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Literature summary for 1.5.1.6 extracted from

  • Reuland, S.N.; Vlasov, A.P.; Krupenko, S.A.
    Disruption of a calmodulin central helix-like region of 10-formyltetrahydrofolate dehydrogenase impairs its dehydrogenase activity by uncoupling the functional domains (2003), J. Biol. Chem., 278, 22894-22900.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D399A 90% of the dehydrogenase activity of the wild-type enzyme Rattus norvegicus
E398A 90% of the dehydrogenase activity of the wild-type enzyme Rattus norvegicus
F384_V405del no dehydrogenase activity Rattus norvegicus
G397A as active as wild-type enzyme Rattus norvegicus
K394A 75% of the dehydrogenase activity of the wild-type enzyme Rattus norvegicus
K394A/L395A/R396A/G397A/E398A/D399A no dehydrogenase activity Rattus norvegicus
K394_D399del no dehydrogenase activity Rattus norvegicus
L395A 80% of the dehydrogenase activity of the wild-type enzyme Rattus norvegicus
R396A as active as wild-type enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus P28037
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Purification (Commentary)

Purification (Comment) Organism
intermediate domain and its mutants Rattus norvegicus

Storage Stability

Storage Stability Organism
-20°C, stable for several months Rattus norvegicus
4°C, stable for 2 weeks Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
10-formyltetrahydrofolate + NADP+ + H2O the enzyme is composed of three domains and possesses three catalytic activities but has only two catalytic centers. The amino-terminal domain (residues 1-310) bears 10-formyltetrahydrofolate hydrolase activity, the carboxyl-terminal domain (residues 420-902) bears an aldehyde dehydrogenase activity, and the full-length FDH produces 10-formyltetrahydrofolate dehydrogenase activity Rattus norvegicus ?
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Synonyms

Synonyms Comment Organism
10-formyltetrahydrofolate dehydrogenase
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Rattus norvegicus
FDH
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Rattus norvegicus