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Literature summary for 1.2.1.12 extracted from

  • Crabb, J.W.; Murdock, A.L.; Amelunxen, R.E.
    Purification and characterization of thermolabile glyceraldehyde-3-phosphate dehydrogenase from the facultative thermophile Bacillus coagulans KU (1977), Biochemistry, 16, 4840-4847.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
-
Weizmannia coagulans

General Stability

General Stability Organism
8 M urea, 30°C, 0.05 M phosphate buffer, 50% loss of activity after 1 min Weizmannia coagulans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
36000
-
4 * 36000, SDS-PAGE Weizmannia coagulans
146800
-
equilibrium sedimentation Weizmannia coagulans

Organism

Organism UniProt Comment Textmining
Weizmannia coagulans
-
KU
-
Weizmannia coagulans KU
-
KU
-

Purification (Commentary)

Purification (Comment) Organism
-
Weizmannia coagulans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
109
-
-
Weizmannia coagulans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Weizmannia coagulans 3-phospho-D-glyceroyl phosphate + NADH
-
?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
Weizmannia coagulans KU 3-phospho-D-glyceroyl phosphate + NADH
-
?

Subunits

Subunits Comment Organism
tetramer 4 * 36000, SDS-PAGE Weizmannia coagulans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
55
-
5 min, 96-98% loss of activity. No inactivation if the ionic strength is increased to 1.8 by addition of NaCl or (NH4)2SO4 Weizmannia coagulans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.6
-
-
Weizmannia coagulans

Cofactor

Cofactor Comment Organism Structure
NAD+ enzyme contains 4 equivalents of firmly bound NAD+ Weizmannia coagulans