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Literature summary for 1.2.1.13 extracted from

  • Biro, J.; Fabry, S.; Dietmaier, W.; Bogedain, C.; Hensel, R.
    Engineering thermostability in archaebacterial glyceraldehyde-3-phosphate dehydrogenase. Hints for the important role of interdomain contacts in stabilizing protein conformation (1990), FEBS Lett., 275, 130-134.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
additional information construction of hybrid enzymes between the glyceraldehyde-3-phosphate dehydrogenases from the mesophilic Methanobacterium bryantii and the thermophilic Methanothermus fervidus Methanobacterium bryantii
additional information construction of hybrid enzymes between the glyceraldehyde-3-phosphate dehydrogenases from the mesophilic Methanobacterium bryantii and the thermophilic Methanothermus fervidus Methanothermus fervidus
Y123W increase of temperature of irreversible inactivation by 1.3°C Methanothermus fervidus
Y323S decrease of temperature of irreversible inactivation by 4.5°C Methanothermus fervidus

Organism

Organism UniProt Comment Textmining
Methanobacterium bryantii
-
-
-
Methanothermus fervidus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Methanothermus fervidus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Methanothermus fervidus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NADP+
-
 Methanothermus fervidus 3-phospho-D-glyceroyl phosphate + NADPH
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADP+ cofactor Methanobacterium bryantii
NADP+ cofactor Methanothermus fervidus