Reaction participants Show >> << Hide
- Name help_outline L-threonine Identifier CHEBI:57926 Charge 0 Formula C4H9NO3 InChIKeyhelp_outline AYFVYJQAPQTCCC-GBXIJSLDSA-N SMILEShelp_outline C[C@@H](O)[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 32 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline D-threonine Identifier CHEBI:57757 Charge 0 Formula C4H9NO3 InChIKeyhelp_outline AYFVYJQAPQTCCC-STHAYSLISA-N SMILEShelp_outline C[C@H](O)[C@@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:13913 | RHEA:13914 | RHEA:13915 | RHEA:13916 | |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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First characterization of an archaeal amino acid racemase with broad substrate specificity from the hyperthermophile Pyrococcus horikoshii OT-3.
Kawakami R., Sakuraba H., Ohmori T., Ohshima T.
A novel amino acid racemase with broad substrate specificity (BAR) was recently isolated from the hyperthermophilic archaeon Pyrococcus horikoshii OT-3. Characterization of this enzyme has been difficult, however, because the recombinant enzyme is produced mainly as an inclusion body in Escherichi ... >> More
A novel amino acid racemase with broad substrate specificity (BAR) was recently isolated from the hyperthermophilic archaeon Pyrococcus horikoshii OT-3. Characterization of this enzyme has been difficult, however, because the recombinant enzyme is produced mainly as an inclusion body in Escherichia coli. In this study, expression of the recombinant protein into the soluble fraction was markedly improved by co-expression with chaperone molecules. The purified enzyme retained its full activity after incubation at 80°C for at least 2 h in buffer (pH 7-10), making this enzyme the most thermostable amino acid racemase so far known. Besides the nine amino acids containing hydrophobic and aromatic amino acids previously reported (Kawakami et al., Amino Acids, 47, 1579-1587, 2015), the enzyme exhibited substantial activity toward Thr (about 42% of relative activity toward Phe) and showed no activity toward Arg, His, Gln, and Asn. The substrate specificity of this enzyme thus differs markedly from those of other known amino acid racemases. In particular, the high reaction rate with Trp and Tyr, in addition to Leu, Met and Phe as substrates is a noteworthy feature of this enzyme. The high reactivity toward Trp and Tyr, as well as extremely high thermostability, is likely a major advantage of using BAR for biochemical conversion of these aromatic amino acids. << Less
J. Biosci. Bioeng. 124:23-27(2017) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
Published in: Amos, H. A racemase for threonine in