5.1.1.5: lysine racemase
This is an abbreviated version!
For detailed information about lysine racemase, go to the full flat file.
Word Map on EC 5.1.1.5
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5.1.1.5
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d-lysine
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putida
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lyr
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enantiomers
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l-pipecolate
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non-antibiotic
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molecular biology
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biotechnology
- 5.1.1.5
- d-lysine
- putida
- lyr
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enantiomers
- l-pipecolate
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non-antibiotic
- molecular biology
- biotechnology
Reaction
Synonyms
lyr, lysine racemase, Racemase, lysine
ECTree
5.1.1.5 lysine racemaseAdvanced search results
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results (Engineering
Engineering on EC 5.1.1.5 - lysine racemase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
T224I
site-directed mutagenesis, the mutant shows significantly decreased activity compared to the wild-type enzyme
T224I/W355Y
site-directed mutagenesis, the double mutant shows significantly decreased activity compared to the wild-type enzyme
W355Y
site-directed mutagenesis, the mutant shows significantly decreased activity compared to the wild-type enzyme
A165K/N174L/T391Y
site-directed mutagenesis, the mutant shows no activity towards L-Ala, L-Lys, or L-Arg
S394C
site-directed mutagenesis, the mutant shows 1.5fold increased activity with L-arginine compared to the wild-type enzyme
S394N
site-directed mutagenesis, the mutant shows about 2.2fold increased activity with L-arginine compared to the wild-type enzyme
S394T
site-directed mutagenesis, the mutant shows 1.8fold increased activity with L-arginine compared to the wild-type enzyme
S394Y
site-directed mutagenesis, the mutant shows 2.1fold increased activity with L-arginine compared to the wild-type enzyme
T391Y
site-directed mutagenesis, the mutant shows 47% reduced activity with L-lysine compared to the wild-type enzyme
T391Y/S394Y
site-directed mutagenesis,the mutant exhibits significantly reduced specific activity towards L-Lys (6% residual activity) and toward L-Arg (0.9% residual activity)
A165K/N174L/T391Y
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site-directed mutagenesis, the mutant shows no activity towards L-Ala, L-Lys, or L-Arg
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S394C
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site-directed mutagenesis, the mutant shows 1.5fold increased activity with L-arginine compared to the wild-type enzyme
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S394N
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site-directed mutagenesis, the mutant shows about 2.2fold increased activity with L-arginine compared to the wild-type enzyme
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S394T
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site-directed mutagenesis, the mutant shows 1.8fold increased activity with L-arginine compared to the wild-type enzyme
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S394Y
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site-directed mutagenesis, the mutant shows 2.1fold increased activity with L-arginine compared to the wild-type enzyme
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T391Y
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site-directed mutagenesis, the mutant shows 47% reduced activity with L-lysine compared to the wild-type enzyme
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additional information
additional information
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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
additional information
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in an attempt to limit extracellular Lyr (while retaining the catalytic activity), amino acids 1-36 are removed from the enzyme (LyrM37) and a C-terminal KDEL ER retention motif (LyrM37-KDEL) is added
additional information
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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
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