Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:1.3.5.1 (
succinate dehydrogenase
)
8,177
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
In adult rats, a significant portion of brain ethanolamine glycerophospholipids are synthesized by a pathway involving
phosphatidylserine decarboxylase
, a mitochondrial enzyme. We have now examined whether this enzyme plays a particularly prominent role during development. Activities for both
phosphatidylserine decarboxylase
and
succinate dehydrogenase
(another mitochondrial enzyme) were determined in brain homogenates from rats 5 days of age to adulthood. Succinate dehydrogenase activity, expressed on a per unit brain protein basis, increased markedly during development. This pattern has been reported previously and is as expected from the postnatal increase in oxidative metabolism. In contrast,
phosphatidylserine decarboxylase
activity decreased 40% from 5 to 30 days of age. The apparent Km for brain
phosphatidylserine decarboxylase
was 85 microM in both young (8- and 20-day-old) and adult animals. Parallel studies in vivo were carried out to determine the contribution of the
phosphatidylserine decarboxylase
pathway, relative to pathways utilizing ethanolamine directly, to the synthesis of brain ethanolamine glycerophospholipids. Animals were injected intracranially with a mixture of L-[G-3H]serine and [2-14C]ethanolamine and incorporation into the base moieties of the phospholipids determined. The 3H/14C ratio of ethanolamine glycerophospholipids decreased about 50% during development. Our studies in vitro and in vivo both suggest that
phosphatidylserine decarboxylase
plays a significant role in the synthesis of brain ethanolamine glycerophospholipids at all ages, although it is relatively more prominent early in development.
...
PMID:Developmental pattern for phosphatidylserine decarboxylase in rat brain. 308 85
It is shown that the trypsin-treatment of rat liver mitochondria, depleted of the outer membrane, causes a strong inactivation of
phosphatidylserine decarboxylase
. This inactivation is dependent on trypsin concentration and the time of digestion in a similar manner as the inactivation of cytochrome oxidase. Under these conditions only a moderate inactivation of
succinate dehydrogenase
is observed. Phosphatidylserine decarboxylase is thus localized in the outer leaflet of the inner mitochondria membrane or, at least, is accessible from the outer surface of the inner membrane.
...
PMID:Phosphatidylserine decarboxylase is located on the external side of the inner mitochondrial membrane. 686 14