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Literature summary for 5.1.1.5 extracted from

  • Wang, X.; Yang, L.; Cao, W.; Ying, H.; Chen, K.; Ouyang, P.
    Efficient production of enantiopure D-lysine from L-lysine by a two-enzyme cascade system (2016), Catalysts, 6, 168-178 .
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
gene LYR, functional recombinant expression in Escherichia coli strain BL21(DE3), showing high lysine racemase activity. L-Lysine is rapidly racemized to give DL-lysine, and the D-lysine yield is approximately 48% after 0.5 h Proteus mirabilis

Protein Variants

Protein Variants Comment Organism
additional information for D-lysine production, a two-step process for D-lysine production from L-lysine by the successive microbial racemization and asymmetric degradation with lysine racemase and decarboxylase is developed. L-lysine is rapidly racemized to give DL-lysine, and L-lysine is selectively catabolized to generate cadaverine by lysine decarboxylase. In order to obtain enantiopure D-lysine, chiral selective degradation of L-lysine from the reaction mixture of DL-lysine is necessary. Under optimal conditions, 750.7 mmol/l D-lysine is finally obtained from 1710 mmol/l L-lysine after 1 h of racemization reaction and 0.5 h of decarboxylation reaction. D-lysine yield can reach 48.8% with enantiomeric excess of 99% or more Proteus mirabilis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information the addition of metal ions including Ca2+, Co2+, Fe2+, Fe3+, K+, Ni2+, Mg2+, Mn2+, Cu2+, and Zn2+ at 1 mM has no significant effect on LYR activity Proteus mirabilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-lysine Proteus mirabilis
-
D-lysine
-
r
L-lysine Proteus mirabilis BCRC10725
-
D-lysine
-
r

Organism

Organism UniProt Comment Textmining
Proteus mirabilis
-
-
-
Proteus mirabilis BCRC10725
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-lysine
-
Proteus mirabilis D-lysine
-
r
L-lysine
-
Proteus mirabilis BCRC10725 D-lysine
-
r

Subunits

Subunits Comment Organism
? x * 45000, recombinant enzyme, SDS-PAGE Proteus mirabilis

Synonyms

Synonyms Comment Organism
lyr
-
Proteus mirabilis

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
37
-
recombinant enzyme Proteus mirabilis

Temperature Range [┬░C]

Temperature Minimum [┬░C] Temperature Maximum [┬░C] Comment Organism
20 50 activity range, recombinant enzyme, profile overview Proteus mirabilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
recombinant enzyme Proteus mirabilis

pH Range

pH Minimum pH Maximum Comment Organism
4 8 activity range, recombinant enzyme, profile overview Proteus mirabilis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate required, addition of pyridoxal 5'-phosphate cannot further improve the specific activity of the recombinant whole-cell BL21?LYR Proteus mirabilis