Literature summary for 1.1.2.10 extracted from

Wang, L.; Hibino, A.; Suganuma, S.; Ebihara, A.; Iwamoto, S.; Mitsui, R.; Tani, A.; Shimada, M.; Hayakawa, T.; Nakagawa, T.
Preference for particular lanthanide species and thermal stability of XoxFs in Methylorubrum extorquens strain AM1 (2020), Enzyme Microb. Technol., 136, 109518 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
La3+	lanthanide-dependent enzyme. Although La3+ and Nd3+ have similar distributions in nature, XoxF can chose La3+ preferentially, likely because of its higher Lewis acidity, which is important for the catalytic activity of the enzyme	Methylorubrum extorquens
Nd3+	lanthanide-dependent enzyme. Although La3+ and Nd3+ have similar distributions in nature, XoxF can chose La3+ preferentially, likely because of its higher Lewis acidity, which is important for the catalytic activity of the enzyme	Methylorubrum extorquens

Organism

Organism	UniProt	Comment	Textmining
Methylorubrum extorquens	C5B120	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Methylorubrum extorquens

Synonyms

Synonyms	Comment	Organism
XoxF-type methanol dehydrogenase	-	Methylorubrum extorquens

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Release 2023.1 (January 2023)