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- Name help_outline (2S)-2-amino-3-oxobutanoate Identifier CHEBI:78948 Charge 0 Formula C4H7NO3 InChIKeyhelp_outline SAUCHDKDCUROAO-VKHMYHEASA-N SMILEShelp_outline CC(=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
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,717 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline aminoacetone Identifier CHEBI:58320 Charge 1 Formula C3H8NO InChIKeyhelp_outline BCDGQXUMWHRQCB-UHFFFAOYSA-O SMILEShelp_outline CC(=O)C[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 5 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CO2 Identifier CHEBI:16526 (CAS: 124-38-9) help_outline Charge 0 Formula CO2 InChIKeyhelp_outline CURLTUGMZLYLDI-UHFFFAOYSA-N SMILEShelp_outline O=C=O 2D coordinates Mol file for the small molecule Search links Involved in 1,032 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:25653 | RHEA:25654 | RHEA:25655 | RHEA:25656 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Highly thermostable L-threonine dehydrogenase from the hyperthermophilic archaeon Thermococcus kodakaraensis.
Bashir Q., Rashid N., Jamil F., Imanaka T., Akhtar M.
l-Threonine dehydrogenase, a key enzyme in the l-threonine metabolism, catalyses the NAD(+)-dependent conversion of l-threonine to 2-amino-3-ketobutyrate, that non-enzymically decarboxylates to aminoacetone. A search of the genome sequence of hyperthermophilic archaeon, Thermococcus kodakaraensis ... >> More
l-Threonine dehydrogenase, a key enzyme in the l-threonine metabolism, catalyses the NAD(+)-dependent conversion of l-threonine to 2-amino-3-ketobutyrate, that non-enzymically decarboxylates to aminoacetone. A search of the genome sequence of hyperthermophilic archaeon, Thermococcus kodakaraensis revealed the presence of a closely related orthologue (TK0916) of archaeal and bacterial l-threonine dehydrogenase genes. Expression in Escherichia coli, purification and characterization of the TK0916 gene product revealed that this gene actually coded for a protein with high levels of l-threonine dehydrogenase activity (7.26 U mg(-1)). The enzyme exhibited highest activity at pH 12 and 90 degrees C. The K(m) values for l-threonine and NAD(+) at 50 degrees C were 1.6 mM and 0.028 mM, respectively. The enzyme activity was dependent on divalent cations. The half-life of the enzyme was more than 2 h at 85 degrees C and 24 min in boiling water. This is the most thermostable threonine dehydrogenase exhibiting optimal activity at the highest pH (12) reported to date. This is the first report on the characterization of a TDH from genus Thermococcus. << Less
J. Biochem. 146:95-102(2009) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
Comments
This reaction can occur spontaneously; in aqueous solution, L-2-amino-3-oxobutanoate can spontaneously decarboxylate to form aminoacetone. RHEA:25653 part of RHEA:43524. RHEA:25653 part of RHEA:33239.