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Literature summary for 4.1.1.18 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
Search for more literature for 4.1.1.18

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
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
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
V147F site-directed mutagenesis, the mutant shows increased LDC activity Hafnia alvei
V147F/E583G site-directed mutagenesis, the mutant shows 1.62fold increased LDC activity compared to wild-type enzyme Hafnia alvei

KM Value [mM]

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

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Hafnia alvei
-
-
-
Hafnia alvei AS1.1009
-
-
-

Purification (Commentary)

Purification (Comment) Organism
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)

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

Synonyms

Synonyms Comment Organism
LDC
-
 Hafnia alvei

Temperature Optimum [°C]

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

Turnover Number [1/s]

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

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Hafnia alvei

General Information

General Information Comment Organism
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]

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