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Literature summary extracted from

  • Saiki, T.; Shinshi, H.; Arima, K.
    Studies on homoserine dehydrogenase from an extreme thermophile, Thermus flavus AT-62. Partial purification and properties (1973), J. Biochem., 74, 1239-1248.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.3 L-threonine not inhibitory Thermus thermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.3 0.17 0.18 NADP+
-
 Thermus thermophilus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.3 K+ activation Thermus thermophilus
1.1.1.3 Na+ activation Thermus thermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.3 Thermus thermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.1.3 partial Thermus thermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.3 L-aspartate 4-semialdehyde + NAD(P)H
-
 Thermus thermophilus L-homoserine + NAD(P)+
-
 r
1.1.1.3 L-homoserine + NAD(P)+
-
 Thermus thermophilus L-aspartate 4-semialdehyde + NAD(P)H
-
 r

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.3 additional information
-
 above 50°C temperature dependent conformational change Thermus thermophilus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.1.3 70
-
 up to Thermus thermophilus
1.1.1.3 80
-
 slow inactivation, protection by K+, Na+ Thermus thermophilus
1.1.1.3 90
-
 rapid inactivation Thermus thermophilus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.3 9
-
-
 Thermus thermophilus