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Literature summary for 4.1.1.86 extracted from

  • Burrell, M.; Hanfrey, C.C.; Kinch, L.N.; Elliott, K.A.; Michael, A.J.
    Evolution of a novel lysine decarboxylase in siderophore biosynthesis (2012), Mol. Microbiol., 86, 485-499.
    View publication on PubMed
Search for more literature for 4.1.1.86

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.3
-
 L-lysine at pH 7.5 and 30°C Trichormus variabilis
0.54
-
 L-2,4-diaminobutanoate at pH 7.5 and 30°C Trichormus variabilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-2,4-diaminobutanoate Trichormus variabilis
-
 propane-1,3-diamine + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Trichormus variabilis Q3M985
-
-

Purification (Commentary)

Purification (Comment) Organism
HiTrap chelating column chromatography, and gel filtration Trichormus variabilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-2,4-diaminobutanoate
-
 Trichormus variabilis propane-1,3-diamine + CO2
-
 ?
L-lysine the catalytic efficiency of the enzyme is 24fold higher with L-2,4-diaminobutanoate than with L-lysine Trichormus variabilis 1,5-diaminopentane + CO2
-
 ?

Synonyms

Synonyms Comment Organism
DABA DC
-
 Trichormus variabilis
L-2,4-diaminobutyrate decarboxylase
-
 Trichormus variabilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.008
-
 L-lysine at pH 7.5 and 30°C Trichormus variabilis
0.34
-
 L-2,4-diaminobutanoate at pH 7.5 and 30°C Trichormus variabilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
26
-
 L-lysine at pH 7.5 and 30°C Trichormus variabilis
630
-
 L-2,4-diaminobutanoate at pH 7.5 and 30°C Trichormus variabilis