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Literature summary for 4.3.1.25 extracted from

  • Abell, C.W.; Shen, R.S.
    Phenylalanine ammonia-lyase from the yeast Rhodotorula glutinis (1987), Methods Enzymol., 142, 242-249.
    View publication on PubMed

Application

Application Comment Organism
analysis rapid quantization of Phe and Tyr in plasma and serum from subjects with phenylketonuria Rhodotorula glutinis

Inhibitors

Inhibitors Comment Organism Structure
4-coumarate
-
Rhodotorula glutinis
Cinnamic acid trans-cinnamic acid Rhodotorula glutinis
D-Phe
-
Rhodotorula glutinis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
L-Tyr
-
Rhodotorula glutinis
0.25
-
L-Phe
-
Rhodotorula glutinis
4.2
-
trans-cinnamate
-
Rhodotorula glutinis
3170
-
NH3
-
Rhodotorula glutinis

Organism

Organism UniProt Comment Textmining
Rhodotorula glutinis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Rhodotorula glutinis

Reaction

Reaction Comment Organism Reaction ID
L-phenylalanine = trans-cinnamate + NH3 ordered uni-bi reaction sequence Rhodotorula glutinis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Rhodotorula glutinis

Storage Stability

Storage Stability Organism
-60°C, enzyme concentration 20-40 mg/ml, stable for 6 months Rhodotorula glutinis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Phe
-
Rhodotorula glutinis (E)-cinnamate + NH3
-
r
L-tyrosine L-Tyr Rhodotorula glutinis p-coumarate + NH3
-
?
trans-cinnamate + NH3
-
Rhodotorula glutinis L-Phe
-
r