Literature summary for 2.1.1.137 extracted from

Marapakala, K.; Packianathan, C.; Ajees, A.A.; Dheeman, D.S.; Sankaran, B.; Kandavelu, P.; Rosen, B.P.
A disulfide-bond cascade mechanism for arsenic(III) S-adenosylmethionine methyltransferase (2015), Acta Crystallogr. Sect. D, 71, 505-515 .

Search for more literature for 2.1.1.137

Cloned(Commentary)

Cloned (Comment)	Organism
expression of a mutant lacking 31 residues from the N-terminus and 28 residues from the C-terminus	Cyanidioschyzon sp. 5508

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure with the bound aromatic arsenicals phenylarsenite at 1.80 A resolution and reduced roxarsone at 2.25 A resolution. Compounds are bound to conserved residues C174 and C224. A loop containing Cys44 and Cys72 shifts by nearly 6.5 A in the arsenic(III)-bound structures compared with the SAM-bound structure	Cyanidioschyzon sp. 5508

Protein Variants

Protein Variants	Comment	Organism
C44A	mutant is unable to methylate arsenic(III) but retains the ability to methylate methylarsenate	Cyanidioschyzon sp. 5508
C44A/C72A	mutant is unable to methylate arsenic(III) but retains the ability to methylate methylarsenate	Cyanidioschyzon sp. 5508

Organism

Organism	UniProt	Comment	Textmining
Cyanidioschyzon sp. 5508	C0JV69	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
S-adenosyl-L-methionine + arsenite	-	Cyanidioschyzon sp. 5508	S-adenosyl-L-homocysteine + methylarsenate(III)	-	?
S-adenosyl-L-methionine + phenylarsenite	-	Cyanidioschyzon sp. 5508	S-adenosyl-L-homocysteine + phenylmethylarsenate(III)	-	?

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)