Reaction ID
protein N6-(dihydrolipoyl)lysine + NAD+ = protein N6-(lipoyl)lysine + NADH + H+ ping-pong mechanism Mycolicibacterium smegmatis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.43
-
-
 Mycolicibacterium smegmatis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,4-benzoquinone + NADH
-
 Mycolicibacterium smegmatis 1,4-benzoquinol + NAD+
-
 ?
dihydrolipoamide + NAD+
-
 Mycolicibacterium smegmatis lipoamide + NADH
-
 ?
dihydrolipoamide + NAD+
-
 Pisum sativum lipoamide + NADH
-
 ?
dihydrolipoate + NAD+
-
 Mycolicibacterium smegmatis lipoate + NADH + H+
-
 r
lipoate + NADH + H+
-
 Mycolicibacterium smegmatis dihydrolipoate + NAD+
-
 r
naphthoquinone + NADH
-
 Mycolicibacterium smegmatis 1,4-naphthoquinol + NAD+
-
 ?

Subunits

Subunits Comment Organism
?
-
 Pisum sativum
? x * 49342, electrospray mass spectrometry Mycolicibacterium smegmatis
More
-
 Pisum sativum
More the enzyme oligomerizes to a high-molecular weight species, above 300000 Da, under nondenaturing conditions Mycolicibacterium smegmatis

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Pisum sativum
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
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