PMID:7663943: Difference between revisions
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''' | '''Nar, H, Huber, R, Meining, W, Schmid, C, Weinkauf, S and Bacher, A''' (1995) Atomic structure of GTP cyclohydrolase I. ''Structure'' '''3''':459-66 | ||
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!align=left |Abstract | !align=left |Abstract | ||
Latest revision as of 04:51, 15 September 2013
| Citation |
Nar, H, Huber, R, Meining, W, Schmid, C, Weinkauf, S and Bacher, A (1995) Atomic structure of GTP cyclohydrolase I. Structure 3:459-66 |
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| Abstract |
Tetrahydrobiopterin serves as the cofactor for enzymes involved in neurotransmitter biosynthesis and as regulatory factor in immune cell proliferation and the biosynthesis of melanin. The biosynthetic pathway to tetrahydrobiopterin consists of three steps starting from GTP. The initial reaction is catalyzed by GTP cyclohdrolase I (GTP-CH-I) and involves the chemically complex transformation of the purine into the pterin ring system. |
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| Keywords |
Alcohol Oxidoreductases/chemistry; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Binding Sites; Biopterin/analogs & derivatives; Biopterin/biosynthesis; Catalysis; Crystallography, X-Ray; Escherichia coli/enzymology; GTP Cyclohydrolase/chemistry; GTP Cyclohydrolase/metabolism; Guanosine Triphosphate/metabolism; Models, Molecular; Neopterin/analogs & derivatives; Phosphorus-Oxygen Lyases; Protein Conformation; Pteridines/metabolism |
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