Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 4.3.1.25 extracted from

  • Parkhurst, J.R.; Hodgins, D.S.
    Yeast phenylalanine ammonia-lyase. Properties of the enzyme from Sporobolomyces pararoseus and its catalytic site (1972), Arch. Biochem. Biophys., 152, 597-605.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2-hydroxycinnamic acid
-
Sporidiobolus pararoseus
benzyl alcohol
-
Sporidiobolus pararoseus
Cinnamic acid
-
Sporidiobolus pararoseus
CN- the substrate analog DL-2-hydroxyphenylalanine or cinnamate protects Sporidiobolus pararoseus
Gly
-
Sporidiobolus pararoseus
L-beta-phenyllactic acid
-
Sporidiobolus pararoseus
trinitrobenzene sulfonic acid
-
Sporidiobolus pararoseus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.085
-
L-Tyr
-
Sporidiobolus pararoseus
0.3
-
L-Phe
-
Sporidiobolus pararoseus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
275000
-
sucrose density gradient centrifugation Sporidiobolus pararoseus
300000
-
gel filtration Sporidiobolus pararoseus

Organism

Organism UniProt Comment Textmining
Sporidiobolus pararoseus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Sporidiobolus pararoseus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Phe
-
Sporidiobolus pararoseus (E)-cinnamate + NH3
-
?
L-Tyr
-
Sporidiobolus pararoseus 4-coumarate + NH3
-
?