5.1.1.10: amino-acid racemase
This is an abbreviated version!
For detailed information about amino-acid racemase, go to the full flat file.
Word Map on EC 5.1.1.10
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5.1.1.10
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racemization
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pyridoxal
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synthesis
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plp-dependent
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alpha-hydrogen
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plp-binding
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buchneri
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5'-phosphate-dependent
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2-epimerase
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biotechnology
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diagnostics
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analysis
- 5.1.1.10
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racemization
- pyridoxal
- synthesis
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plp-dependent
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alpha-hydrogen
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plp-binding
- buchneri
-
5'-phosphate-dependent
-
2-epimerase
- biotechnology
- diagnostics
- analysis
Reaction
Synonyms
AAR, ACL racemase, amino acid racemase, amino-acid racemase, ArgR, BAR, broad specificity amino acid racemase, broad substrate specificity amino acid racemase, broad-specificity amino acid racemase, broad-spectrum amino acid racemase, Bsar, D-amino acid racemase 1, DAR1, GkNSAAR, L-Amino acid racemase, LACBS_00576, MalY, More, N-succinylamino acid racemase, NSAR, patB, PH0138, PLP-independent amino acid racemase, Racemase, amino acid, RacX, YgeA
ECTree
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Engineering
Engineering on EC 5.1.1.10 - amino-acid racemase
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H152S
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ratio of elimination reaction to racemization is 1.4 compared to 3.7 in wild-type
N154F
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ratio of elimination reaction to racemization is 0.33 compared to 3.7 in wild-type
P153S
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ratio of elimination reaction to racemization is 0.24 compared to 3.7 in wild-type
Q155D
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ratio of elimination reaction to racemization is 0.25 compared to 3.7 in wild-type
I384M
I83L/D361V/Y396C
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specific activity: 0.0303 (substrate Trp), 0.0257 (substrate Phe), 0.473 (substrate Lys), 0.0121 (substrate Ala)
L126H/Y396C
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specific activity: 0.0524 (substrate Trp), 0.0436 (substrate Phe), 0.477 (substrate Lys), 0.0144 (substrate Ala)
R174A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R174K
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. Mutant Bsar-R174K shows no deleterious effects on the transgenic plants and broad range amino acid racemase activity, might serve as a good selection marker
Y293A/Y301S/Y396C
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specific activity: 0.0267 (substrate Trp), 0.0249 (substrate Phe), 0.458 (substrate Lys), 0.0141 (substrate Ala)
Y396C
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specific activity: 0.0487 (substrate Trp), 0.00706 (substrate Phe), 0.03215 (substrate Lys), 0.825 (substrate Ala)
R174A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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R174K
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme. Mutant Bsar-R174K shows no deleterious effects on the transgenic plants and broad range amino acid racemase activity, might serve as a good selection marker
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additional information
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I384M mutant BAR shows the highest activity for Trp. Using I384M mutant BAR the proportion of D-Trp reaches 43% while wildtype BAR racemizes only 6% of initial L-Trp
I384M
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specific activity: 0.124 (substrate Trp), 0.0744 (substrate Phe), 0.223 (substrate Lys), 0.026 (substrate Ala)
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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. Enzyme AAR is not a suitable candidate compared to enzyme Lyr (EC 5.1.1.5) from Proteus mirabilis
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. Enzyme AAR is not a suitable candidate compared to enzyme Lyr (EC 5.1.1.5) from Proteus mirabilis
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additional information
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random mutagenesis on bar gene is performed to obtain mutant BAR derivates with high activity for Trp. Five positive mutant are isolated after the two-step-screening of the randomly mutated BAR
additional information
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substitutions at Y396 and I384 increases the Trp specific racemization activity and the racemazation activity for overall amino acids, respectively