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L-threonine 3-dehydrogenase

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L-threonine 3-dehydrogenase
L-threonine 3-dehydrogenase homotetramer, Thermus thermophilus
Identifiers
EC no.1.1.1.103
CAS no.9067-99-6
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

In enzymology, L-threonine 3-dehydrogenase (EC 1.1.1.103), or just threonine dehydrogenase, is an enzyme that participates in the process of breaking down threonine in certain non-human organisms like mice.[1] In particular, it catalyzes the chemical reaction

2D representation of the chemical structure of threonine.
L-threonine
+ NAD+
 
 
 
H+
Reversible left-right reaction arrow with minor forward product(s) to top right and minor reverse substrate(s) from bottom right
 
H+
 
2D representation of the chemical structure of Q27094776.
(S)-2-amino-3-ketobutyric acid
+ NADH
 

The two substrates of this enzyme are L-threonine and oxidised nicotinamide adenine dinucleotide (NAD+). Its products are (S)-2-amino-3-ketobutyric acid, reduced NADH, and a proton.[2][3][4][5][6]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-threonine:NAD+ oxidoreductase. Other names in common use include L-threonine dehydrogenase, and threonine 3-dehydrogenase.

In humans

[edit]
TDH
Identifiers
AliasesTDH, SDR14E1P, L-threonine dehydrogenase (pseudogene)
External IDsGeneCards: TDH
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

157739

n/a

Ensembl

ENSG00000154316
ENSG00000284856

n/a

UniProt

n
a

n/a

RefSeq (mRNA)

NM_152566

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)Chr 8: 11.34 – 11.37 Mbn/a
PubMed search[8]n/a
Wikidata
View/Edit Human

In humans, the homolog gene, TDH, is a non-functional pseudogene.[9] The loss of an acceptor splice site consistently leads to a non-functional truncated protein.[9] The primary pathway for threonine degradation in humans instead starts with threonine ammonia-lyase (aka threonine dehydratase) and produces propionyl-CoA instead of glycine.[10]

Structural studies

[edit]

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 2D8A​, PDB: 2DFV​, and PDB: 2DQ4​.

References

[edit]
  1. ↑ "Q8K3F7 · TDH_MOUSE". uniprot.org. UniProt consortium. Retrieved 2026-08-12.
  2. ↑ Enzyme 1.1.1.103 at KEGG Pathway Database.
  3. ↑ Green ML, Elliott WH (1964). "The enzymic formation of aminoacetone from threonine and its further metabolism". Biochem. J. 92 (3): 537–49. doi:10.1042/bj0920537. PMC 1206098. PMID 4284408.
  4. ↑ Hartshorne D, Greenberg DM (1964). "Studies on liver threonine dehydrogenase". Arch. Biochem. Biophys. 105: 173–8. doi:10.1016/0003-9861(64)90250-4. PMID 14165492.
  5. ↑ Epperly BR, Dekker EE (April 1991). "L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies". The Journal of Biological Chemistry. 266 (10): 6086–92. doi:10.1016/S0021-9258(18)38087-6. PMID 2007567.
  6. ↑ Edgar AJ (October 2002). "The human L-threonine 3-dehydrogenase gene is an expressed pseudogene". BMC Genetics. 3 18. doi:10.1186/1471-2156-3-18. PMC 131051. PMID 12361482.
  7. 1 2 3 ENSG00000284856 GRCh38: Ensembl release 89: ENSG00000154316, ENSG00000284856 – Ensembl, May 2017
  8. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  9. 1 2 "Q8IZJ6 · TDH_HUMAN". uniprot.org. UniProt consortium. Retrieved 2026-08-12.
  10. ↑ Nelson DL, Cox MC (2021). Lehninger principles of biochemistry, 8th edition (kindle version). New York: WH Freeman. p. 3357. ISBN 978-1-319-32238-0.


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