Studies of the phosphorylation of Escherichia coli isocitrate dehydrogenase. Recognition of the enzyme by isocitrate dehydrogenase kinase/phosphatase and effects of phosphorylation on its structure and properties.
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Crystal structure of Bacillus subtilis isocitrate dehydrogenase at 1.55 A. Insights into the nature of substrate specificity exhibited by Escherichia coli isocitrate dehydrogenase kinase/phosphataseStructural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK.Dimerization and bifunctionality confer robustness to the isocitrate dehydrogenase regulatory system in Escherichia coliPurification, crystallization and preliminary X-ray analysis of bifunctional isocitrate dehydrogenase kinase/phosphatase in complex with its substrate, isocitrate dehydrogenase, from Escherichia coli.A novel protein kinase that controls carbon catabolite repression in bacteria.
P2860
Studies of the phosphorylation of Escherichia coli isocitrate dehydrogenase. Recognition of the enzyme by isocitrate dehydrogenase kinase/phosphatase and effects of phosphorylation on its structure and properties.
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1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
Studies of the phosphorylation ...... its structure and properties.
@en
Studies of the phosphorylation ...... its structure and properties.
@nl
type
label
Studies of the phosphorylation ...... its structure and properties.
@en
Studies of the phosphorylation ...... its structure and properties.
@nl
prefLabel
Studies of the phosphorylation ...... its structure and properties.
@en
Studies of the phosphorylation ...... its structure and properties.
@nl
P1433
P1476
Studies of the phosphorylation ...... its structure and properties.
@en
P2093
P304
P356
10.1016/0300-9084(89)90111-9
P577
1989-09-01T00:00:00Z