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Literature summary for 6.3.4.3 extracted from

  • Strong, W.; Joshi, G.; Lura, R.; Muthukumaraswamy, N.; Schirch, V.
    10-Formyltetrahydrofolate synthetase. Evidence for a conformational change in the enzyme upon binding of tetrahydropteroylpolyglutamates (1987), J. Biol. Chem., 262, 12519-12525.
    View publication on PubMed
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General Stability

General Stability Organism
the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ alters the susceptibility to digestion by chymotrypsin Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information effect of polyglutamate chain length of tetrahydropteroyl-(Glu)n on the Km values of formate and MgATP2- Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Oryctolagus cuniculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + formate + tetrahydrofolate
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 Oryctolagus cuniculus ADP + phosphate + 10-formyltetrahydrofolate
-
 ?
ATP + formate + tetrahydropteroyl-(Glu)n n: 1-5 Oryctolagus cuniculus ADP + phosphate + 10-formyltetrahydropteroyl-(Glu)n
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 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
-
 the binding of tetrahydropteroylpolyglutamate, MgATP2-, and NH4+ increases the denaturation temperature by 12°C and abolishes the cold lability of the enzyme Oryctolagus cuniculus