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In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7.
Biochem Biophys Res Commun. 1988 Jun 16; 153(2):875-80.BB

Abstract

This report describes the in vivo phosphorylation of isocitrate lyase and examines the possible consequences to the control of the Kreb's cycle and glyoxylate bypass. NADP-specific isocitrate dehydrogenase from E. coli was the first bacterial protein whose enzymic activity was shown to be modulated by reversible phosphorylation. This enzyme has been thought to be solely responsible for the partitioning of isocitrate between the Kreb's cycle and glyoxylate bypass. No studies to date have examined the possible role of isocitrate lyase in controlling this flux.

Authors+Show Affiliations

Department of Microbiology, Arizona State University, Tempe 85287.No affiliation info available

Pub Type(s)

Journal Article
Research Support, U.S. Gov't, Non-P.H.S.

Language

eng

PubMed ID

3289540

Citation

Hoyt, J C., and H C. Reeves. "In Vivo Phosphorylation of Isocitrate Lyase From Escherichia Coli D5H3G7." Biochemical and Biophysical Research Communications, vol. 153, no. 2, 1988, pp. 875-80.
Hoyt JC, Reeves HC. In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7. Biochem Biophys Res Commun. 1988;153(2):875-80.
Hoyt, J. C., & Reeves, H. C. (1988). In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7. Biochemical and Biophysical Research Communications, 153(2), 875-80.
Hoyt JC, Reeves HC. In Vivo Phosphorylation of Isocitrate Lyase From Escherichia Coli D5H3G7. Biochem Biophys Res Commun. 1988 Jun 16;153(2):875-80. PubMed PMID: 3289540.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7. AU - Hoyt,J C, AU - Reeves,H C, PY - 1988/6/16/pubmed PY - 1988/6/16/medline PY - 1988/6/16/entrez SP - 875 EP - 80 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 153 IS - 2 N2 - This report describes the in vivo phosphorylation of isocitrate lyase and examines the possible consequences to the control of the Kreb's cycle and glyoxylate bypass. NADP-specific isocitrate dehydrogenase from E. coli was the first bacterial protein whose enzymic activity was shown to be modulated by reversible phosphorylation. This enzyme has been thought to be solely responsible for the partitioning of isocitrate between the Kreb's cycle and glyoxylate bypass. No studies to date have examined the possible role of isocitrate lyase in controlling this flux. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/3289540/In_vivo_phosphorylation_of_isocitrate_lyase_from_Escherichia_coli_D5H3G7_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(88)81177-X DB - PRIME DP - Unbound Medicine ER -