L-threonine dehydrogenase: Difference between revisions

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== References ==
== References ==
* {{cite journal |author=Epperly BR, Dekker EE |title=L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies |journal=J. Biol. Chem. |volume=266 |issue=10 |pages=6086–92 |date=April 1991 |pmid=2007567 |doi= |url=http://www.jbc.org/cgi/pmidlookup?view=long&pmid=2007567}}
* {{cite journal | vauthors = Epperly BR, Dekker EE | title = L-threonine dehydrogenase from Escherichia coli. Identification of an active site cysteine residue and metal ion studies | journal = The Journal of Biological Chemistry | volume = 266 | issue = 10 | pages = 6086–92 | date = April 1991 | pmid = 2007567 | doi = | url = http://www.jbc.org/cgi/pmidlookup?view=long&pmid=2007567 }}
* {{cite journal |author=Edgar AJ |title=The human L-threonine 3-dehydrogenase gene is an expressed pseudogene |journal=BMC Genet. |volume=3|pages=18 |date=October 2002 |pmid=12361482 |doi= 10.1186/1471-2156-3-18|url=http://www.biomedcentral.com/1471-2156/3/18 |pmc=131051}}
* {{cite journal | vauthors = Edgar AJ | title = The human L-threonine 3-dehydrogenase gene is an expressed pseudogene | journal = BMC Genetics | volume = 3 | pages = 18 | date = October 2002 | pmid = 12361482 | pmc = 131051 | doi = 10.1186/1471-2156-3-18 | url = http://www.biomedcentral.com/1471-2156/3/18 }}


{{Amino acid metabolism enzymes}}
{{Amino acid metabolism enzymes}}
{{Alcohol oxidoreductases}}
{{Alcohol oxidoreductases}}


{{biochem-stub}}
{{biochem-stub}}

Latest revision as of 08:35, 10 January 2019

L-Threonine dehydrogenase
Identifiers
EC number1.1.1.103
CAS number9067-99-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
L-Threonine dehydrogenase
Identifiers
SymbolTDH
Entrez157739
HUGO15547
RefSeqNM_152566
UniProtQ8IZJ6
Other data
EC number1.1.1.103
LocusChr. 8 p23.1

L-Threonine dehydrogenase is an enzyme that facilitates the catabolism of threonine. It catalyses its conversion to glycine via 2-amino-3-ketobutyrate with concomitant reduction of NAD+.

References

  • 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. PMID 2007567.
  • 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.