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Pregled bibliografske jedinice broj: 997340

Interconversion of (S)-glutamate and (2S, 3S)-3-methylaspartate: A distinctive B-12-dependent carbon-skeleton rearrangement


Wetmore, Stacey D.; Smith, David M.; Golding, Bernard T.; Radom, Leo
Interconversion of (S)-glutamate and (2S, 3S)-3-methylaspartate: A distinctive B-12-dependent carbon-skeleton rearrangement // Journal of the American Chemical Society, 123 (2001), 33; 7963-7972 doi:10.1021/ja004246f (međunarodna recenzija, članak, znanstveni)


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Naslov
Interconversion of (S)-glutamate and (2S, 3S)-3-methylaspartate: A distinctive B-12-dependent carbon-skeleton rearrangement

Autori
Wetmore, Stacey D. ; Smith, David M. ; Golding, Bernard T. ; Radom, Leo

Izvornik
Journal of the American Chemical Society (0002-7863) 123 (2001), 33; 7963-7972

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
METHYLMALONYL-COA MUTASE ; DEPENDENT GLUTAMATE MUTASE ; SYNTHETIC BILAYER-MEMBRANE ; ELECTRON-PARAMAGNETIC-RESONANCE ; PARTIAL PROTON-TRANSFER ; CLOSTRIDIUM-COCHLEARIUM ; HYDROPHOBIC VITAMIN-B12 ; 2-METHYLENEGLUTARATE MUTASE ; CRYPTIC STEREOSPECIFICITY ; ESCHERICHIA-COLI

Sažetak
The interconversion of (S)-glutamate and (2S, 3S)-3-methylaspartate catalyzed by B-12-dependent glutamate mutase is discussed using results from high-level ab initio molecular orbital calculations. Evidence is presented regarding the possible role of coenzyme-B-12 in substrate activation and product formation via radical generation. Calculated electron paramagnetic resonance parameters support experimental evidence for the involvement of substrate-derived radicals and will hopefully aid the future detection of other important radical intermediates. The height of the rearrangement barrier for a fragmentation-recombination pathway, calculated with a model that includes neutral amino and carboxylic acid substituents in the migrating glycyl group, supports recent experimental evidence for the interconversion of (S)-glutamate and (2S, 3S)-3-methylaspartate through such a pathway. Our calculations suggest that the enzyme may facilitate the rearrangement of (S)-glutamate through (partial) proton-transfer processes that control the protonation state of substituents in the migrating group.

Izvorni jezik
Engleski

Znanstvena područja
Kemija



POVEZANOST RADA


Profili:

Avatar Url David Matthew Smith (autor)

Citiraj ovu publikaciju

Wetmore, Stacey D.; Smith, David M.; Golding, Bernard T.; Radom, Leo
Interconversion of (S)-glutamate and (2S, 3S)-3-methylaspartate: A distinctive B-12-dependent carbon-skeleton rearrangement // Journal of the American Chemical Society, 123 (2001), 33; 7963-7972 doi:10.1021/ja004246f (međunarodna recenzija, članak, znanstveni)
Wetmore, S., Smith, D., Golding, B. & Radom, L. (2001) Interconversion of (S)-glutamate and (2S, 3S)-3-methylaspartate: A distinctive B-12-dependent carbon-skeleton rearrangement. Journal of the American Chemical Society, 123 (33), 7963-7972 doi:10.1021/ja004246f.
@article{article, year = {2001}, pages = {7963-7972}, DOI = {10.1021/ja004246f}, keywords = {METHYLMALONYL-COA MUTASE, DEPENDENT GLUTAMATE MUTASE, SYNTHETIC BILAYER-MEMBRANE, ELECTRON-PARAMAGNETIC-RESONANCE, PARTIAL PROTON-TRANSFER, CLOSTRIDIUM-COCHLEARIUM, HYDROPHOBIC VITAMIN-B12, 2-METHYLENEGLUTARATE MUTASE, CRYPTIC STEREOSPECIFICITY, ESCHERICHIA-COLI}, journal = {Journal of the American Chemical Society}, doi = {10.1021/ja004246f}, volume = {123}, number = {33}, issn = {0002-7863}, title = {Interconversion of (S)-glutamate and (2S, 3S)-3-methylaspartate: A distinctive B-12-dependent carbon-skeleton rearrangement}, keyword = {METHYLMALONYL-COA MUTASE, DEPENDENT GLUTAMATE MUTASE, SYNTHETIC BILAYER-MEMBRANE, ELECTRON-PARAMAGNETIC-RESONANCE, PARTIAL PROTON-TRANSFER, CLOSTRIDIUM-COCHLEARIUM, HYDROPHOBIC VITAMIN-B12, 2-METHYLENEGLUTARATE MUTASE, CRYPTIC STEREOSPECIFICITY, ESCHERICHIA-COLI} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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