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Literature summary for 3.5.99.7 extracted from

  • Walsh, C.T.; Pascal, R.A.; Johnston, M.; Raines, R.; Dikshit, D.; Krantz, A.; Honma, M.
    Mechanistic studies on the pyridoxal phosphate enzyme 1-aminocyclopropane-1-carboxylate deaminase from Pseudomonas sp. (1981), Biochemistry, 20, 7509-7519.
    View publication on PubMed
Search for more literature for 3.5.99.7

Inhibitors

Inhibitors Comment Organism Structure
beta-chloro-Ala
-
 Pseudomonas sp.
beta-fluoro-D-Ala
-
 Pseudomonas sp.
O-acetyl-D-Ser
-
 Pseudomonas sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4
-
 2-vinyl-1-aminocyclopropane-1-carboxylate
-
 Pseudomonas sp.
9.2
-
 1-aminocyclopropane-1-carboxylate
-
 Pseudomonas sp.
97
-
 D-vinylglycine
-
 Pseudomonas sp.

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
1-aminocyclopropane-1-carboxylate + H2O = 2-oxobutanoate + NH3 mechanism Pseudomonas sp.
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-aminocyclopropane-1-carboxylate + H2O
-
 Pseudomonas sp. 2-oxobutanoate + NH3
-
 ?
2-vinyl-1-aminocyclopropane-1-carboxylate + H2O
-
 Pseudomonas sp. 2-keto-5-hexenoate + NH3
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.6
-
 D-vinylglycine 37°C, pH 8.5 Pseudomonas sp.
4.83
-
 1-aminocyclopropane-1-carboxylate 37°C, pH 8.5 Pseudomonas sp.
5.17
-
 2-vinyl-1-aminocyclopropane-1-carboxylate 37°C, pH 8.5 Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate pyridoxal 5'-phosphate dependent enzyme Pseudomonas sp.