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Literature summary for 4.4.1.14 extracted from

  • Khani-Oskouee, S.; Ramalingam, K.; Kalvin, D.; Woodard, R.W.
    Alternate substrates and inhibitors of 1-aminocyclopropane-1-carboxylic acid synthase (1987), Bioorg. Chem., 15, 92-99.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
S-adenosyl-L-methionine inactivation during catalytic action, (+) and (+/-) isomer Solanum lycopersicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
(-)-S-adenosyl-L-methionine
-
Solanum lycopersicum
0.04
-
S-adenosyl-L-methionine
-
Solanum lycopersicum

Organism

Organism UniProt Comment Textmining
Solanum lycopersicum
-
tomato
-

Purification (Commentary)

Purification (Comment) Organism
-
Solanum lycopersicum

Source Tissue

Source Tissue Comment Organism Textmining
pericarp
-
Solanum lycopersicum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information rigid specificity for (-)-S-adenosyl-L-methionine, only purine base adenosine and adenosine analogs in which N6 nitrogen is modified Solanum lycopersicum ?
-
?
S-adenosyl-L-methionine
-
Solanum lycopersicum 1-aminocyclopropane-1-carboxylate + methylthioadenosine
-
ir

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Solanum lycopersicum