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5.1.1.10 |
Description |
Amino-acid racemase |
Alternative names |
broad-specificity amino acid racemase;
BAR; |
Catalyzed reaction |
An L-amino acid = a D-amino acid. |
Cofactor |
Pyridoxal-phosphate. |
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The bacterial sequences identified in the literature as BARs (such as a P. putida BAR, accession number AAZ83975) usually show maximum activity towards lysine, and have been included in lysine racemase subfamily a (5.1.1.5_a) |
Organisms |
-Eubacteria -Archea |
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Family |
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Links |
Enzyme (activities) 5.1.1.10
BRENDA (activities) 5.1.1.10
KEGG (pathways) 5.1.1.10
PLPMDB (PLP mutants) 5.1.1.10
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References |
Kawakami, R.; Ohshida, T.; Sakuraba, H.; Ohshima, T. (2018) A Novel PLP-Dependent Alanine/Serine Racemase From the Hyperthermophilic Archaeon Pyrococcus horikoshii OT-3 Front Microbiol 9 1481. Kawakami, R.; Sakuraba, H.; Ohmori, T.; Ohshima, T. (2017) First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3 J Biosci Bioeng 124 23-27. Kawakami, R.; Ohmori, T.; Sakuraba H, Ohshima, T. (2015) Identification of a novel amino acid racemase from a hyperthermophilic archaeon Pyrococcus horikoshii OT-3 induced by D-amino acids Amino Acids 47 1579-87. Reynolds, K.; Martin, J.; Shen, S. J.; Esaki, N.; Soda, K.; Floss, H. G. (1991) Mechanistic studies of two amino acid racemases of broad substrate specificity from Pseudomonas striata and Aeromonas caviae J Basic Microbiol 31 177-88. Roise, D.; Soda, K.; Yagi, T.; Walsh, C. T. (1984) Inactivation of the Pseudomonas striata broad specificity amino acid racemase by D and L isomers of beta-substituted alanines: kinetics, stoichiometry, active site peptide, and mechanistic studies Biochemistry 23 5195-201. Soda, K.; Osumi, T. (1969) Crystalline amino acid racemase with low substrate specificity Biochem Biophys Res Commun 35 363-8. Articles on 5.1.1.10 |
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last changed |
2019/06/20 13:29 |
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