Phosphorylation of liver pyruvate kinase by Ca++ /calmodulin-dependent protein kinase: Characterization of two phosphorylation sites

Thomas R. Soderling; Charles M. Schworer; M. Raafat El-Maghrabi; Simon J. Pilkis

doi:10.1016/S0006-291X(86)80279-0

Phosphorylation of liver pyruvate kinase by Ca⁺⁺ /calmodulin-dependent protein kinase: Characterization of two phosphorylation sites

Thomas R. Soderling
, Charles M. Schworer
, M. Raafat El-Maghrabi
, Simon J. Pilkis

Physiology and Biophysics

Stony Brook University

Howard Hughes Medical Institute
Vanderbilt University

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

15 Scopus citations

Abstract

Rat liver pyruvate kinase is phosphorylated by calcium/calmodulindependent protein kinase II at serine and threonine residues in a 3-4 kDa CNBr fragment located near the amino terminus. The two sites of phosphorylation were separated by reverse-phase HPLC of a thermolysin digest. Sequence analysis established the sites of phosphorylation as follows: LeuArg-Arg-Ala-Ser(PO₄)-Val-Ala-Gln-Leu-Thr(PO₄)-Gln-Glu.

Original language	English
Pages (from-to)	1017-1023
Number of pages	7
Journal	Biochemical and Biophysical Research Communications
Volume	139
Issue number	3
DOIs	https://doi.org/10.1016/S0006-291X(86)80279-0
State	Published - Sep 30 1986

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10.1016/S0006-291X(86)80279-0

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title = "Phosphorylation of liver pyruvate kinase by Ca++ /calmodulin-dependent protein kinase: Characterization of two phosphorylation sites",

abstract = "Rat liver pyruvate kinase is phosphorylated by calcium/calmodulindependent protein kinase II at serine and threonine residues in a 3-4 kDa CNBr fragment located near the amino terminus. The two sites of phosphorylation were separated by reverse-phase HPLC of a thermolysin digest. Sequence analysis established the sites of phosphorylation as follows: LeuArg-Arg-Ala-Ser(PO4)-Val-Ala-Gln-Leu-Thr(PO4)-Gln-Glu.",

author = "Soderling, \{Thomas R.\} and Schworer, \{Charles M.\} and \{Raafat El-Maghrabi\}, M. and Pilkis, \{Simon J.\}",

year = "1986",

month = sep,

day = "30",

doi = "10.1016/S0006-291X(86)80279-0",

language = "English",

volume = "139",

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journal = "Biochemical and Biophysical Research Communications",

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Phosphorylation of liver pyruvate kinase by Ca⁺⁺ /calmodulin-dependent protein kinase: Characterization of two phosphorylation sites. / Soderling, Thomas R.; Schworer, Charles M.; Raafat El-Maghrabi, M. et al.
In: Biochemical and Biophysical Research Communications, Vol. 139, No. 3, 30.09.1986, p. 1017-1023.

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

TY - JOUR

T1 - Phosphorylation of liver pyruvate kinase by Ca++ /calmodulin-dependent protein kinase

T2 - Characterization of two phosphorylation sites

AU - Soderling, Thomas R.

AU - Schworer, Charles M.

AU - Raafat El-Maghrabi, M.

AU - Pilkis, Simon J.

PY - 1986/9/30

Y1 - 1986/9/30

N2 - Rat liver pyruvate kinase is phosphorylated by calcium/calmodulindependent protein kinase II at serine and threonine residues in a 3-4 kDa CNBr fragment located near the amino terminus. The two sites of phosphorylation were separated by reverse-phase HPLC of a thermolysin digest. Sequence analysis established the sites of phosphorylation as follows: LeuArg-Arg-Ala-Ser(PO4)-Val-Ala-Gln-Leu-Thr(PO4)-Gln-Glu.

AB - Rat liver pyruvate kinase is phosphorylated by calcium/calmodulindependent protein kinase II at serine and threonine residues in a 3-4 kDa CNBr fragment located near the amino terminus. The two sites of phosphorylation were separated by reverse-phase HPLC of a thermolysin digest. Sequence analysis established the sites of phosphorylation as follows: LeuArg-Arg-Ala-Ser(PO4)-Val-Ala-Gln-Leu-Thr(PO4)-Gln-Glu.

UR - https://www.scopus.com/pages/publications/0023037086

U2 - 10.1016/S0006-291X(86)80279-0

DO - 10.1016/S0006-291X(86)80279-0

M3 - Article

C2 - 3094523

SN - 0006-291X

VL - 139

SP - 1017

EP - 1023

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Phosphorylation of liver pyruvate kinase by Ca⁺⁺ /calmodulin-dependent protein kinase: Characterization of two phosphorylation sites

Abstract

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