Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.2.1.1 (ACS)
 78,556 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Growth tests and enzyme determinations strongly suggest that the acetamidase of Aspergillus nidulans is induced by a product of acetate metabolism rather than the substrate, acetamide. The cis-dominant mutation, amdI9, which is closely linked to amdS, the structural gene for the acetamidase, results in greatly increased sensitivity to induction by acetate metabolism. Propionate, L-threonine, and ethanol also result in acetamidase induction. Mutations in the facA, facB, and facC genes, which lead to low levels of acetyl-coenzyme A synthase, are epistatic to the amdI9 mutation for strong growth on acetamide medium and abolish acetamide and propionamide induction of the acetamidase and isocitrate lyase enzymes. Acetate, L-threonine, and ethanol, however, can induce these enzymes in strains containing facA and facC lesions but not in strains containing a facB lesion. The evidence suggests that acetamidase and isocitrate lyase may be induced by a similar mechanism.
J Bacteriol 1977 Sep
PMID:Induction of the acetamidase of Aspergillus nidulans by acetate metabolism. 1 18

Formation of acetyl-CoA through acetyl-CoA synthetase (forward reaction) and through choline acyltransferase (backward reaction) was investigated in tissue extract from the electric organ of Torpedo marmorata. When the tissue extract was submitted to gel filtration on Sephadex G-25, the formation of acetyl-CoA by acetyl-CoA synthetase appeared fully dependent on ATP and CoA and partially dependent on acetate (an endogenous supply of acetate is discussed). Choline acetyltransferase was a potent source of acetyl-CoA, only requiring acetylcholine and CoA, and was much more efficient than acetyl-CoA synthetase for concentrations of acetylcholine likely to be present in nerve endings.
Biochem J 1977 Sep 15
PMID:Biosynthesis of acetyl-coenzyme A in the electric organ of Torpedo marmorata in relation to acetylcholine metabolism. 2 1

A comparative study of the effects of varying levels of oxygen on some of the metabolic functions of the primitive eukaryote, Saccharomyces cerevisiae, has shown that these cells are responsive to very low levels of oxygen: the level of palmitoyl-Co A desaturase was greatly enhanced by only 0.03% (v/v) oxygen. Similarly, an acetyl-CoA synthetase associated predominantly with anaerobic growth, was stimulated by as little as 0.1% oxygen, while an isoenzyme correlated with aerobic growth, was maximally active at much higher oxygen levels (greater than 1%). Closely following this latter pattern were three mitochondrial enzymes that attained maximal activity only under atmospheric levels of oxygen.
Orig Life 1979 Sep
PMID:Oxygen as a factor in eukaryote evolution: some effects of low levels of oxygen on Saccharomyces cerevisiae. 4 Dec 5

In the interests of uniformly high radiological physics standards at ACS-NCI Breast Cancer Detection Demonstration Projects, measurements were made at 29 breast cancer screening clinics. These measurements were made throughout the country with equipment calibrated with standards traceable to National Bureau of Standards. Histograms which indicate the frequency distribution of exposures to the surface of a 6 cm breast for various machine/receptor combinations were prepared.
AJR Am J Roentgenol 1976 Sep
PMID:Interim report: mammographic exposures at the breast cancer detection demonstration project screening centers. 18 50

Sixty-four consecutive patients with coronary artery disease who had resections of left ventricular scars during 1969 to 1973 were retrospectively identified. Extent of angiographic coronary artery disease was scored by the jeopardy score system. Size of the abnormally contracting segment (akinetic or dyskinetic in all) was measured as a percent of the end-diastolic ventriculographic perimeter (% ACS). Contractility of the non-ACS was expressed as the difference between the actual ejection fraction and that predicted by the spherical model of Feild and Dowling (excess ejection fraction, XEF.) Perioperative survival correlated with jeopardy score (21 of 27, jeopardy score less than or equal to 6; 19 of 37 jeopardy score greater than 6) and with XEF (30 OF 38, XEF greater than +0.10; 10 of 26, XEF less than or equal to "0.10). When XEF and jeopardy score were combined, the patients were separated into four subgroups with perioperative survival ranging from 89% to 33%. Long-term survival (minimum follow-up period 30 months) in the 40 perioperative survivors also correlated with jeopardy score (95% at 54 mo for jeopardy score less than or equal to 6; 49% for jeopardy score greater than 6). Survival was unrelated to whether or not aortocoronary bypass graft procedures had been done. It is concluded that survival following aneurysmectomy is predicted by two preoperative angiographic variables--the extent of coronary artery disease and the contractility of the non-aneurysmal portion of the left ventricle.
Circulation 1977 Sep
PMID:Angiographic predictors of survival following left ventricular aneurysmectomy. 88 15

The benzoyl-CoA ligase from an anaerobic syntrophic culture was purified to homogeneity. It had a molecular mass of around 420 kDa and consisted of seven or eight subunits of 58 kDa. The temperature optimum was 37-40 degrees C, the optimum pH around 8.0 and optimal activity required 50-100 mM TRIS-HCl buffer, pH 8.0 and 3-7 mM MgCl2; MgCl2 in excess of 10 mM was inhibitory. The activation energy for benzoate was 11.3 kcal/mol. Although growth occurred only with benzoate as a carbon source, the benzoyl-coenzyme A (CoA) ligase formed benzoyl-CoA esters with benzoate, 2-, 3- and 4-fluorobenzoate, picolinate, nicotinate and isonicotinate. Acetate was activated to acetyl-CoA by an acetyl-CoA synthetase. The Km values for benzoate, 2-, 3- and 4-fluorobenzoate were 0.04, 0.28, 1.48 and 0.32 mM, the Vmax values 1.05, 1.0, 0.7 and 0.98 units (U)/mg, respectively. For reduced CoA (CoA-SH) a Km of 0.07 mM and a Vmax of 1.05 U/mg and for ATP a Km of 0.16 mM and a Vmax of 1.08 U/mg was determined. Benzoate activation was inhibited by more than 6 mM ATP, presumably by pyrophosphate generation from ATP. The inhibition constant (Ki) for pyrophosphate was 5.7 mM. No homology of the N-terminal amino acid sequence with that of a 2-aminobenzoyl-CoA ligase of a denitrifying Pseudomonas sp. was found.
Appl Microbiol Biotechnol 1992 Sep
PMID:Purification and characterization of benzoyl-CoA ligase from a syntrophic, benzoate-degrading, anaerobic mixed culture. 136 92

The success of the Pap smear in screening for cervical cancer illustrates many of the tenets of screening for disease. Unfortunately, no other gynecologic malignancy shares this success. Detection of most gynecologic malignancies occurs once they have become symptomatic and on clinical examination at the interval cancer-related checkup as recommended by the ACS. These examinations, done yearly in women older than 40 and every 3 years in younger women, can go a long way in the detection of genital tract disease. In detecting vulvar neoplasms, visual inspection of the entire perineum coupled with palpation to include Bartholin's glands and early biopsy of suspicious vulvar lesions promotes earlier diagnosis. Self-examination similar to breast self-examination and increased patient awareness are potential education goals for physicians as well as cancer and medical societies. Vaginal examination at the cancer checkup should continue. The finding that most vaginal cancers are picked up by abnormal cytology while they are still asymptomatic argues strongly for Pap testing after menopause. The knowledge that women who are status posthysterectomy for benign disease are not protected from developing vaginal cancers mandates continued Pap testing in this population as well. Because endometrial cancer is common, primary care physicians should maintain a high index of suspicion. Aspiration biopsy is a simple office-based procedure with low risk and good yield, and any woman in the perimenopausal and postmenopausal period who presents with atypical bleeding patterns should be evaluated. Although not recommended as a general screening test, the ACS does advocate endometrial sampling in the high risk woman at the time of menopause. The greatest challenge to primary care physicians may be the early detection of ovarian cancer. No single test is available, nor is any advocated in screening for this lethal disease. Currently, only periodic physical examination is recommended at the cancer checkup interval. Ultrasound, both transabdominal and transvaginal, may help in detecting adnexal masses, but is not sensitive enough to differentiate benign from malignant lesions. In this setting, and in the patient with suspected ovarian cancer, CA 125 and AFP may be helpful in determining which patients require surgical exploration. Women with positive family histories for ovarian cancer require greater vigilance and close follow-up with serial ultrasound and CA 125 determinations. As the population ages, cancer, which is primarily a disease of age, will continue to increase in incidence.(ABSTRACT TRUNCATED AT 400 WORDS)
Prim Care 1992 Sep
PMID:Screening for gynecologic cancer. Vulvar, vaginal, endometrial, and ovarian neoplasms. 141 66

The ACS RX flow support catheter, which functions as a temporary stent, was placed successfully during four procedures in three patients who had suboptimal results following angioplasty. This investigational device allowed prolonged perfusion and supported the vessel wall when coronary blood flow was compromised, avoiding emergent coronary artery bypass graft surgery during two procedures. In the remaining procedures the device was used as a bridge to surgery. These early applications of the flow support catheter following failed balloon angioplasty suggest a rapid, effective alternative to the autoperfusion balloon when it fails or is contraindicated because of the lesion location.
Cathet Cardiovasc Diagn 1992 Sep
PMID:ACS RX flow support catheter as a temporary stent for dissection or occlusion during balloon angioplasty: initial experience. 152 14

Carnitine acetyltransferase was isolated from yeast Saccharomyces cerevisiae with an apparent molecular weight of 400,000. The enzyme contains identical subunits of 65,000 Da. The Km values of the isolated enzyme for acetyl-CoA and for carnitine were 17.7 microM and 180 microM, respectively. Carnitine acetyltransferase is an inducible enzyme, a 15-fold increase in the enzyme activity was found when the cells were grown on glycerol instead of glucose. Carnitine acetyltransferase, similarly to citrate synthase, has a double localization (approx. 80% of the enzyme is mitochondrial), while acetyl-CoA synthetase was found only in the cytosol. In the mitochondria carnitine acetyltransferase is located in the matrix space. The incorporation of 14C into CO2 and in lipids showed a similar ratio, 2.9 and 2.6, when the substrate was [1-14C]acetate and [1-14C]acetylcarnitine, respectively. Based on these results carnitine acetyltransferase can be considered as an enzyme necessary for acetate metabolism by transporting the activated acetyl group from the cytosol into the mitochondrial matrix.
Biochim Biophys Acta 1991 Sep 11
PMID:Isolation and characterization of carnitine acetyltransferase from S. cerevisiae. 189 91

We describe a new clinical laboratory instrument, the ACS:180, used to automate heterogeneous immunoassay testing. The ACS:180 automates immunoassays in which paramagnetic particles are the solid phase and changes in chemiluminescence are measured. The system can accommodate both competitive and sandwich-type assay configurations. The microprocessor-based instrument fully automates each step of the assay, including sample and reagent addition, separation and wash of paramagnetic particles, and generation and acquisition of the chemiluminescent signal. The instrument has the flexibility to operate in random-access or batch mode. The time from application of sample to first result is less than 15 min; throughput is as much as 180 tests per hour.
Clin Chem 1990 Sep
PMID:The Ciba Corning ACS:180 benchtop immunoassay analyzer. 220 99


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