Literature summary extracted from

Matthews, R.G.; Sheppard, C.; Goulding, C.
Methylenetetrahydrofolate reductase and methionine synthase: biochemistry and molecular biology (1998), Eur. J. Pediatr., 157, 54-59.

No PubMed abstract available

Protein Variants

EC Number	Protein Variants	Comment	Organism
1.5.1.20	A177V	enzyme is thermolabile	Escherichia coli

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
1.5.1.20	S-adenosylmethionine	-	Homo sapiens
1.5.1.20	S-adenosylmethionine	allosteric inhibition	Sus scrofa

Molecular Weight [Da]

EC Number	Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1.5.1.20	77000	-	2 * 77000	Homo sapiens
1.5.1.20	77000	-	2 * 77000	Sus scrofa

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.5.1.20	Escherichia coli	-	-	-
1.5.1.20	Homo sapiens	-	-	-
1.5.1.20	Sus scrofa	-	-	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
1.5.1.20	-	Escherichia coli

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.5.1.20	5,10-methylenetetrahydrofolate + NADPH	-	Homo sapiens	5-methyltetrahydrofolate + NADP+	-	?
1.5.1.20	5,10-methylenetetrahydrofolate + NADPH	-	Sus scrofa	5-methyltetrahydrofolate + NADP+	-	?

Subunits

EC Number	Subunits	Comment	Organism
1.5.1.20	dimer	2 * 77000	Homo sapiens
1.5.1.20	dimer	2 * 77000	Sus scrofa

Cofactor

EC Number	Cofactor	Comment	Organism	Structure
1.5.1.20	FAD	-	Homo sapiens
1.5.1.20	FAD	non covalently bound	Sus scrofa
1.5.1.20	FAD	flavoprotein with non-covalently bound FAD	Escherichia coli

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Release 2023.1 (January 2023)