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  Location of the active site and proposed catalytic mechanism of pterin-4a-carbinolamine dehydratase

Köster, S., Stier, G., Ficner, R., Hölzer, M., Curtius, H., Suck, D., et al. (1996). Location of the active site and proposed catalytic mechanism of pterin-4a-carbinolamine dehydratase. European Journal of Biochemistry, 241(3), 858-864. doi:10.1111/j.1432-1033.1996.00858.x.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-A681-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-AC2C-9
Genre: Journal Article

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EurJBiochem_241_1996_858.pdf (Any fulltext), 2MB
 
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 Creators:
Köster, Sandra, Author
Stier, Gunter1, Author              
Ficner, Ralf, Author
Hölzer, Manuela, Author
Curtius, Hans−Christoph, Author
Suck, Dietrich, Author
Ghisla, Sandro, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: hepatocyte nuclear factor-1α-dimerization cofactor; dehydratase; tetrahydrobiopterin; phenyl-alanine hydroxylase
 Abstract: Based on the recently solved three-dimensional structure of pterin-4a-carbinolamine dehydratase from rat/human liver the involvement of the proposed active-site residues Glu57, Asp60, His61, His62, Tyr69, His79, Arg87 and Asp88 was examined by site-directed mutagenesis. Most of the mutants showed reduced activity, and only the Glu57→Ala mutant and the His61→Ala, His62→Ala double mutant were fully devoid of activity. The dissociation constants of quinonoid 6,6-dimethyl-7,8-dihydropterin were significantly increased for binding to the Glu57→Ala, His61→Ala, His62→Ala single mutants and the His61→Ala, His62→Ala double mutant, confirming that His61 and His62 are essential for substrate binding and catalysis. The mechanism of dehydration is proposed to involve base catalysis at the N(5)-H group of the substrate by His61.

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Language(s): eng - English
 Dates: 1996-07-031996-09-062004-07-231996-11-01
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 664794
DOI: 10.1111/j.1432-1033.1996.00858.x
Other: 7343
 Degree: -

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Title: European Journal of Biochemistry
Source Genre: Journal
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Publ. Info: Berlin : Published by Springer-Verlag on behalf of the Federation of European Biochemical Societies
Pages: - Volume / Issue: 241 (3) Sequence Number: - Start / End Page: 858 - 864 Identifier: ISSN: 0014-2956
CoNE: https://pure.mpg.de/cone/journals/resource/111097776606040