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August 1, 1986Journal of Biological ChemistryOpen Access

Amino acid sequence of the pyruvate and the glyoxylate active-site lysine peptide of Escherichia coli 2-keto-4-hydroxyglutarate aldolase.

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Authors

CVChris J. VlahosBrigham and Women's HospitalEDEugene E. DekkerUniversity of Michigan

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Vlahos et al. (1986) studied this question.

synapsesocial.com/papers/6a8293dcd7a462ab0d8ad832https://doi.org/10.1016/s0021-9258(18)67346-6
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Also Consider

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  1. 1<b>On the Mechanism of the Enzymatic Decarboxylation of Acetoacetate. II</b>1962 · 89 citations
  2. 2Complete primary structure of 2-keto-3-deoxy-6-phosphogluconate aldolase.1980 · 28 citations
  3. 3Physical and chemical evidence for the trimeric subunit structure of 2-keto-4-hydroxyglutarate aldolase from Escherichia coli K-12.1981 · 16 citations
  4. 4Structure of 2-Keto-3-deoxy-6-phosphogluconate Aldolase1971 · 65 citations
  5. 5Malyl-CoA formation in the NAD-, CoASH-, and alpha-ketoglutarate dehydrogenase-dependent oxidation of 2-keto-4-hydroxyglutarate. Possible coupled role of this reaction with 2-keto-4-hydroxyglutarate aldolase activity in a pyruvate-catalyzed cyclic oxidation of glyoxylate.1984 · 27 citations