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

doi:10.1016/0006-291X(78)90746-5

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 journal › Article › peer-review

10 Scopus citations

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 language	English (US)
Pages (from-to)	589-594
Number of pages	6
Journal	Biochemical and Biophysical Research Communications
Volume	84
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(78)90746-5
State	Published - Oct 16 1978
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

Access to Document

10.1016/0006-291X(78)90746-5

Cite this

@article{f0cc84b5eeea4cc787896188ade4eed2,

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

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.",

author = "Meloche, {H. Paul} and Monti, {Claire T.} and Hogue-Angeletti, {Ruth A.}",

year = "1978",

month = oct,

day = "16",

doi = "10.1016/0006-291X(78)90746-5",

language = "English (US)",

volume = "84",

pages = "589--594",

journal = "Biochemical and Biophysical Research Communications",

issn = "0006-291X",

publisher = "Academic Press Inc.",

number = "3",

}

TY - JOUR

T1 - Identification of the bromopyruvate-sensitive glutamate within the active site of 2-keto-3-deoxygluconate-6-P aldolase

AU - Meloche, H. Paul

AU - Monti, Claire T.

AU - Hogue-Angeletti, Ruth A.

PY - 1978/10/16

Y1 - 1978/10/16

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0018167677&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018167677&partnerID=8YFLogxK

U2 - 10.1016/0006-291X(78)90746-5

DO - 10.1016/0006-291X(78)90746-5

M3 - Article

C2 - 718702

AN - SCOPUS:0018167677

SN - 0006-291X

VL - 84

SP - 589

EP - 594

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

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

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this