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:3.4.21.64 (
proteinase K
)
4,071
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Human
monoamine oxidase A
that had been synthesized in a reticulocyte lysate translation system was capable of binding to and inserting into either rat liver mitochondria or isolated mitochondrial outer membranes. The inserted form was as resistant to
proteinase K
as endogenous mitochondrial
monoamine oxidase A
. The insertion, but not the binding, of
monoamine oxidase A
was prevented by depleting the reaction mixture of either ATP (with apyrase) or ubiquitin (with purified antibodies against this polypeptide). Addition of ATP or ubiquitin, respectively, to these depleted mixtures restored the insertion of the enzyme. In the absence of mitochondria, in vitro synthesized
monoamine oxidase A
did not catalyze its own alkylation by the mechanism-based inhibitor, [3H]clorgyline. However, both
monoamine oxidase A
that had been membrane-inserted in vitro and
monoamine oxidase A
that had been bound to the mitochondria under conditions of ATP depletion catalyzed adduct formation. Furthermore, reaction of either clorgyline or another mechanism-based inhibitor, pargyline, with the membrane-bound enzyme during ATP depletion inhibited the insertion of
monoamine oxidase A
when ATP was restored. These observations indicate that
monoamine oxidase A
acquired a catalytically active conformation on interaction with the mitochondrial outer membranes prior to its ATP and ubiquitin-dependent insertion into the membrane.
...
PMID:The insertion of monoamine oxidase A into the outer membrane of rat liver mitochondria. 130 56
Geranylgeranoic acid (GGA), a 20-carbon acyclic polyprenoic acid (all-trans 3,7,11,15-tetramethyl- 2,4,6,10,14-hexadecatetraenoic acid) and its derivatives were developed as synthetic "acyclic retinoids" for cancer chemoprevention. Previously, we have shown the natural occurrence of GGA in various medicinal herbs and reported enzymatic formation of GGA from geranylgeraniol (GGOH) through geranylgeranial (GGal) by rat liver homogenates. Here, we present several lines of evidence that a putative GGOH oxidase is involved in GGA synthesis by human hepatoma cell lysates. First, conversion of GGOH to GGal did not require exogenous NAD(+), whereas the conversion from GGal to GGA absolutely required additional NAD(+). Second, GGal synthesis from GGOH was coupled with consumption of oxygen from the reaction mixture. Third, GGOH-dependent GGal synthesis activity was
proteinase K
-resistant and even enhanced by
proteinase K
treatment; GGOH oxidase activity was enriched in the mitochondrial fraction. Finally, recombinant human monoamine oxidase (MAO)-B, but not
MAO-A
catalyzed oxidation of GGOH to GGal. These data suggest that a putative mitochondrial GGOH oxidase is involved in the initial step of GGA synthesis from GGOH.
...
PMID:Geranylgeraniol oxidase activity involved in oxidative formation of geranylgeranoic acid in human hepatoma cells. 2236 82
