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Literature summary for 4.4.1.14 extracted from

  • Huxtable, S.; Zhou, H.; Wong, S.; Li, N.
    Renaturation of 1-aminocyclopropane-1-carboxylate synthase expressed in Escherichia coli in the form of inclusion bodies into a dimeric and catalytically active enzyme (1998), Protein Expr. Purif., 12, 305-314.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Cucurbita pepo

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.023
-
S-adenosyl-L-methionine refolded enzyme Cucurbita pepo

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
100000
-
refolded enzyme, gel filtration Cucurbita pepo

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine Cucurbita pepo biosynthesis of ethylene: plant hormone 1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
?

Organism

Organism UniProt Comment Textmining
Cucurbita pepo P23279 zucchini
-

Purification (Commentary)

Purification (Comment) Organism
inclusion body purified Cucurbita pepo

Renatured (Commentary)

Renatured (Comment) Organism
refolding by a combination of dialysis and dilution in 100mM MOPS, pH 8, 30 mM Chaps and 5 mM GSH Cucurbita pepo

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.5
-
refolded enzyme Cucurbita pepo

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine biosynthesis of ethylene: plant hormone Cucurbita pepo 1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
?