Mount Sinai Team Maps the AASS Enzyme in Full, Offering New Clues for Treating the Rare Genetic Disease Glutaric Aciduria Type 1
Researchers at the Icahn School of Medicine at Mount Sinai announced on November 13 that they have produced the first detailed, complete structure of the human AASS enzyme, which breaks down the amino acid lysine. The work, published in the November 13 online issue of Science Advances, combined cryo-electron microscopy, biochemical experiments and computer simulations.
The team identified a flexible, hinge-like regulatory region of the enzyme where small changes can substantially alter its activity. The finding matters for glutaric aciduria type 1 (GA1), an inherited metabolic disorder in which toxic substances build up in the body and can cause irreversible brain damage. Understanding how AASS is built and regulated gives drug designers a starting point for molecules that could adjust its activity.
The researchers stress that this is an early, laboratory-stage step, not a treatment or a cure; the next step is designing inhibitor molecules. The study was supported by the National Institutes of Health, and its senior and co-corresponding authors include Michael B. Lazarus, Sander M. Houten and Robert J. DeVita. (Source: Mount Sinai)
Source: Mount Sinai
Published by GSM · USA (original Chinese edition)
Photo: 图片来源：Wikimedia Commons「Mount Sinai Hospital (55494328982).jpg」（Ajay Suresh 摄，CC BY 4.0），图中为位于纽约的西奈山医院建筑群 Image: Wikimedia Commons "Mount Sinai Hospital (55494328982).jpg" (by Ajay Suresh, CC BY 4.0), The Mount Sinai Hospital complex in New York
