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Literature summary for 4.1.1.18 extracted from

  • Kloss, R.; Limberg, M.H.; Mackfeld, U.; Hahn, D.; Gruenberger, A.; Jaeger, V.D.; Krauss, U.; Oldiges, M.; Pohl, M.
    Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production (2018), Sci. Rep., 8, 5856 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene ldcC, recombinant overexpression in Escherichia coli strain BL21(DE3) in inclusion bodies with 3-10 mg/ml protein in batch cultivation. The aggregated enzyme EcLDCc-CatIBs is catalytically active Escherichia coli

Protein Variants

Protein Variants Comment Organism
additional information development of an innovative immobilisation approach using catalytically active recombinant constitutive L-lysine decarboxylase (EcLDCc) in inclusion bodies, CatIBs, overview. EcLDCc-CatIBs can compete with the whole cell biocatalyst in production of cadaverine Escherichia coli

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Escherichia coli
-
cadaverine + CO2
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli P52095
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine
-
Escherichia coli cadaverine + CO2
-
?

Subunits

Subunits Comment Organism
homodecamer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
constitutive LDCc
-
Escherichia coli
EcLDCc
-
Escherichia coli
L-lysine decarboxylase
-
Escherichia coli
LDC
-
Escherichia coli
ldcC
-
Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2 8 broad optimum, soluble wild-type enzyme Escherichia coli
8 8.5 recombinant enzyme inclusion bodies, EcLDCc-CatIBs, the activity is dependent on the medium Escherichia coli

pH Range

pH Minimum pH Maximum Comment Organism
6.2 8.8 soluble wild-type enzyme, maximal activity at pH 6.2-8.0, 30% of maximal activity at pH 8.8 Escherichia coli
7.5 9 recombinant enzyme inclusion bodies, EcLDCc-CatIBs, range of higher activity Escherichia coli

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate dependent on Escherichia coli

General Information

General Information Comment Organism
evolution the L-lysine decarboxylase (LDC) genes from Escherichia coli include genes cadA and ldcC encoding the acid-inducible enzyme CadA and the constitutive LDCc, respectively Escherichia coli