Literature summary extracted from

Zhou, Z.S.; Smith, A.E.; Matthews, R.G.
L-Selenohomocysteine: One-step synthesis from L-selenomethionine and kinetic analysis as substrate for methionine synthases (2000), Bioorg. Med. Chem. Lett., 10, 2471-2475.

KM Value [mM]

EC Number	KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
2.1.1.13	0.017	-	L-Selenohomocysteine	-	Escherichia coli
2.1.1.13	0.069	-	L-homocysteine	-	Escherichia coli
2.1.1.14	0.016	-	selenohomocysteine	-	Escherichia coli
2.1.1.14	0.069	-	homocysteine	-	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.1.1.13	Escherichia coli	-	-	-
2.1.1.14	Escherichia coli	-	-	-

Reaction

EC Number	Reaction	Comment	Organism	Reaction ID
2.1.1.14	5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine	mechanism	Escherichia coli	a

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.1.1.13	S-adenosyl-L-methionine + L-selenohomocysteine	-	Escherichia coli	selenomethionine + S-adenosyl-L-homocysteine	-	?
2.1.1.14	S-adenosylmethionine + L-selenohomocysteine	-	Escherichia coli	L-selenomethionine + S-adenosylhomocysteine	reaction catalyzed both by vitamin B12 dependent and independent enzyme	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)