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Literature summary for 1.8.1.4 extracted from

  • Neuburger, M.; Polidori, A.M.; Pietre, E.; Faure, M.; Jourdain, A.; Bourguignon, J.; Pucci, B.; Douce, R.
    Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system (2000), Eur. J. Biochem., 267, 2882-2889.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.027
-
lipoyl H-protein
-
Pisum sativum
0.5
-
(R,S)-lipoamide
-
Pisum sativum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pisum sativum the physiological substrates are the dihydrolipoyl domain of the E2 component, dihydrolipoyl acyltransferase, of the 2-oxoacid dehydrogenase multienzyme complexs or the dihydrolipoyl H-protein of the mitochobdrial glycine decarboxylase ?
-
?

Organism

Organism UniProt Comment Textmining
Pisum sativum
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
Pisum sativum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R,S)-lipoamide + NADH + H+
-
Pisum sativum dihydrolipoamide + NAD+
-
r
dihydrolipoamide + NAD+
-
Pisum sativum lipoamide + NADH
-
?
lipoyl H-protein + NADH + H+
-
Pisum sativum dihydrolipoyl H-protein + NAD+
-
r
additional information EC 1.8.1.4 is the E3-protein component of the mitochondrial 2-oxoacid dehydrogenase multienzyme complexes and the L-protein component of the glycine decarboxylase system Pisum sativum ?
-
?
additional information the physiological substrates are the dihydrolipoyl domain of the E2 component, dihydrolipoyl acyltransferase, of the 2-oxoacid dehydrogenase multienzyme complexs or the dihydrolipoyl H-protein of the mitochobdrial glycine decarboxylase Pisum sativum ?
-
?

Subunits

Subunits Comment Organism
More EC 1.8.1.4 is the E3-protein component of the mitochondrial 2-oxoacid dehydrogenase multienzyme complexes and the L-protein component of the glycine decarboxylase system Pisum sativum

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
additional information turnover numbers for small polypeptides derived from proteolytic treatment of the H-protein Pisum sativum
190
-
(R,S)-lipoamide
-
Pisum sativum
345
-
lipoyl H-protein
-
Pisum sativum

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Pisum sativum