Zinc plays a key role in human and bacterial GTP cyclohydrolase I.

Auerbach G; Herrmann A; Bracher ABader GGutlich MFischer MNeukamm MGarrido-Franco MRichardson JNar HHuber RBacher A

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Zinc plays a key role in human and bacterial GTP cyclohydrolase I.

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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.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2000年第25期|13567-13572|共6页
作者
Auerbach G; Herrmann A; Bracher ABader GGutlich MFischer MNeukamm MGarrido-Franco MRichardson JNar HHuber RBacher A;
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作者单位

Abteilung Strukturforschung, Max-Planck-Institut fur Biochemie, Am Klopferspitz 18a, D-82152 Martinsried, Germany.;

reussEngineering.com;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
GTP Cyclohydrolase; Zinc; Oligodeoxyribonucleotides; Recombinant Proteins; GTP环化水解酶; 锌;

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Zinc plays a key role in human and bacterial GTP cyclohydrolase I.

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