Literature summary for 2.1.1.10 extracted from

Li, K.; Li, G.; Bradbury, L.M.; Hanson, A.D.; Bruner, S.D.
Crystal structure of the homocysteine methyltransferase MmuM from Escherichia coli (2015), Biochem. J., 473, 277-284.

Search for more literature for 2.1.1.10

Cloned(Commentary)

Cloned (Comment)	Organism
-	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
in oxidized, apo, and metallated form, to 1.8-1.9 A resolution	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
Y71F/T169Y	mutant designed to mimic the betaine-homocysteine methyltransferase substrate binding pocket, complete loss of activity	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
additional information	contrary to human enzyme, K+ is not required	Escherichia coli
Zn2+	required. The metallated crystal form has residues C229, C295 and C296 coordinated to a Zn2+ center. the coordination of homocysteine to metal with a distance of 2.8 A contributes to near-ideal Zn2+-centered tetrahedron geometry	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
34490	-	1 * 34490, calculated, 1 * 35000, SDS-PAGE	Escherichia coli
35000	-	gel filtration	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	Q47690	-	-

Subunits

Subunits	Comment	Organism
monomer	1 * 34490, calculated, 1 * 35000, SDS-PAGE	Escherichia coli

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Release 2023.1 (January 2023)