On the structure and linkage of the covalent cofactor of methylamine dehydrogenase from the methylotrophic bacterium W3A1 |
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| Authors: | W S McIntire J T Stults |
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| Institution: | 1. Veterans Administration Medical Center, Molecular Biology Division (151-S), San Francisco, CA 94121, USA;2. Michigan State University, Department of Biochemistry , East Lansing, MI 48824, USA;1. Federal Research Center of Problems of Chemical Physics and Medicinal Chemistry, Russian Academy of Sciences, 142432 Chernogolovka, Moscow Region, Russian Federation;2. A. N. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, 119334 Moscow, Russian Federation;3. Department of Fundamental Physical and Chemical Engineering, M. V. Lomonosov Moscow State University, 119991 Moscow, Russian Federation;4. Moscow Region State Pedagogical University, 141014 Mytishi, Moscow Region, Russian Federation;5. Zhengzhou Research Institute, Harbin Institute of Technology, Jinshui District, 450003 Zhengzhou, China;1. A. N. Frumkin Institute of Physical Chemistry and Electrochemistry, Russian Academy of Sciences, 119071 Moscow, Russian Federation;2. N. S. Kurnakov Institute of General and Inorganic Chemistry, Russian Academy of Sciences, 119991 Moscow, Russian Federation;1. Institute of Chemistry, St. Petersburg State University, 198504 St. Petersburg, Russian Federation;2. Medicinal Chemistry Center, Togliatti State University, 445020 Togliatti, Russian Federation |
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| Abstract: | Short amino acid sequences around the two linkage sites of the cofactor of methylamine dehydrogenase are presented. Mass spectral data indicates that the covalently bound cofactor is the tricyclic pyrroloquinoline quinone (PQQ). However, the 3 carboxyl groups characteristic of this o-quinone are absent. A cysteine thioether, via a methylene bridge, and a serine ether link the cofactor to the small subunit of methylamine dehydrogenase. |
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