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May 1, 2000Journal of Biological ChemistryOpen Access

Specificity Determinants for the Pyruvate Dehydrogenase Component Reaction Mapped with Mutated and Prosthetic Group Modified Lipoyl Domains

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Authors

XGXiaoming GongShanghai Customs CollegeTPTao PengKunming University of Science and TechnologyAYAlexander V. YakhninNational Cancer Institute

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Gong et al. (2000) studied this question.

synapsesocial.com/papers/6a826f3a70df46ce3ea215eehttps://doi.org/10.1074/jbc.275.18.13645
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Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Crystallographic analysis of substrate binding and catalysis in dihydrolipoyl transacetylase (E2p)1993 · 77 citations
  2. 2Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase multienzyme complexes1989 · 77 citations
  3. 3The Pyruvate Dehydrogenase Complex of Escherichia coli K121983 · 128 citations
  4. 4Kinetics and specificity of reductive acylation of wild‐type and mutated lipoyl domains of 2‐oxo‐acid dehydrogenase complexes from Azotobacter vinelandii1998 · 49 citations
  5. 5Sizing of bovine heart and kidney pyruvate dehydrogenase complex and dihydrolipoyl transacetylase core by quasielastic light scattering1993 · 15 citations