Literature summary for 4.3.1.19 extracted from

Hofmeister, A.E.M.; Grabowski, R.; Linder, D.; Buckel, W.
L-Serine and L-threonine dehydratase from Clostridium propionicum. Two enzymes with different prosthetic groups (1993), Eur. J. Biochem., 215, 341-349.

Search for more literature for 4.3.1.19

Inhibitors

Inhibitors	Comment	Organism	Structure
hydroxylamine	-	Anaerotignum propionicum
NaBH4	-	Anaerotignum propionicum
phenylhydrazine	reversed by pyridoxal 5'-phosphate	Anaerotignum propionicum

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
7.7	-	L-Thr	-	Anaerotignum propionicum
380	-	L-Ser	-	Anaerotignum propionicum

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
39000	-	4 * 39000, SDS-PAGE	Anaerotignum propionicum
160000	-	gel filtration	Anaerotignum propionicum

Organism

Organism	UniProt	Comment	Textmining
Anaerotignum propionicum	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Anaerotignum propionicum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
additional information	-	-	Anaerotignum propionicum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Ser	-	Anaerotignum propionicum	pyruvate + NH3	-	?
L-threonine	-	Anaerotignum propionicum	2-oxobutanoate + NH3	-	?

Subunits

Subunits	Comment	Organism
tetramer	4 * 39000, SDS-PAGE	Anaerotignum propionicum

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	required	Anaerotignum propionicum

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Release 2023.1 (January 2023)