High impact information on Alas1

• 5-Aminolevulinate synthase (ALAS) catalyzes the first step in the heme biosynthetic pathway in nonplant eukaryotes and some prokaryotes, which is the condensation of glycine with succinyl-coenzyme A to yield coenzyme A, carbon dioxide, and 5-aminolevulinate [1].
• In contrast, the heme biosynthesis genes aminolevulinic acid synthase 1 and 2 were maximally induced by estrogen at 2 and 4 h, respectively, prior to increased cell proliferation [2].
• Fluorimetric determination of hepatic delta-aminolevulinic acid synthase activity by high-performance liquid chromatography [3].
• Differential induction responses of delta-aminolevulinate synthase mRNAs during erythroid differentiation: use of nonradioactive in situ hybridization [4].
• The induction of 6-Aminolevulinic acid synthase (ALA-S) activity and the diminution in microsomal heme oxygenase (MHO) did not change when DAB fed animals were treated with AIA [5].

Associations of Alas1 with chemical compounds

• A fluorimetric method for measuring the activity of delta-aminolevulinic acid synthase (ALAS) in the liver of mice has been developed [3].

Analytical, diagnostic and therapeutic context of Alas1

• The amount of CYP1A1 and CYP1A2 mRNA, as determined by real-time PCR, was not significantly changed; mRNA encoding the housekeeping 5-aminolevulinic acid synthase was elevated 10-fold [6].

References