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: UMLS:C0344329 (
collapse
)
28,634
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Two deaths occurred after ingestion of cyanide-containing Extra-Strength
Excedrin
capsules. Cranial CT scans obtained within 3 hr of each patient's
collapse
showed diffuse cerebral swelling and loss of gray-white differentiation. Most diffuse cerebral insults (hypoxia, ischemia) do not show such changes so soon after injury. The early onset of diffuse cerebral edema with loss of gray-white differentiation may be a clue to the diagnosis of acute cyanide poisoning.
...
PMID:CT diagnosis of toxic brain injury in cyanide poisoning: considerations for forensic medicine. 312 May 33
Carbamoyl phosphate synthetase (CPS) plays a key role in both arginine and pyrimidine biosynthesis by catalyzing the production of carbamoyl phosphate. The enzyme from Escherichi coli consists of two polypeptide chains referred to as the small and large subunits. On the basis of both amino acid sequence analyses and X-ray structural studies, it is known that the small subunit belongs to the
Triad
or Type I class of amidotransferases, all of which contain a cysteine-histidine (Cys269 and His353) couple required for activity. The hydrolysis of glutamine by the small subunit has been proposed to occur via two tetrahedral intermediates and a glutamyl-thioester moiety. Here, we describe the three-dimensional structures of the C269S/glutamine and CPS/glutamate gamma-semialdehyde complexes, which serve as mimics for the Michaelis complex and the tetrahedral intermediates, respectively. In conjunction with the previously solved glutamyl-thioester intermediate complex, the stereochemical course of glutamine hydrolysis in CPS has been outlined. Specifically, attack by the thiolate of Cys269 occurs at the Si face of the carboxamide group of the glutamine substrate leading to a tetrahedral intermediate with an S-configuration. Both the backbone amide groups of Gly241 and Leu270, and O(gamma) of Ser47 play key roles in stabilizing the developing oxyanion.
Collapse
of the tetrahedral intermediate leads to formation of the glutamyl-thioester intermediate, which is subsequently attacked at the Si face by an activated water molecule positioned near His353. The results described here serve as a paradigm for other members of the
Triad
class of amidotranferases.
...
PMID:The small subunit of carbamoyl phosphate synthetase: snapshots along the reaction pathway. 1058 38