Literature summary for 2.1.1.69 extracted from

Zhao, Y.; Wang, N.; Wu, H.; Zhou, Y.; Huang, C.; Luo, J.; Zeng, Z.; Kong, L.
Structure-based tailoring of the first coumarins-specific bergaptol O-methyltransferase to synthesize bergapten for depigmentation disorder treatment (2020), J. Adv. Res., 21, 57-64 .

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli BL21(DE3) cells	Peucedanum praeruptorum

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with S-adenosyl-L-homocysteine and bergaptol	Peucedanum praeruptorum

Protein Variants

Protein Variants	Comment	Organism
I157F/V320I	the mutant shows about 4fold increased activity compared to the wild type enzyme	Peucedanum praeruptorum
I157H	the mutant shows strongly reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
I157Y	the mutant shows about 2.4fold increased activity compared to the wild type enzyme	Peucedanum praeruptorum
I157Y/S265F/V315N	the mutant shows severely reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
I157Y/S265N	the mutant shows about 1.5fold increased activity compared to the wild type enzyme	Peucedanum praeruptorum
L122F	the mutant shows reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
L122H	the mutant shows severely reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
L122H/W261H	the mutant shows reduced severely activity compared to the wild type enzyme	Peucedanum praeruptorum
L122H/W261H/H126F	the mutant shows severely reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
L122H/W261H/H126W	the mutant shows severely reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
L122R	inactive	Peucedanum praeruptorum
M175Y/M316W	inactive	Peucedanum praeruptorum
S265H/V315N	inactive	Peucedanum praeruptorum
S265I	the mutant shows about 2.5fold increased activity compared to the wild type enzyme	Peucedanum praeruptorum
S265N	the mutant shows about 1.9fold increased activity compared to the wild type enzyme	Peucedanum praeruptorum
V315F	the mutant shows severely reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
V320I	high-catalytic activity mutant with about 8.5fold increased activity compared to the wild type enzyme	Peucedanum praeruptorum
V320Y	the mutant shows reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
W261H	the mutant shows about 1.9fold increased activity compared to the wild type enzyme	Peucedanum praeruptorum
W261K/M316Y	inactive	Peucedanum praeruptorum
W261L	the mutant shows slightly reduced activity compared to the wild type enzyme	Peucedanum praeruptorum
Y319F	the mutant shows about 5fold increased activity compared to the wild type enzyme	Peucedanum praeruptorum
Y319R	inactive	Peucedanum praeruptorum

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin	Peucedanum praeruptorum	-	S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin	-	?
S-adenosyl-L-methionine + bergaptol	Peucedanum praeruptorum	-	S-adenosyl-L-homocysteine + bergapten	-	?

Organism

Organism	UniProt	Comment	Textmining
Peucedanum praeruptorum	A0A166U5H3	-	-

Purification (Commentary)

Purification (Comment)	Organism
glutathione S-transferase-conjugated affinity resin column chromatography	Peucedanum praeruptorum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + a 5-hydroxyfurocoumarin	-	Peucedanum praeruptorum	S-adenosyl-L-homocysteine + a 5-methoxyfurocoumarin	-	?
S-adenosyl-L-methionine + bergaptol	-	Peucedanum praeruptorum	S-adenosyl-L-homocysteine + bergapten	-	?

Subunits

Subunits	Comment	Organism
homodimer	-	Peucedanum praeruptorum

Synonyms

Synonyms	Comment	Organism
bergaptol O-methyltransferase	-	Peucedanum praeruptorum
BMT	-	Peucedanum praeruptorum