Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.3.5.5 (CPS)
 1,262 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The mechanism of the reaction catalyzed by rat liver mitochondrial carbamoyl-phosphate synthetase has been studied by using [beta-18O2]ATP and HC18O-3, monitoring the isotopic composition of adenosine triphosphate (ATP) and inorganic phosphate (Pi) by high-resolution 31P NMR spectroscopy. In the presence of both HCO3- and acetylglutamate, the enzyme catalyzes the exchange of oxygen atoms between the beta, gamma bridging and the beta nonbridging positions of ATP. Addition of NH3 stops the exchange, Pi released by the ATPase activity of the enzyme in the absence of NH3 contains one oxygen atom from HC18O3- but there is no incorporation of 18O into ATP. There is no significant incorporation of [14C]ADP or 32Pi into ATP. It is concluded that in the enzyme-ATPA.HCO30.ATPB complex formed in the presence of ATP and HCO3- there is reversible transfer of the gamma-PO3 group of ATPA (the molecule that yields Pi) to HCO3- without dissociation of products. The beta-PO3 of the enzyme-bound ADP that is formed can rotate. Virtually all of the complex appears to be in the form in which ATPA is cleaved, but in the absence of NH3, ATP is reconstituted and dissociates from the complex on at least 75% of the occasions. On the remainder, the carbonyl phosphate is cleaved in an irreversible process that yields Pi and a low-energy form of carbonic acid (probably HCO3-). NH3 reacts rapidly and irreversibly with the complex, and at saturation the rate (greater than 10 times the rate of Pi release in the absence of NH3) is sufficient to prevent dissociation of ATPA. In the absence of HCO3- an enzyme-ATPA.ATPB complex is formed, but cleavage of the bond between beta, gamma bridging oxygen and P gamma of ATPA does not occur.
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PMID:Mechanism of activation of bicarbonate ion by mitochondrial carbamoyl-phosphate synthetase: formation of enzyme-bound adenosine diphosphate from the adenosine triphosphate that yields inorganic phosphate. 626 8

The purpose of this study was to evaluate the effects of disinfectants on the bond strength of resin to dentine. The surface of bovine dentine was exposed to formaldehyde (FA) aqueous solutions, glutaraldehyde (GA) aqueous solutions, 2-hydroxyethyl methacrylate aqueous solutions (HEMA), a commercially available dentine primer (Gluma CPS desensitizer, GLUMA), isotonic sodium chloride solution (IS), and distilled water (DW), and placed in a humidor (HU) at 37 degrees C, or non-stored (baseline). All dentine surfaces were conditioned with a 10% citric acid and 3% ferric chloride solution (10-3 liquid), and then bonded to an acrylic rod with a self-curing adhesive resin (Super-Bond C&B). The mean tensile bond strengths determined 24 h after bonding were compared by analysis of variance (ANOVA) and Fisher's protected LSD test (n=5, P < or = 0.05). The exposure of dentine to IS, DW and HU for both 48 and 168 h resulted in a decrease in bond strength when compared with the baseline. The highest bond strengths after 168 h of exposure were obtained with 5% GA, 10% HEMA, and GLUMA, the values of which were equivalent to baseline and were significantly higher than that of FA. It is concluded that disinfectant pre-treatment with 5% GA or GLUMA stabilizes the bonding of tri-n-butylborane (TBB) initiated luting agent to bovine dentine conditioned with 10-3 liquid.
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PMID:Effect of disinfectants containing glutaraldehyde on bonding of a tri-n-butylborane initiated resin to dentine. 1202 97