Identification of the bromopyruvate-sensitive glutamate within the active site of 2-keto-3-deoxygluconate-6-P aldolase

H. Paul Meloche, Claire T. Monti, Ruth A. Hogue-Angeletti

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Bromopyruvate inactivates 2-keto-3-deoxygluconate-6-P aldolase by a mechanism in which the reagent is incorporated by esterification. A tryptic peptide derived from inactivated enzyme has the sequence Thr-Leu-Glu*-Val-Thr-Leu-Arg. Derivatization of the γ-carboxyl of the single glutamate by bromopyruvate was confirmed by Lossen rearrangement in which the glutamate γ-ester was converted to 2,4-diamino butyrate.

Original languageEnglish (US)
Pages (from-to)589-594
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume84
Issue number3
DOIs
StatePublished - Oct 16 1978
Externally publishedYes

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Fructose-Bisphosphate Aldolase
Glutamic Acid
Catalytic Domain
Butyrates
Esterification
Esters
Peptides
Enzymes
bromopyruvate
2-keto-3-deoxygluconate

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification of the bromopyruvate-sensitive glutamate within the active site of 2-keto-3-deoxygluconate-6-P aldolase. / Meloche, H. Paul; Monti, Claire T.; Hogue-Angeletti, Ruth A.

In: Biochemical and Biophysical Research Communications, Vol. 84, No. 3, 16.10.1978, p. 589-594.

Research output: Contribution to journalArticle

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