about
Arsenic binding and transfer by the ArsD As(III) metallochaperonePathway of human AS3MT arsenic methylation.Identification of catalytic residues in the As(III) S-adenosylmethionine methyltransferase.Biochemical evidence for interaction between the two nucleotide binding domains of ArsA. Insights from mutants and ATP analogs.Nonequivalence of the nucleotide binding domains of the ArsA ATPase.
P2860
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Unisite and multisite catalysis in the ArsA ATPase.
@en
Unisite and multisite catalysis in the ArsA ATPase.
@nl
type
label
Unisite and multisite catalysis in the ArsA ATPase.
@en
Unisite and multisite catalysis in the ArsA ATPase.
@nl
prefLabel
Unisite and multisite catalysis in the ArsA ATPase.
@en
Unisite and multisite catalysis in the ArsA ATPase.
@nl
P2860
P356
P1476
Unisite and multisite catalysis in the ArsA ATPase
@en
P2093
P2860
P304
23815-23820
P356
10.1074/JBC.M203432200
P407
P577
2002-04-18T00:00:00Z