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Literature summary 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)

EC Number Cloned (Comment) Organism
5.1.1.5 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
5.1.1.10 gene AAR, recombinant expression in Escherichia coli strain BL21(DE3), showing lower lysine racemase activity, protein AAR is highly insoluble in Escherichia coli Lacticaseibacillus paracasei

Protein Variants

EC Number Protein Variants Comment Organism
5.1.1.5 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
5.1.1.10 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. Enzyme AAR is not a suitable candidate compared to enzyme Lyr (EC 5.1.1.5) from Proteus mirabilis Lacticaseibacillus paracasei

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
5.1.1.5 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)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.1.1.5 L-lysine Proteus mirabilis
-
 D-lysine
-
 r
5.1.1.5 L-lysine Proteus mirabilis BCRC10725
-
 D-lysine
-
 r
5.1.1.10 L-lysine Lacticaseibacillus paracasei
-
 D-lysine
-
 r
5.1.1.10 L-lysine Lacticaseibacillus paracasei ATCC 334
-
 D-lysine
-
 r

Organism

EC Number Organism UniProt Comment Textmining
5.1.1.5 Proteus mirabilis
-
-
-
5.1.1.5 Proteus mirabilis BCRC10725
-
-
-
5.1.1.10 Lacticaseibacillus paracasei
-
-
-
5.1.1.10 Lacticaseibacillus paracasei ATCC 334
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.1.1.5 L-lysine
-
 Proteus mirabilis D-lysine
-
 r
5.1.1.5 L-lysine
-
 Proteus mirabilis BCRC10725 D-lysine
-
 r
5.1.1.10 L-lysine
-
 Lacticaseibacillus paracasei D-lysine
-
 r
5.1.1.10 L-lysine
-
 Lacticaseibacillus paracasei ATCC 334 D-lysine
-
 r

Subunits

EC Number Subunits Comment Organism
5.1.1.5 ? x * 45000, recombinant enzyme, SDS-PAGE Proteus mirabilis
5.1.1.10 ? x * 43000, recombinant enzyme, SDS-PAGE Lacticaseibacillus paracasei

Synonyms

EC Number Synonyms Comment Organism
5.1.1.5 lyr
-
 Proteus mirabilis
5.1.1.10 AAR
-
 Lacticaseibacillus paracasei
5.1.1.10 amino acid racemase
-
 Lacticaseibacillus paracasei
5.1.1.10 additional information cf. EC 5.1.1.5 Lacticaseibacillus paracasei

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
5.1.1.5 37
-
 recombinant enzyme Proteus mirabilis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
5.1.1.5 20 50 activity range, recombinant enzyme, profile overview Proteus mirabilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
5.1.1.5 7
-
 recombinant enzyme Proteus mirabilis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
5.1.1.5 4 8 activity range, recombinant enzyme, profile overview Proteus mirabilis

Cofactor

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