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Literature summary for 1.4.3.20 extracted from

  • Sehanobish, E.; Chacon-Verdu, M.D.; Sanchez-Amat, A.; Davidson, V.L.
    Roles of active site residues in LodA, a cysteine tryptophylquinone dependent epsilon-lysine oxidase (2015), Arch. Biochem. Biophys., 579, 26-32 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.4.3.20

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta cells Marinomonas mediterranea

Protein Variants

Protein Variants Comment Organism
C448A the mutation causes large increases in the Km values for L-lysine Marinomonas mediterranea
C448D the mutation causes large increases in the Km values for L-lysine Marinomonas mediterranea
K530A the variant exhibits diminished levels of cysteine tryptophylquinone but significantly increased kcat value. The mutation causes large increases in the Km values for L-lysine Marinomonas mediterranea
K530R the variant exhibits diminished levels of cysteine tryptophylquinone but significantly increased kcat value. The mutation causes large increases in the Km values for L-lysine Marinomonas mediterranea
Y211A the variant the highest level of cysteine tryptophylquinone but exhibits no activity Marinomonas mediterranea
Y211E the variant the highest level of cysteine tryptophylquinone but exhibits no activity Marinomonas mediterranea
Y211F the mutant has reduced levels of cysteine tryptophylquinone but near normal levels of kcat. The mutation causes large increases in the Km values for L-lysine Marinomonas mediterranea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0039
-
 L-lysine wild type enzyme, at pH 7.5 and 25°C Marinomonas mediterranea
0.048
-
 L-lysine mutant enzyme C448A, at pH 7.5 and 25°C Marinomonas mediterranea
0.052
-
 L-lysine mutant enzyme K530A, at pH 7.5 and 25°C Marinomonas mediterranea
0.113
-
 L-lysine mutant enzyme K530R, at pH 7.5 and 25°C Marinomonas mediterranea
0.129
-
 L-lysine mutant enzyme Y211F, at pH 7.5 and 25°C Marinomonas mediterranea
0.142
-
 L-lysine mutant enzyme C448D, at pH 7.5 and 25°C Marinomonas mediterranea
0.199
-
 O2 wild type enzyme, at pH 7.5 and 25°C Marinomonas mediterranea
0.386
-
 O2 mutant enzyme C448D, at pH 7.5 and 25°C Marinomonas mediterranea
0.522
-
 O2 mutant enzyme Y211F, at pH 7.5 and 25°C Marinomonas mediterranea
0.543
-
 O2 mutant enzyme C448A, at pH 7.5 and 25°C Marinomonas mediterranea
0.706
-
 O2 mutant enzyme K530R, at pH 7.5 and 25°C Marinomonas mediterranea
1.043
-
 O2 mutant enzyme K530A, at pH 7.5 and 25°C Marinomonas mediterranea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine + O2 + H2O Marinomonas mediterranea
-
 (S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
 ?
L-lysine + O2 + H2O Marinomonas mediterranea NBRC 103028
-
 (S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
 ?

Organism

Organism UniProt Comment Textmining
Marinomonas mediterranea F2JXJ3
-
-
Marinomonas mediterranea NBRC 103028 F2JXJ3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine + O2 + H2O
-
 Marinomonas mediterranea (S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
 ?
L-lysine + O2 + H2O
-
 Marinomonas mediterranea NBRC 103028 (S)-2-amino-6-oxohexanoate + H2O2 + NH3
-
 ?

Synonyms

Synonyms Comment Organism
epsilon-lysine oxidase
-
 Marinomonas mediterranea
LodA
-
 Marinomonas mediterranea
marinocine
-
 Marinomonas mediterranea

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.19
-
 L-lysine mutant enzyme Y211F, at pH 7.5 and 25°C Marinomonas mediterranea
0.29
-
 L-lysine mutant enzyme C448D, at pH 7.5 and 25°C Marinomonas mediterranea
0.34
-
 L-lysine wild type enzyme, at pH 7.5 and 25°C Marinomonas mediterranea
0.39
-
 L-lysine mutant enzyme C448A, at pH 7.5 and 25°C Marinomonas mediterranea
0.68
-
 L-lysine mutant enzyme K530R, at pH 7.5 and 25°C Marinomonas mediterranea
1.2
-
 L-lysine mutant enzyme K530A, at pH 7.5 and 25°C Marinomonas mediterranea

Cofactor

Cofactor Comment Organism Structure
cysteine tryptophylquinone dependent on Marinomonas mediterranea