Details

Autor(en) / Beteiligte

• Auerbach, G
• Herrmann, A
• Bracher, A
• Bader, G
• Gutlich, M
• Fischer, M
• Neukamm, M
• Garrido-Franco, M
• Richardson, J
• Nar, H
• Huber, R
• Bacher, A

Titel

Zinc Plays a Key Role in Human and Bacterial GTP Cyclohydrolase I

Ist Teil von

• Proceedings of the National Academy of Sciences - PNAS, 2000-12, Vol.97 (25), p.13567-13572

Ort / Verlag

United States: National Academy of Sciences of the United States of America

Erscheinungsjahr

2000

Link zum Volltext

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• The crystal structure of recombinant human GTP cyclohydrolase I was solved by Patterson search methods by using the coordinates of the Escherichia coli enzyme as a model. The human as well as bacterial enzyme were shown to contain an essential zinc ion coordinated to a His side chain and two thiol groups in each active site of the homodecameric enzymes that had escaped detection during earlier studies of the E. coli enzyme. The zinc ion is proposed to generate a hydroxyl nucleophile for attack of imidazole ring carbon atom eight of the substrate, GTP. It may also be involved in the hydrolytic release of formate from the intermediate, 2-amino-5-formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-triphosphate, and in the consecutive Amadori rearrangement of the ribosyl moiety.