1C3U

T. MARITIMA ADENYLOSUCCINATE LYASE

Summary for 1C3U

• Entry DOI: 10.2210/pdb1c3u/pdb
• Related: 1C3C
• Descriptor: ADENYLOSUCCINATE LYASE, SULFATE ION (3 entities in total)
• Functional Keywords: purine biosynthesis, lyase
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 100280.53

Authors

Toth, E.A.,Yeates, T.O. (deposition date: 1999-07-28, release date: 2000-03-08, Last modification date: 2024-02-07)

Primary citation

Toth, E.A.,Yeates, T.O.
The structure of adenylosuccinate lyase, an enzyme with dual activity in the de novo purine biosynthetic pathway.
Structure Fold.Des., 8:163-174, 2000

PubMed Abstract: Adenylosuccinate lyase is an enzyme that plays a critical role in both cellular replication and metabolism via its action in the de novo purine biosynthetic pathway. Adenylosuccinate lyase is the only enzyme in this pathway to catalyze two separate reactions, enabling it to participate in the addition of a nitrogen at two different positions in adenosine monophosphate. Both reactions catalyzed by adenylosuccinate lyase involve the beta-elimination of fumarate. Enzymes that catalyze this type of reaction belong to a superfamily, the members of which are homotetramers. Because adenylosuccinate lyase plays an integral part in maintaining proper cellular metabolism, mutations in the human enzyme can have severe clinical consequences, including mental retardation with autistic features.

PubMed: 10673438
DOI: 10.1016/S0969-2126(00)00092-7

Experimental method

X-RAY DIFFRACTION (2.3 Å)