Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “LEVULINIC ACID”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 937 records · Page 52Linked to original sources
PubMed1980

Urinary delta-aminolevulinic acid (ALA) excretion in humans and cattle as an index of exposure to lead.

Disposable ion-exchange chromatographic columns were used to determine delta-aminolevulinic acid (ALA) concentrations in 11 bovine and 184 human urine samples. The mean urinary ALA concentrations in persons working as battery charges, autopainters, automechanics, and urban first-grade pupils were 11.61 +/- 14.23, 6.51 +/- 3.31, 6.48 +/- 3.36, and 5.71 +/- 2.91 micrograms/ml respectively. These values were higher than those found in urine from gasoline station attendants, university students and laboratory assistants, rural adult farmers, and rural first-grade pupils, which were 4.90 +/- 1.95, 4.93 +/- 1.76, 4.40 +/- 1.79 and 4.51 +/- 2.65 micrograms/ml respectively. In cattle (Holstein Friesian/White Fulani cross) the mean urinary ALA concentration was 1.84 +/- 0.04 micron/ml. The data indicates that persons working around automobile, lead batteries and leaded gasoline had elevated ALA concentrations in urine. Rural humans and cattle did not have significant elevations of urinary ALA.

Aminolevulinic Acid↗
PubMed2001

The x-ray structure of yeast 5-aminolaevulinic acid dehydratase complexed with substrate and three inhibitors.

The structures of 5-aminolaevulinic acid dehydratase (ALAD) complexed with substrate (5-aminolaevulinic acid) and three inhibitors: laevulinic acid, succinylacetone and 4-keto-5-aminolaevulinic acid, have been solved at high resolution. The ligands all bind by forming a covalent link with Lys263 at the active site. The structures define the interactions made by one of the two substrate moieties that bind to the enzyme during catalysis. All of the inhibitors induce a significant ordering of the flap covering the active site. Succinylacetone appears to be unique by inducing a number of conformational changes in loops covering the active site, which may be important for understanding the co-operative properties of ALAD enzymes. Succinylacetone is produced in large amounts by patients suffering from the hereditary disease type I tyrosinaemia and its potent inhibition of ALAD also has implications for the pathology of this disease. The most intriguing result is that obtained with 4-keto-5-amino-hexanoic acid, which seems to form a stable carbinolamine intermediate with Lys263. It appears that we have defined the structure of an intermediate of Schiff base formation that the substrate forms upon binding to the P-site of the enzyme.

Aminolevulinic Acid↗