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Isodtrate dehydrogenase Phosphorylation

Interconversion processes (see p. 120) also play an important role. They are shown here in detail using the example of the PDH complex (see p. 134). The inactivating protein kinase [la] is inhibited by the substrate pyruvate and is activated by the products acetyl-CoA and NADH+H. The protein phosphatase [Ibj—like isodtrate dehydrogenase [3] and the ODH complex [4j-is activated by Ca. This is particularly important during muscle contraction, when large amounts of ATP are needed. Insulin also activates the PDH complex (through inhibition of phosphorylation) and thereby promotes the breakdown of glucose and its conversion into fatty acids. [Pg.144]

Phosphorylation in bacteria. A bacterial enzyme whose activity is controlled by phosphorylation is isodtrate dehydrogenase. Transfer of a phospho group to the -OF4 of Ser 113 completely inactivates the... [Pg.545]


See other pages where Isodtrate dehydrogenase Phosphorylation is mentioned: [Pg.125]    [Pg.103]    [Pg.125]    [Pg.125]    [Pg.19]    [Pg.19]    [Pg.355]   
See also in sourсe #XX -- [ Pg.103 ]

See also in sourсe #XX -- [ Pg.545 ]




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