Literature summary extracted from

Bhatt, A.N.; Bhakuni, V.
Characterization of pyridoxal 5'-phosphate-binding domain and folding intermediate of Bacillus subtilis serine hydroxymethyltransferase: an autonomous folding domain (2008), J. Biochem., 144, 295-303.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
2.1.2.1	expressed in Escherichia coli BL21(DE3) cells	Bacillus subtilis

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
2.1.2.1	25000	-	refolded pyridoxal-5'-phosphate-binding domain of SHMT, gel filtration	Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number	Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
2.1.2.1	L-serine + tetrahydrofolate	Bacillus subtilis	-	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.2.1	Bacillus subtilis	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
2.1.2.1	the pyridoxal-5'-phosphate-binding domain of SHMT is purified from inclusion bodies by rapid mixing followed by MonoQ column chromatography	Bacillus subtilis

Renatured (Commentary)

EC Number	Renatured (Comment)	Organism
2.1.2.1	5 ml of supernatant containing the solubilized domain is added drop by drop to 100 ml of stirring potassium phosphate buffer (50 mM, pH 7.4 containing 1 mM EDTA, 2 mM beta-mercaptoethanol, 0.1 mM pyridoxal 5'-phosphate, and 0.1 M NaCl)	Bacillus subtilis

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.1.2.1	L-serine + tetrahydrofolate	-	Bacillus subtilis	glycine + 5,10-methylenetetrahydrofolate + H2O	-	?

Subunits

EC Number	Subunits	Comment	Organism
2.1.2.1	dimer	native SHMT	Bacillus subtilis

Synonyms

EC Number	Synonyms	Comment	Organism
2.1.2.1	serine hydroxymethyltransferase	-	Bacillus subtilis
2.1.2.1	SHMT	-	Bacillus subtilis

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
2.1.2.1	30	65	a broad sigmoidal transition between 30°C and 65°C having an apparent Tm of about 48°C is observed for the native dimeric SHMT molecule, SHMT is a noncooperative molecule which starts losing the structure from very low temperature (30°C) and loses most of ist secondary structure at relatively high temperature	Bacillus subtilis

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
2.1.2.1	pyridoxal 5'-phosphate	-	Bacillus subtilis

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Release 2023.1 (January 2023)