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Literature summary for 4.3.1.24 extracted from

  • Viergutz, S.; Retey, J.
    Kinetic analysis of the reactions catalyzed by histidine and phenylalanine ammonia lyases (2004), Chem. Biodivers., 1, 296-302.
    View publication on PubMed
Search for more literature for 4.3.1.24

Protein Variants

Protein Variants Comment Organism
L137H mutation almost doubles the kinetic D-isotope effect compared to wild-type enzyme Petroselinum crispum
L137H/Q487E mutation almost doubles the kinetic D-isotope effect compared to wild-type enzyme Petroselinum crispum
Q487A kinetic D isotope effect is of the same magnitude as wild-type enzyme Petroselinum crispum
Y350F kinetic D isotope effect is of the same magnitude as wild-type enzyme Petroselinum crispum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.022
-
 L-phenylalanine pH 8.8, 30°C, mutant enzyme Q487A Petroselinum crispum
0.027
-
 L-Phe pH 8.8, 30°C, mutant enzyme Q487A Petroselinum crispum
0.028
-
 L-phenylalanine pH 8.8, 30°C, mutant enzyme Y350F Petroselinum crispum
0.033
-
 L-Phe pH 8.8, 30°C, mutant enzyme Y350F Petroselinum crispum
9.8
-
 L-phenylalanine pH 8.8, 30°C, mutant enzyme L137H Petroselinum crispum
14.2
-
 L-Phe pH 8.8, 30°C, mutant enzyme L137H Petroselinum crispum
42.4
-
 L-phenylalanine pH 8.8, 30°C, mutant enzyme L137H/Q487E Petroselinum crispum
75.6
-
 L-Phe pH 8.8, 30°C, mutant enzyme L137H/Q487E Petroselinum crispum

Organism

Organism UniProt Comment Textmining
Petroselinum crispum
-
 recombinant wild-type enzyme and mutant enzymes Q487A, Y350F, and L137H
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-Phe
-
 Petroselinum crispum (E)-cinnamate + NH3
-
 ?
L-phenylalanine
-
 Petroselinum crispum trans-cinnamate + NH3
-
 ?