Literature summary for 2.1.2.1 extracted from

Angelaccio, S.; Dworkowski, F.; Di Bello, A.; Milano, T.; Capitani, G.; Pascarella, S.
Conformational transitions driven by pyridoxal-5-phosphate uptake in the psychrophilic serine hydroxymethyltransferase from Psychromonas ingrahamii (2014), Proteins, 82, 2831-2841.

Search for more literature for 2.1.2.1

Cloned(Commentary)

Cloned (Comment)	Organism
gene glyA, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain HMS174 (DE3)	Psychromonas ingrahamii

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified recombinant enzyme in apoform, mixing of 200 nl of 10 mg/ml protein in 50 mM HEPES, pH 7.2, and 0.2 mM DTT with 200 nl of well solution containing 2M ammonium sulfate, 150 mM sodium chloride, and 100 mM sodium cacodylate, pH 6.5, 4°C, several days, X-ray diffraction structure determination and analysis at 1.85 A resolution, molecular replacement and modeling	Psychromonas ingrahamii

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
45050	-	2 * 45050, recombinant N-terminally His-tagged enzyme, mass spectrometry	Psychromonas ingrahamii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
5,10-methylenetetrahydrofolate + glycine + H2O	Psychromonas ingrahamii	-	tetrahydrofolate + L-serine	-	r

Organism

Organism	UniProt	Comment	Textmining
Psychromonas ingrahamii	A1SUU0	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli strain HMS174 (DE3) by nickel affinity chromatography	Psychromonas ingrahamii

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5,10-methylenetetrahydrofolate + glycine + H2O	-	Psychromonas ingrahamii	tetrahydrofolate + L-serine	-	r

Subunits

Subunits	Comment	Organism
dimer	2 * 45050, recombinant N-terminally His-tagged enzyme, mass spectrometry	Psychromonas ingrahamii

Synonyms

Synonyms	Comment	Organism
serine hydroxymethyltransferase	-	Psychromonas ingrahamii
SHMT	-	Psychromonas ingrahamii

Cofactor

Cofactor	Comment	Organism	Structure
5,10-methylenetetrahydrofolate	-	Psychromonas ingrahamii
pyridoxal 5'-phosphate	dependent on, cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side	Psychromonas ingrahamii
tetrahydrofolate	-	Psychromonas ingrahamii

General Information

General Information	Comment	Organism
evolution	the enzyme belongs to the fold type-I superfamily of PLP-dependent enzymes	Psychromonas ingrahamii
additional information	the enzyme psychrophilic shows high catalytic activity at low temperature and thermolability, three-dimensional structure analysis and structure-function relationship, homology modeling of the holoenzyme form, overview. The apoform enzyme is in an open conformation and possesses four or five (in chain A) disordered loops that interact with the cofactor. Cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side	Psychromonas ingrahamii
physiological function	SHMTs are an important group of pyridoxal-5'-phosphate-dependent enzymes that catalyze the reversible conversion of L-serine and tetrahydropteroylglutamate to glycine and 5,10-methylenetetrahydropteroylglutamate. The enzyme plays a central role in one-carbon unit metabolism	Psychromonas ingrahamii

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Release 2023.1 (January 2023)