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Literature summary for 4.3.1.17 extracted from

  • Fujino, A.; Ose, T.; Yao, M.; Tokiwano, T.; Honma, M.; Watanabe, N.; Tanaka, I.
    Structural and enzymatic properties of 1-aminocyclopropane-1-carboxylate deaminase homologue from Pyrococcus horikoshii (2004), J. Mol. Biol., 341, 999-1013 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop vapor-diffusion method, crystal structures of the native and 1-aminocyclopropane-1-carboxylate-complexed enzyme. The crystals of native and Se-Met belong to the space group P3(2)21 with unit cell parameters of a=b= 122.3 A, c = 115.0 A, and gamma = 120°, and there are three molecules in an asymmetric unit. The crystals of the ACC complex belong to space group P1 with unit cell parameters of a = 105.8 A, b = 147.2 A, c = 149.0 A, a = 73.18, b = 90.18, and gamma = 68.48, and 24 molecules are included in an asymmetric cell Pyrococcus horikoshii

Organism

Organism UniProt Comment Textmining
Pyrococcus horikoshii O57809
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-serine
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Pyrococcus horikoshii pyruvate + NH3
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?
additional information the enzyme does not show 1-aminocyclopropane-1-carboxylate deaminase activity at high temperature as well as at room temperature though it has significant sequence similarity to 1-aminocyclopropane-1-carboxylate deaminase from the yeast Hansenula saturnus Pyrococcus horikoshii ?
-
?

Synonyms

Synonyms Comment Organism
PH0054
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Pyrococcus horikoshii

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Pyrococcus horikoshii