Stereochemical Course of Thiophosphoryl Group Transfer Catalyzed by Mitochondrial Phosphoenolpyruvate Carboxykinase

Kwan Fu Sheu; Paul Markovitz; Merton F. Utter; Lynn D. Nolan; John P. Richard; Hsu Tso Ho; Perry A. Frey

doi:10.1021/bi00303a030

Stereochemical Course of Thiophosphoryl Group Transfer Catalyzed by Mitochondrial Phosphoenolpyruvate Carboxykinase

Kwan Fu Sheu
, Paul Markovitz
, Merton F. Utter
, Lynn D. Nolan
, John P. Richard
, Hsu Tso Ho
, Perry A. Frey

Chemistry

Case Western Reserve University
Ohio State University
University of Wisconsin-Madison
The Burke Medical Research Institute

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

Abstract

Guinea pig liver mitochondrial phosphoenolpyruvate carboxykinase catalyzes the conversion of (R_p)-guanosine 5’ -(3-thio[3-¹⁸O]triphosphate) and oxalacetate to (S_p)-[¹⁸O]thiophosphoenolpyruvate, GDP, and CO₂ by a mechanism that involves overall inversion in the configuration of the chiral [¹⁸O]thiophosphate group. This result is most consistent with a single displacement mechanism in which the [¹⁸O] thiophosphoryl group is transferred from (R_p)-guanosine 5′-(3-thio[3-¹⁸O]triphosphate) bound at the active site directly to enolpyruvate generated at the active site by the decarboxylation of oxalacetate. In particular, this result does not indicate the involvement of a covalent thiophosphoryl-enzyme on the reaction pathway.

Original language	English
Pages (from-to)	1779-1783
Number of pages	5
Journal	Biochemistry
Volume	23
Issue number	8
DOIs	https://doi.org/10.1021/bi00303a030
State	Published - Apr 1984

Access to Document

10.1021/bi00303a030

Cite this

@article{8f55f747522b4f18910a8d6810337668,

title = "Stereochemical Course of Thiophosphoryl Group Transfer Catalyzed by Mitochondrial Phosphoenolpyruvate Carboxykinase",

abstract = "Guinea pig liver mitochondrial phosphoenolpyruvate carboxykinase catalyzes the conversion of (Rp)-guanosine 5{\textquoteright} -(3-thio[3-18O]triphosphate) and oxalacetate to (Sp)-[18O]thiophosphoenolpyruvate, GDP, and CO2 by a mechanism that involves overall inversion in the configuration of the chiral [18O]thiophosphate group. This result is most consistent with a single displacement mechanism in which the [18O] thiophosphoryl group is transferred from (Rp)-guanosine 5′-(3-thio[3-18O]triphosphate) bound at the active site directly to enolpyruvate generated at the active site by the decarboxylation of oxalacetate. In particular, this result does not indicate the involvement of a covalent thiophosphoryl-enzyme on the reaction pathway.",

author = "Sheu, \{Kwan Fu\} and Paul Markovitz and Utter, \{Merton F.\} and Nolan, \{Lynn D.\} and Richard, \{John P.\} and Ho, \{Hsu Tso\} and Frey, \{Perry A.\}",

year = "1984",

month = apr,

doi = "10.1021/bi00303a030",

language = "English",

volume = "23",

pages = "1779--1783",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "8",

}

TY - JOUR

T1 - Stereochemical Course of Thiophosphoryl Group Transfer Catalyzed by Mitochondrial Phosphoenolpyruvate Carboxykinase

AU - Sheu, Kwan Fu

AU - Markovitz, Paul

AU - Utter, Merton F.

AU - Nolan, Lynn D.

AU - Richard, John P.

AU - Ho, Hsu Tso

AU - Frey, Perry A.

PY - 1984/4

Y1 - 1984/4

N2 - Guinea pig liver mitochondrial phosphoenolpyruvate carboxykinase catalyzes the conversion of (Rp)-guanosine 5’ -(3-thio[3-18O]triphosphate) and oxalacetate to (Sp)-[18O]thiophosphoenolpyruvate, GDP, and CO2 by a mechanism that involves overall inversion in the configuration of the chiral [18O]thiophosphate group. This result is most consistent with a single displacement mechanism in which the [18O] thiophosphoryl group is transferred from (Rp)-guanosine 5′-(3-thio[3-18O]triphosphate) bound at the active site directly to enolpyruvate generated at the active site by the decarboxylation of oxalacetate. In particular, this result does not indicate the involvement of a covalent thiophosphoryl-enzyme on the reaction pathway.

AB - Guinea pig liver mitochondrial phosphoenolpyruvate carboxykinase catalyzes the conversion of (Rp)-guanosine 5’ -(3-thio[3-18O]triphosphate) and oxalacetate to (Sp)-[18O]thiophosphoenolpyruvate, GDP, and CO2 by a mechanism that involves overall inversion in the configuration of the chiral [18O]thiophosphate group. This result is most consistent with a single displacement mechanism in which the [18O] thiophosphoryl group is transferred from (Rp)-guanosine 5′-(3-thio[3-18O]triphosphate) bound at the active site directly to enolpyruvate generated at the active site by the decarboxylation of oxalacetate. In particular, this result does not indicate the involvement of a covalent thiophosphoryl-enzyme on the reaction pathway.

UR - https://www.scopus.com/pages/publications/0021759420

U2 - 10.1021/bi00303a030

DO - 10.1021/bi00303a030

M3 - Article

C2 - 6372862

AN - SCOPUS:0021759420

SN - 0006-2960

VL - 23

SP - 1779

EP - 1783

JO - Biochemistry

JF - Biochemistry

IS - 8

ER -

Stereochemical Course of Thiophosphoryl Group Transfer Catalyzed by Mitochondrial Phosphoenolpyruvate Carboxykinase

Abstract

Access to Document

Other files and links

Fingerprint

Cite this