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Literature summary for 4.1.99.2 extracted from

  • Mouratou, B.; Kasper, P.; Gehring, H.; Christen, P.
    Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature (1999), J. Biol. Chem., 274, 1320-1325.
    View publication on PubMed
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Protein Variants

Protein Variants Comment Organism
R100T/V283R increases the beta-elimination activity towards dicarboxylic amino acids, L-Asp, L-Glu and L-2-aminoadipate at least 10000-fold Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
 L-Tyr wild-type enzyme Escherichia coli
0.21
-
 L-Asp mutant enzyme R100T/V283R Escherichia coli
0.32
-
 L-Tyr mutant enzyme R100T/V283R Escherichia coli
1.7
-
 3-chloro-L-Ala wild-type enzyme Escherichia coli
5.3
-
 L-Glu mutant enzyme R100T/V283R Escherichia coli
46
-
 3-chloro-L-Ala mutant enzyme R100T/V283R Escherichia coli
54
-
 L-Asp mutant enzyme R100T/V283R Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 wild-type enzyme, mutant enzyme R100T, mutant enzyme R100T/V283R
-
Escherichia coli
-
 SV370
-
Escherichia coli SV370
-
 SV370
-

Purification (Commentary)

Purification (Comment) Organism
-
 Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-chloro-L-Ala + H2O
-
 Escherichia coli ?
-
 ?
3-chloro-L-Ala + H2O
-
 Escherichia coli SV370 ?
-
 ?
L-2-aminoadipate + H2O no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R Escherichia coli ?
-
 ?
L-2-aminoadipate + H2O no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R Escherichia coli SV370 ?
-
 ?
L-Asp + H2O no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R Escherichia coli formate + pyruvate + NH3
-
 ?
L-Asp + H2O no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R Escherichia coli SV370 formate + pyruvate + NH3
-
 ?
L-Glu + H2O no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R Escherichia coli ?
-
 ?
L-Glu + H2O no activity with wild-type enzyme, activity with mutant enzyme R100T/V283R Escherichia coli SV370 ?
-
 ?
Tyr + H2O
-
 Escherichia coli phenol + pyruvate + NH3
-
 ?
Tyr + H2O
-
 Escherichia coli SV370 phenol + pyruvate + NH3
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.11
-
 L-Tyr mutant enzyme R100T/V283R Escherichia coli
1.13
-
 3-chloro-L-Ala mutant enzyme R100T/V283R Escherichia coli
3
-
 3-chloro-L-Ala wild-type enzyme Escherichia coli
3.7
-
 L-Tyr
-
 Escherichia coli