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Literature summary for 1.5.1.11 extracted from

  • Zettlmeissl, G.; Teschner, W.; Rudolph, R.; Jaenicke, R.; Gδde, G.
    Isolation, physicochemical properties, and folding of octopine dehydrogenase from Pecten jacobeus (1984), Eur. J. Biochem., 143, 401-407.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
 NADH
-
 Pecten jacobaeus
0.21
-
 NAD+
-
 Pecten jacobaeus
1.05
-
 L-Arg
-
 Pecten jacobaeus
1.18
-
 pyruvate
-
 Pecten jacobaeus
2
-
 D-octopine
-
 Pecten jacobaeus

Organism

Organism UniProt Comment Textmining
Pecten jacobaeus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
2 isoenzymes: A and B Pecten jacobaeus

Renatured (Commentary)

Renatured (Comment) Organism
refolding kinetics. Upon reactivation after short denaturation of less than 8 s, about 25% of the activity is recovered in a fast initial phase of 20 s. The slow phase of reactivation, which predominates after long-term denaturation, is determined by a single-first-order reaction Pecten jacobaeus

Source Tissue

Source Tissue Comment Organism Textmining
adductor
-
 Pecten jacobaeus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Arg + pyruvate + NADH
-
 Pecten jacobaeus N2-(D-1-carboxyethyl)-L-Arg + NAD+ + H2O
-
 ?

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7
-
 octopine formation Pecten jacobaeus
9.5
-
 octopine oxidation Pecten jacobaeus

Cofactor

Cofactor Comment Organism Structure
NADH
-
 Pecten jacobaeus