1.1.1.103: L-threonine 3-dehydrogenase
This is an abbreviated version!
For detailed information about L-threonine 3-dehydrogenase, go to the full flat file.
Reaction
Synonyms
CLOST_1621, L-ThrDH, L-threonine dehydrogenase, More, orf382, TDG, TDH, Thr dehydrogenase, ThrDH, threonine 3-dehydrogenase, threonine dehydrogenase
ECTree
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General Information
General Information on EC 1.1.1.103 - L-threonine 3-dehydrogenase
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evolution
malfunction
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knockdown of the enzyme and posttranslational downregulation by microRNA-9 inhibits reprogramming efficiency
metabolism
physiological function
additional information
the enzyme belongs to the extended short-chain alcohol dehydrogenase superfamily
evolution
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the enzyme belongs to the extended short-chain alcohol dehydrogenase superfamily
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embryonic stem cells are critically dependent on the amino acid threonine, and threonine catabolism via the TDH enzyme is important to the growth and metabolic state of mouse embryonic stem cells
physiological function
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over-expression of a feedback-resistant threonine operon thrA*BC, with deletion of the genes that encode threonine dehydrogenase tdh and threonine transporters tdcC and sstT, and introduction of a mutant threonine exporter rhtA23 in Escherichia coliMDS42. The resulting strain shows about 83% increase in L-threonine production when cells are grown by flask fermentation, compared to a wild-type Escherichia coli strain MG1655 engineered with the same threonine-specific modifications described above
physiological function
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the enzyme plays an important role in the regulation of somatic cell reprogramming
physiological function
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over-expression of a feedback-resistant threonine operon thrA*BC, with deletion of the genes that encode threonine dehydrogenase tdh and threonine transporters tdcC and sstT, and introduction of a mutant threonine exporter rhtA23 in Escherichia coliMDS42. The resulting strain shows about 83% increase in L-threonine production when cells are grown by flask fermentation, compared to a wild-type Escherichia coli strain MG1655 engineered with the same threonine-specific modifications described above
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active site structure and subunit interaction, overview
additional information
the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues
additional information
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the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues
additional information
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the enzyme possesses a glycine-rich NAD+-binding domain at the N terminus and conserved catalytic triad of YxxxK residues
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