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
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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
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General Information
General Information on EC 5.1.1.10 - amino-acid racemase
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evolution
the enzyme belongs to the fold-type I PLP-dependent enzyme family
malfunction
the mutation of either Asp210 or Lys267 to alanine abolish the racemization activity for 2-aminohexano-6-lactam
metabolism
physiological function
additional information
the enzyme is likely responsible for utilization of D-amino acids for growth
metabolism
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the enzyme is likely responsible for utilization of D-amino acids for growth
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enzyme AAR is responsible for D-amino acid utilization in Pyrococcus horikoshii
physiological function
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enzyme AAR is responsible for D-amino acid utilization in Pyrococcus horikoshii
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analysis of the structure-function relationship, overview. Lys241 is a key amino acid residue, active site structure of ACL racemase. The substrate binding site is typically located between Trp49 and Tyr137. Lys241 Nepsilon is considered to be important for recognizing the carbonyl O of the substrate. Lys241 also forms a salt bridge with Glu396. Asp210 and Lys267 are two plausible acid/base catalytic candidate residues, situated on the re and si faces of the pyridoxal 5'-phosphate ring, respectively. The racemization of ACL racemase proceeds via a two-base mechanism
additional information
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analysis of the structure-function relationship, overview. Lys241 is a key amino acid residue, active site structure of ACL racemase. The substrate binding site is typically located between Trp49 and Tyr137. Lys241 Nepsilon is considered to be important for recognizing the carbonyl O of the substrate. Lys241 also forms a salt bridge with Glu396. Asp210 and Lys267 are two plausible acid/base catalytic candidate residues, situated on the re and si faces of the pyridoxal 5'-phosphate ring, respectively. The racemization of ACL racemase proceeds via a two-base mechanism
additional information
conformational structure modeling of RacX based on the structure of Asp racemase from Pyrococcus horikoshi, PDB ID 1JFL
additional information
structural modeling of Ls-MalY, structure comparisons, overview
additional information
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conformational structure modeling of RacX based on the structure of Asp racemase from Pyrococcus horikoshi, PDB ID 1JFL
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additional information
Latilactobacillus sakei LT-13
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structural modeling of Ls-MalY, structure comparisons, overview
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