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Literature summary for 2.2.1.2 extracted from

  • Levering, P.R.; Dijkhuizen, L.
    Transaldolase isoenzymes frm Arthrobacter P1 (1990), Methods Enzymol., 188, 405-411.
No PubMed abstract available
Search for more literature for 2.2.1.2

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 D-fructose 6-phosphate
-
 Arthrobacter sp.

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47500
-
 gel filtration, C1-inducible enzyme Arthrobacter sp.
50000
-
 1 * 50000, SDS-PAGE Arthrobacter sp.
52000
-
 gel filtration, constitutive enzyme Arthrobacter sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate Arthrobacter sp.
-
 D-erythrose 4-phosphate + D-fructose 6-phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Arthrobacter sp.
-
 P1, 2 isoenzymes: C1-inducible enzyme, C2-constitutive enzyme
-

Purification (Commentary)

Purification (Comment) Organism
-
 Arthrobacter sp.

Storage Stability

Storage Stability Organism
-20°C, stable for at least 2 months Arthrobacter sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate
-
 Arthrobacter sp. D-erythrose 4-phosphate + D-fructose 6-phosphate
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 50000, SDS-PAGE Arthrobacter sp.

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 2 min, C1-inducible enzyme loses 90% of activity, constitutive enzyme remains fully active Arthrobacter sp.