Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Inhibitors

EC Number Inhibitors Comment 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 Comment 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] Comment Organism
1.8.1.4 49342
-
 x * 49342, electrospray mass spectrometry Mycolicibacterium smegmatis

Organism

EC Number Organism UniProt Comment Textmining
1.8.1.4 Mycolicibacterium smegmatis
-
-
-
1.8.1.4 Pisum sativum
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.1.4
-
 Mycolicibacterium smegmatis

Reaction

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.8.1.4 2.43
-
-
 Mycolicibacterium smegmatis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.1.4 1,4-benzoquinone + NADH
-
 Mycolicibacterium smegmatis 1,4-benzoquinol + NAD+
-
 ?
1.8.1.4 dihydrolipoamide + NAD+
-
 Mycolicibacterium smegmatis lipoamide + NADH
-
 ?
1.8.1.4 dihydrolipoamide + NAD+
-
 Pisum sativum lipoamide + NADH
-
 ?
1.8.1.4 dihydrolipoate + NAD+
-
 Mycolicibacterium smegmatis lipoate + NADH + H+
-
 r
1.8.1.4 lipoate + NADH + H+
-
 Mycolicibacterium smegmatis dihydrolipoate + NAD+
-
 r
1.8.1.4 naphthoquinone + NADH
-
 Mycolicibacterium smegmatis 1,4-naphthoquinol + NAD+
-
 ?

Subunits

EC Number Subunits Comment Organism
1.8.1.4 ?
-
 Pisum sativum
1.8.1.4 ? x * 49342, electrospray mass spectrometry Mycolicibacterium smegmatis
1.8.1.4 More
-
 Pisum sativum
1.8.1.4 More the enzyme oligomerizes to a high-molecular weight species, above 300000 Da, under nondenaturing conditions Mycolicibacterium smegmatis

Cofactor

EC Number Cofactor Comment Organism Structure
1.8.1.4 NAD+
-
 Pisum sativum
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 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