| Literature DB >> 11006546 |
T J Kappock1, S E Ealick, J Stubbe.
Abstract
Structural studies, sequence alignments, and biochemistry have provided new insights into the evolution of the purine biosynthetic pathway. The importance of chemistry, the binding of ribose 5-phosphate (common to all purine biosynthetic intermediates), and transient protein-protein interactions in channeling of chemically unstable intermediates have all been examined in the past few years.Entities:
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Year: 2000 PMID: 11006546 DOI: 10.1016/s1367-5931(00)00133-2
Source DB: PubMed Journal: Curr Opin Chem Biol ISSN: 1367-5931 Impact factor: 8.822