Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.9.3.1 (cytochrome oxidase)
 8,822 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Liver D-3-hydroxybutyrate dehydrogenase (OHBD) is subjected to estrogen modulation. Estrogen action was demonstrated by (a) the lesser activity of liver OHBD in female rats, as compared with their male counterparts; (b) the increase of OHBD activity after ovariectomy of sexually mature rats; (c) the decrease of OHBD activity after treatment of gonadectomized or normal rats with 17 beta-estradiol or with artificial estrogens; (d) the decrease of OHBD activity in female rats during sexual development; (e) the effects of tamoxifen on the enzyme activity. The kinetics of OHBD reaction using liver mitochondria from estrogen-treated rats showed a 50% decrease of Vmax, as compared with the control value, in contrast to the other parameters which did not vary. These results, taken together with the effect of estrogens on liver mitochondrial phospholipids, point to a decreased content of OHBD in liver mitochondria from estrogen-treated rats. In contrast to OHBD, succinate dehydrogenase and cytochrome oxidase activities, mitochondrial protein synthesis and L-malate + L-glutamate oxidation by coupled liver mitochondria either increased or were not affected by estrogens. Kidney and heart OHBD were affected by ovariectomy and estrogens like the liver enzyme, though to a lesser degree.
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PMID:Modulation of D-3-hydroxybutyrate dehydrogenase activity by estrogens. 345 87

Hydrogen sulfide (H2S) which is considered as a novel gasotransmitter after reactive oxygen species and nitric oxide in plants has dual character, that is, toxicity that inhibits cytochrome oxidase at high concentration and as signal molecule which is involved in plant growth, development, and the acquisition of tolerance to adverse environments such as extreme temperature, drought, salt, and heavy metal stress at low concentration. Therefore, H2S homeostasis is very important in plant cells. The level of H2S in plant cells is regulated by its synthetic and degradative enzymes, L-/D-cysteine desulfhydrase (L-/D-DES), sulfite reductase (SiR), and cyanoalanine synthase (CAS), which are responsible for H2S synthesis, while cysteine synthase (CS) takes charge of the degradation of H2S, but its reverse reaction also can produce H2S. Here, after crude enzyme is extracted from plant tissues, the activities of L-/D-DES, SiR, CAS, and CS are measured by spectrophotometry, the aim is to further understand homeostasis of H2S in plant cells and its potential mechanisms.
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PMID:Analysis of some enzymes activities of hydrogen sulfide metabolism in plants. 2574 84