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Literature summary extracted from

  • Wang, C.; Zhang, K.; Zhongjun, C.; Cai, H.; Honggui, W.; Ouyang, P.
    Directed evolution and mutagenesis of lysine decarboxylase from Hafnia alvei AS1.1009 to improve its activity toward efficient cadaverine production (2015), Biotechnol. Bioprocess Eng., 20, 439-446 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.18 gene ldc, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain JM109/pTrc99a-ldc2-41 Hafnia alvei

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.18 E583G site-directed mutagenesis, the mutant shows 1.32fold increased LDC activity and 1.48fold improved productivity of cadaverine compared to wild-type enzyme Hafnia alvei
4.1.1.18 additional information directed evolution of LDC and high-throughput mutant screening, mutant library construction using DNA shuffling or error-prone PCR (optimum concentrations of Mn2+ and Mg2+ are 5 and 0.2 mM, respectively). Three nucleotide mutations, A438G, G439T, and A1748G correspond to amino acid changes V147F and E583G Hafnia alvei
4.1.1.18 V147F site-directed mutagenesis, the mutant shows increased LDC activity Hafnia alvei
4.1.1.18 V147F/E583G site-directed mutagenesis, the mutant shows 1.62fold increased LDC activity compared to wild-type enzyme Hafnia alvei

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.18 additional information
-
 additional information kinetic analysis of wild-type and mutant enzymes, overview Hafnia alvei
4.1.1.18 3.23
-
 L-lysine pH 6.0, 37°C, recombinant mutant E583G Hafnia alvei
4.1.1.18 4.93
-
 L-lysine pH 6.0, 37°C, recombinant wild-type enzyme Hafnia alvei

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.18 L-lysine Hafnia alvei
-
 cadaverine + CO2
-
 ?
4.1.1.18 L-lysine Hafnia alvei AS1.1009
-
 cadaverine + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.18 Hafnia alvei
-
-
-
4.1.1.18 Hafnia alvei AS1.1009
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.18 recombinant wild-type and mutant enzymes from Escherichia coli strain JM109 by three steps of hydrophobic interaction chromatography on two different resins, and dialysis Hafnia alvei

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.18 L-lysine
-
 Hafnia alvei cadaverine + CO2
-
 ?
4.1.1.18 L-lysine
-
 Hafnia alvei AS1.1009 cadaverine + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.18 LDC
-
 Hafnia alvei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.18 37
-
 assay at Hafnia alvei

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.18 4.12
-
 L-lysine pH 6.0, 37°C, recombinant wild-type enzyme Hafnia alvei
4.1.1.18 5.43
-
 L-lysine pH 6.0, 37°C, recombinant mutant E583G Hafnia alvei

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.18 6
-
 assay at Hafnia alvei

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.18 pyridoxal 5'-phosphate
-
 Hafnia alvei

General Information

EC Number General Information Comment Organism
4.1.1.18 additional information the LDC monomer has a C-terminal domain (residues 564-715), that has a predominantly alpha-helical outer surface and an inner surface that consists of two sets of beta-sheets, and is very important. The C-terminal domain forms part of the entry channel into the active site of the enzyme. The amino acid change E583G changes a residue located in this channel with improving effects on enzyme activity Hafnia alvei

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.18 0.84
-
 L-lysine pH 6.0, 37°C, recombinant wild-type enzyme Hafnia alvei
4.1.1.18 1.68
-
 L-lysine pH 6.0, 37°C, recombinant mutant E583G Hafnia alvei